微生物β-1，3-葡聚糖的强化合成及最小功能单元挖掘
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摘要
本论文以一株产β-1,3-葡聚糖(热凝胶)工业化生产菌株农杆菌ATCC 31749(Agrobacterium sp. ATCC 31749)为研究模型,从提升β-1,3-葡聚糖的生产效率入手,采用比较基因组学技术构建了电子传递链及β-1,3-葡聚糖合成相关的代谢途径,运用定量PCR(qRT-PCR)、和胞内核苷酸分析考察了不同溶氧(DO)条件下β-1,3-葡聚糖合成相关基因的RNA转录丰度变化,从而阐明溶氧影响Agrobacterium sp. ATCC 31749基因转录水平、碳代谢流以及其适应外界环境的生理机制,在此基础上,提出并验证了用于强化β-1,3-葡聚糖生物合成的二阶段溶氧和pH控制的策略。对不同糖苷键连接的葡聚糖进行水解,构建了包括β-1,3-葡聚寡糖在内的具有多种构型的葡聚寡糖糖库,并合成拟糖脂和制备寡糖糖芯片,借助糖芯片技术研究了糖与免疫系统信号蛋白之间的作用关系,挖掘出能够被信号蛋白识别的最小葡聚寡糖单元,探索功能糖-免疫信号蛋白之间的构效关系规律,为以免疫信号蛋白为靶点的高效功能糖单元的筛选和设计提供实验基础、理论依据与新思路,为基于代谢工程手段的功能糖生物合成提供改进方向。主要研究结果如下:
1)构建了Agrobacterium sp. ATCC 31749的电子呼吸链和β-1,3-葡聚糖(热凝胶)合成代谢途径。在Agrobacterium sp. ATCC 31749全基因组还没有测序的情况下,通过设计兼并引物和定量PCR技术,获得假定的NADH氧化还原酶、琥珀酸脱氢酶、辅酶Q生物合成蛋白、细胞色素d末端氧化酶、细胞色素bo末端氧化酶、细胞色素cbb3-型氧化酶、细胞色素caa3-型氧化酶和苹果酸脱氢酶基因序列,将获得的基因序列与NCBI数据库中基因信息进行比对分析,完成了对所获得基因的解析,在鉴定假定基因与预期完全一致的基础上构建Agrobacterium sp. ATCC 31749电子传递链网络。进一步从基因组水平对获得的基因序列与已测序的4种Agrobacterium属菌株之间进行比对,发现了所有检测基因仅与Agrobacterium tumefaciens C58中的对应基因有98%以上的高度近似性,这表明Agrobacterium sp. ATCC 31749与Agrobacterium tumefaciens C58基因组具有高度相似性,基于此结论,采用比较基因组学构建了热β-1,3-葡聚糖(热凝胶)合成代谢途径。
2)溶氧可以调控胞内与β-1,3-葡聚糖(热凝胶)合成相关基因的转录水平。借助qRT-PCR技术解析DO水平与β-1,3-葡聚糖(热凝胶)合成相关基因的mRNA丰度之间的相关关系。不同DO水平下与热凝胶合成相关的基因(①葡萄糖用于热凝胶合成与细胞壁多糖合成的基因;②TCA循环途径中酶的基因;③电子传递链中蛋白的基因)的转录水平分析表明,所考察基因的转录水平随溶氧的增加而增强,DO在50%时所考察基因的转录水平最高,细胞内cyoA、catD、fixN、icd、sdh B、mdh、glmM和galU基因的转录水平是低溶氧条件下(5%)的3-6倍。
3)溶氧通过调整胞内的核苷酸水平来调整碳代谢流,强化β-1,3-葡聚糖(热凝胶)的合成。在通过溶氧来控制β-1,3-葡聚糖(热凝胶)发酵过程的基础上,系统地研究了溶氧变化对β-1,3-葡聚糖(热凝胶)合成及其相关前体核苷酸物质丰度的影响,阐明了溶氧水平对改变碳代谢流分布和加快糖代谢流用于β-1,3-葡聚糖(热凝胶)合成的分子机制。与低溶氧条件相比(15% DO),高溶氧条件下细胞内AMP、UMP、UDP-葡萄糖、NADH、UTP分别是低溶氧条件下的1.4、7.9、4、3和1.5倍;与5%溶氧相比,在45%和60%溶氧浓度下,底物比消耗速率和热凝胶比合成速率增幅均超过2倍。
4)提出并验证了用于强化β-1, 3-葡聚糖(热凝胶)合成的二阶段溶氧与pH控制发酵策略。在热凝胶生产过程中用两阶段溶氧调控策略(20 h到50 h溶氧为60%,pH 5.6;51 h到120 h,溶氧为40%,pH 5.6)可以提高葡萄糖消耗速率和热凝胶合成速率,使热凝胶产量达到42.8 g/L。与恒定转速控制发酵相比,热凝胶的产量、生产强度、底物转化率分别提高28%,30%和20%。这一结果表明二阶段溶氧与pH控制策略可以有效地加速碳源的消耗,增强碳代谢流用于热凝胶的合成。
5)基于糖芯片技术,确认了与免疫系统功能蛋白Dectin-1和DC-SIGN结合的葡聚寡糖最小功能单元,探索了不同结构葡聚寡糖与功能蛋白间的识别及构效关系。对来自源不同微生物的寡糖和多糖进行部分水解,获得了一系列不同糖苷链连接的寡糖分子,用质谱与核磁技术对寡糖分子的结构进行解析,合成了拟糖脂探针,并用于制备糖芯片。寡糖的二级质谱谱图表明:对于不同糖苷键连接的葡聚寡糖,其ES-CID-MS/MS具有不同的断裂方式;而对于相同糖苷键连接的葡聚寡糖,其单糖指纹图谱具有特定特征,即1,2-连接的寡糖,其单离子峰的碎片峰规律是:0,4A, B和C型离子峰在每一个寡糖单元内均全部出现,相邻峰C型离子峰间具有相同的差值规律(102, 42, 18),而1,3-连接的寡糖仅仅出现了C型离子峰。功能蛋白Dectin-1特异识别主链聚合度大于10的β-1,3-葡聚寡糖。功能蛋白DC-SIGN广泛识别来自于细菌与真菌的葡聚寡糖,尤其对主链为β-1,3-四糖在1和3位有β-1,6-分支的β-1,3-葡聚寡糖具有极高的识别能力。本研究只是初步表明DC-SIGN可以和β-1,3-葡聚寡糖作用,目前在Feizi ,针对DC-SIGN和β-1,3-葡聚寡糖识别的特异性如何?以及DC-SIGN和其他寡糖探针的作用强度如何等问题正在进一步的分析研究。以上结果为以Dectin-1和DC-SIGN为靶标的β-1,3-葡聚寡糖(热凝胶寡糖)的功能开发提供了方向。
This dissertation selected Agrobacterium sp. strain, ATCC 31749 as a model system to explore an efficient fermentation strategy for the production ofβ-1,3-glucan (curdlan). There has been very limited genomic information on the Agrobacterium sp. ATCC 31749. The ETCs (Electron Transfer Chains) and metabolic network were constructed based on the comparative genomic method. The effects of DO (dissolved oxygen) gradients on the metabolic characteristics, gene expression profiles of Agrobacterium sp. were studied. Based on these results, an efficient curdlan production process (two-stage DO combined with pH control) was developed. In the second part of the Thesis (described in Chapter 5) a library of glucan oligosaccharides, obtained from various types of glucans after their partial depolymerization, was constructed. These oligosaccharides were converted into neoglycolipid (NGL) probes for generating glucan oligosaccharide microarrays. Microarray binding experiments were then carried out with two proteins the human immune system to determine the specificities of the interactions, including the minimum chain length and glucose linkage requirement for oligosaccharides.
The main results were described as follows:
1) With the PCR and gene sequence methodology, ten genes sequences of Agrobacterium sp. ATCC 31749 were acquired and analysis as well as the genomic specificity identification between Agrobacterium sp. ATCC 31749 and other 1000 bacterial genomes were undertaken. As the genome sequence of Agrobacterium sp. ATCC 31749 was not available when this work was undertaken, the primers were designed based on the highly conservative region of the same gene from different bacteria. The DNA fragments acquired by PCR were sequenced. On that basis, the sequences of eleven gene fragments from Agrobacterium sp. ATCC 31749 were determined. These sequences were highly consistent with that from previous reports. The eleven genes from Agrobacterium sp. ATCC 31749 and the genes from other four Agrobacterium which is sequenced successfully were compared on the basis of homology. The genome of Agrobacterium sp. ATCC 31749 is highly consistent with the genome of Agrobacterium tumefaciens C58 at 100% value. The respiration chain and metabolic network in Agrobacterium sp. ATCC 31749 was constructed base on these in Agrobacterium tumefaciens C58.
2) To determine the mechanism of DO modulation of mRNA translation, the effect of DO gradients on the expression of genes related to the ETCs, TCA cycle and curdlan synthesis in Agrobacterium sp. ATCC 31749 were investigated under nitrogen limited condition using qRT-PCR. The transcriptional levels of the genes governing TCA cycle (icd, sdh B and mdh), curdlan synthesis (glm M and gal U) and ETC system (cyo A, cat D and fix N) increased concomitantly with the elevation of DO. Whereas, the transcriptional level of cytochrome d (cyd A) exposed to different DO was changed slightly. At 50% DO level, the mRNAs of cyo A, cat D, fix N, icd, sdh B, mdh, glm M and gal U were 3-6 times higher than those under other DO conditions studied. The results suggested that DO can apparently affect the translational levels of the genes particularly related to the metabolic network of glucose and ATP regeneration have similar modulation profile under 50% DO.
3) Based on the fermentation technology with DO control, the effect of DO gradients combined with pH on curdlan yield, intracellular nucleotide levels and glucose conversion efficiency into curdlan, and understanding of the mechanism of change of DO and the glucose metabolic network distribution to enhance the glucose metabolic flux for curdlan biosynthesis. The intracellular AMP, UMP, UDP-glucose, NADH and UTP at 60% DO is 1.4, 7.9, 4, 3, and 1.5-times, respectively, under 15% DO. The curdlan yield improved with the elevation of DO. The highest curdlan yield was 43 g/L under 60% DO which was 2.85 times higher than that of 5% DO condition (15 g/L).
4) The DO concentration had apparent effect on curdlan production through enhancement of mRNA translational levels and intracellular nucleotide levels. Baseed on these results, a two-stage curdlan fermentation process has been developed and verified. The more optimal DO for curdlan production was between 45% and 60 %. The two-stage DO combine with pH (0-20 h, the pH was 7.0 after 20 h, the pH was controlled at 5.6; for DO levels, from 20 h to 50 h, 60% DO was suitable, thereafter 40% DO) was used. The resulting curdlan yield, curdlan productivity and glucose conversion efficiency into curdlan were improved by 28%, 30% and 20%, respectively.
5) Series of gluco-oligosaccharide neoglycolipid (NGL) probes from 2mer to 13mer, includingβ-1,3,α-1,4,β-1,4,α-1,6 andβ-1,6-linkage, have been prepared in Prof. Ten Feizi’s laboratory. To complement currently available gluco-oligosaccharides and have a comprehensive series of the for microarray analysis,α-1,2-glucofructosides, cyclicβ-1,2-glucan,α-1,3-glucan and lentinan (β-1,3/β-1,6-branched glucan) were partially depolymerized by acid hydrolysis and fractionated by gel-filtration chromatography. Mass spectrometry and NMR were used for linkage and sequence analyses of the oligosaccharide fractions. Electrospray tandem mass spectrometry analysis of all the gluco-heptasaccharides revealed that different linkage-types produced different characteristic fragmentation. Howeverαorβanomeric configuration does not affect the fragmentation behaviour. Theαandβconfigurations can be readily assigned by 1H-NMR. In this way, all the oligosaccharide sequences were determined. NGL probes ( a total of 63 probes) were then synthesized from oligosaccharides obtained from different glucans before construction of glucan oligosaccharide microarrays. The microarrays were applied to analyze the linkage specificities and the minimum oligosaccharide chain lengths recognized by several recombinant proteins of the immune system, among them are Dectin-1 and DC-SIGN. As predicted Dectin-1 specifically bound toβ-1,3-gluco-oligosaccharides, and did not bind to any of theα-1,2-,α-1,3-,α-1,4-,α-1,6-,β-1,2-,β-1,4-,β-1,6-,β-1,3-β-1,4-gluco-oligosaccharides. The interactions of Dectin-1 with branched gluco-oligosaccharides, in particular those withβ-1,3/β1,6-linkages require further investigation. A particularly potent preparation of DC-SIGN was found to bind to gluco-oligosaccharides derived from bacteria, fungi or plants. The binding of DC-SIGN to gluco-oligosaccharides is a novel finding. Further investigation is ongoing in the Feizi laboratory to define the fine specificity, including the glucosyl linkage preference of DC-SIGN and the binding strength to gluco-oligosaccharides compared with other known DC-SIGN carbohydrate ligands. The results indicated that the position and frequency ofβ-1,6-branch play an important role for DC-SIGN interaction with gluco-oligosaccharides.
1)构建了Agrobacterium sp. ATCC 31749的电子呼吸链和β-1,3-葡聚糖(热凝胶)合成代谢途径。在Agrobacterium sp. ATCC 31749全基因组还没有测序的情况下,通过设计兼并引物和定量PCR技术,获得假定的NADH氧化还原酶、琥珀酸脱氢酶、辅酶Q生物合成蛋白、细胞色素d末端氧化酶、细胞色素bo末端氧化酶、细胞色素cbb3-型氧化酶、细胞色素caa3-型氧化酶和苹果酸脱氢酶基因序列,将获得的基因序列与NCBI数据库中基因信息进行比对分析,完成了对所获得基因的解析,在鉴定假定基因与预期完全一致的基础上构建Agrobacterium sp. ATCC 31749电子传递链网络。进一步从基因组水平对获得的基因序列与已测序的4种Agrobacterium属菌株之间进行比对,发现了所有检测基因仅与Agrobacterium tumefaciens C58中的对应基因有98%以上的高度近似性,这表明Agrobacterium sp. ATCC 31749与Agrobacterium tumefaciens C58基因组具有高度相似性,基于此结论,采用比较基因组学构建了热β-1,3-葡聚糖(热凝胶)合成代谢途径。
2)溶氧可以调控胞内与β-1,3-葡聚糖(热凝胶)合成相关基因的转录水平。借助qRT-PCR技术解析DO水平与β-1,3-葡聚糖(热凝胶)合成相关基因的mRNA丰度之间的相关关系。不同DO水平下与热凝胶合成相关的基因(①葡萄糖用于热凝胶合成与细胞壁多糖合成的基因;②TCA循环途径中酶的基因;③电子传递链中蛋白的基因)的转录水平分析表明,所考察基因的转录水平随溶氧的增加而增强,DO在50%时所考察基因的转录水平最高,细胞内cyoA、catD、fixN、icd、sdh B、mdh、glmM和galU基因的转录水平是低溶氧条件下(5%)的3-6倍。
3)溶氧通过调整胞内的核苷酸水平来调整碳代谢流,强化β-1,3-葡聚糖(热凝胶)的合成。在通过溶氧来控制β-1,3-葡聚糖(热凝胶)发酵过程的基础上,系统地研究了溶氧变化对β-1,3-葡聚糖(热凝胶)合成及其相关前体核苷酸物质丰度的影响,阐明了溶氧水平对改变碳代谢流分布和加快糖代谢流用于β-1,3-葡聚糖(热凝胶)合成的分子机制。与低溶氧条件相比(15% DO),高溶氧条件下细胞内AMP、UMP、UDP-葡萄糖、NADH、UTP分别是低溶氧条件下的1.4、7.9、4、3和1.5倍;与5%溶氧相比,在45%和60%溶氧浓度下,底物比消耗速率和热凝胶比合成速率增幅均超过2倍。
4)提出并验证了用于强化β-1, 3-葡聚糖(热凝胶)合成的二阶段溶氧与pH控制发酵策略。在热凝胶生产过程中用两阶段溶氧调控策略(20 h到50 h溶氧为60%,pH 5.6;51 h到120 h,溶氧为40%,pH 5.6)可以提高葡萄糖消耗速率和热凝胶合成速率,使热凝胶产量达到42.8 g/L。与恒定转速控制发酵相比,热凝胶的产量、生产强度、底物转化率分别提高28%,30%和20%。这一结果表明二阶段溶氧与pH控制策略可以有效地加速碳源的消耗,增强碳代谢流用于热凝胶的合成。
5)基于糖芯片技术,确认了与免疫系统功能蛋白Dectin-1和DC-SIGN结合的葡聚寡糖最小功能单元,探索了不同结构葡聚寡糖与功能蛋白间的识别及构效关系。对来自源不同微生物的寡糖和多糖进行部分水解,获得了一系列不同糖苷链连接的寡糖分子,用质谱与核磁技术对寡糖分子的结构进行解析,合成了拟糖脂探针,并用于制备糖芯片。寡糖的二级质谱谱图表明:对于不同糖苷键连接的葡聚寡糖,其ES-CID-MS/MS具有不同的断裂方式;而对于相同糖苷键连接的葡聚寡糖,其单糖指纹图谱具有特定特征,即1,2-连接的寡糖,其单离子峰的碎片峰规律是:0,4A, B和C型离子峰在每一个寡糖单元内均全部出现,相邻峰C型离子峰间具有相同的差值规律(102, 42, 18),而1,3-连接的寡糖仅仅出现了C型离子峰。功能蛋白Dectin-1特异识别主链聚合度大于10的β-1,3-葡聚寡糖。功能蛋白DC-SIGN广泛识别来自于细菌与真菌的葡聚寡糖,尤其对主链为β-1,3-四糖在1和3位有β-1,6-分支的β-1,3-葡聚寡糖具有极高的识别能力。本研究只是初步表明DC-SIGN可以和β-1,3-葡聚寡糖作用,目前在Feizi ,针对DC-SIGN和β-1,3-葡聚寡糖识别的特异性如何?以及DC-SIGN和其他寡糖探针的作用强度如何等问题正在进一步的分析研究。以上结果为以Dectin-1和DC-SIGN为靶标的β-1,3-葡聚寡糖(热凝胶寡糖)的功能开发提供了方向。
This dissertation selected Agrobacterium sp. strain, ATCC 31749 as a model system to explore an efficient fermentation strategy for the production ofβ-1,3-glucan (curdlan). There has been very limited genomic information on the Agrobacterium sp. ATCC 31749. The ETCs (Electron Transfer Chains) and metabolic network were constructed based on the comparative genomic method. The effects of DO (dissolved oxygen) gradients on the metabolic characteristics, gene expression profiles of Agrobacterium sp. were studied. Based on these results, an efficient curdlan production process (two-stage DO combined with pH control) was developed. In the second part of the Thesis (described in Chapter 5) a library of glucan oligosaccharides, obtained from various types of glucans after their partial depolymerization, was constructed. These oligosaccharides were converted into neoglycolipid (NGL) probes for generating glucan oligosaccharide microarrays. Microarray binding experiments were then carried out with two proteins the human immune system to determine the specificities of the interactions, including the minimum chain length and glucose linkage requirement for oligosaccharides.
The main results were described as follows:
1) With the PCR and gene sequence methodology, ten genes sequences of Agrobacterium sp. ATCC 31749 were acquired and analysis as well as the genomic specificity identification between Agrobacterium sp. ATCC 31749 and other 1000 bacterial genomes were undertaken. As the genome sequence of Agrobacterium sp. ATCC 31749 was not available when this work was undertaken, the primers were designed based on the highly conservative region of the same gene from different bacteria. The DNA fragments acquired by PCR were sequenced. On that basis, the sequences of eleven gene fragments from Agrobacterium sp. ATCC 31749 were determined. These sequences were highly consistent with that from previous reports. The eleven genes from Agrobacterium sp. ATCC 31749 and the genes from other four Agrobacterium which is sequenced successfully were compared on the basis of homology. The genome of Agrobacterium sp. ATCC 31749 is highly consistent with the genome of Agrobacterium tumefaciens C58 at 100% value. The respiration chain and metabolic network in Agrobacterium sp. ATCC 31749 was constructed base on these in Agrobacterium tumefaciens C58.
2) To determine the mechanism of DO modulation of mRNA translation, the effect of DO gradients on the expression of genes related to the ETCs, TCA cycle and curdlan synthesis in Agrobacterium sp. ATCC 31749 were investigated under nitrogen limited condition using qRT-PCR. The transcriptional levels of the genes governing TCA cycle (icd, sdh B and mdh), curdlan synthesis (glm M and gal U) and ETC system (cyo A, cat D and fix N) increased concomitantly with the elevation of DO. Whereas, the transcriptional level of cytochrome d (cyd A) exposed to different DO was changed slightly. At 50% DO level, the mRNAs of cyo A, cat D, fix N, icd, sdh B, mdh, glm M and gal U were 3-6 times higher than those under other DO conditions studied. The results suggested that DO can apparently affect the translational levels of the genes particularly related to the metabolic network of glucose and ATP regeneration have similar modulation profile under 50% DO.
3) Based on the fermentation technology with DO control, the effect of DO gradients combined with pH on curdlan yield, intracellular nucleotide levels and glucose conversion efficiency into curdlan, and understanding of the mechanism of change of DO and the glucose metabolic network distribution to enhance the glucose metabolic flux for curdlan biosynthesis. The intracellular AMP, UMP, UDP-glucose, NADH and UTP at 60% DO is 1.4, 7.9, 4, 3, and 1.5-times, respectively, under 15% DO. The curdlan yield improved with the elevation of DO. The highest curdlan yield was 43 g/L under 60% DO which was 2.85 times higher than that of 5% DO condition (15 g/L).
4) The DO concentration had apparent effect on curdlan production through enhancement of mRNA translational levels and intracellular nucleotide levels. Baseed on these results, a two-stage curdlan fermentation process has been developed and verified. The more optimal DO for curdlan production was between 45% and 60 %. The two-stage DO combine with pH (0-20 h, the pH was 7.0 after 20 h, the pH was controlled at 5.6; for DO levels, from 20 h to 50 h, 60% DO was suitable, thereafter 40% DO) was used. The resulting curdlan yield, curdlan productivity and glucose conversion efficiency into curdlan were improved by 28%, 30% and 20%, respectively.
5) Series of gluco-oligosaccharide neoglycolipid (NGL) probes from 2mer to 13mer, includingβ-1,3,α-1,4,β-1,4,α-1,6 andβ-1,6-linkage, have been prepared in Prof. Ten Feizi’s laboratory. To complement currently available gluco-oligosaccharides and have a comprehensive series of the for microarray analysis,α-1,2-glucofructosides, cyclicβ-1,2-glucan,α-1,3-glucan and lentinan (β-1,3/β-1,6-branched glucan) were partially depolymerized by acid hydrolysis and fractionated by gel-filtration chromatography. Mass spectrometry and NMR were used for linkage and sequence analyses of the oligosaccharide fractions. Electrospray tandem mass spectrometry analysis of all the gluco-heptasaccharides revealed that different linkage-types produced different characteristic fragmentation. Howeverαorβanomeric configuration does not affect the fragmentation behaviour. Theαandβconfigurations can be readily assigned by 1H-NMR. In this way, all the oligosaccharide sequences were determined. NGL probes ( a total of 63 probes) were then synthesized from oligosaccharides obtained from different glucans before construction of glucan oligosaccharide microarrays. The microarrays were applied to analyze the linkage specificities and the minimum oligosaccharide chain lengths recognized by several recombinant proteins of the immune system, among them are Dectin-1 and DC-SIGN. As predicted Dectin-1 specifically bound toβ-1,3-gluco-oligosaccharides, and did not bind to any of theα-1,2-,α-1,3-,α-1,4-,α-1,6-,β-1,2-,β-1,4-,β-1,6-,β-1,3-β-1,4-gluco-oligosaccharides. The interactions of Dectin-1 with branched gluco-oligosaccharides, in particular those withβ-1,3/β1,6-linkages require further investigation. A particularly potent preparation of DC-SIGN was found to bind to gluco-oligosaccharides derived from bacteria, fungi or plants. The binding of DC-SIGN to gluco-oligosaccharides is a novel finding. Further investigation is ongoing in the Feizi laboratory to define the fine specificity, including the glucosyl linkage preference of DC-SIGN and the binding strength to gluco-oligosaccharides compared with other known DC-SIGN carbohydrate ligands. The results indicated that the position and frequency ofβ-1,6-branch play an important role for DC-SIGN interaction with gluco-oligosaccharides.
引文
[1] Saraswat-Ohri S, Vashishta A, Vetvicka V, et al. Biological properties ofβ-1,3-D-glucan-based synthetic oligosaccharides [J]. J Med Food, 2011, 14: 369-376.
[2] Descroix K, Vetvicka V, Laurent I, et al. New oligo-β-1,3-glucan derivatives as immunostimulating agents [J]. Bioorg Med Chem, 2010, 18: 348-357.
[3] Ruiz-Herrera J. Biosynthesis ofβ-glucans in fungi [J]. Antonie Van Leeuwenhoek, 1991, 60: 72-81.
[4] Yiannikouris A, Francois J, Poughon L, et al. Alkali extraction ofβ-D-glucans from Saccharomyces cerevisiae cell wall and study of their adsorptive properties toward zearalenone [J]. J Agric Food Chem, 2004, 52: 3666-3673.
[5] Masuoka J. Surface glycans of Candida albicans and other pathogenic fungi: physiological roles, clinical uses, and experimental challenges [J]. Clin Microbiol Rev, 2004, 17: 281-310.
[6] Kondori N, Edebo L, Mattsby-Baltzer I. A novel monoclonal antibody recognizingβ-1,3-glucans in intact cells of Candida and Cryptococcus [J]. APMIS, 2008, 116: 867-876.
[7] Ishibashi K, Yoshida M, Nakabayashi I, et al. Role of anti-beta-glucan antibody in host defense against fungi [J]. FEMS Immunol Med Microbiol, 2005, 44: 99-109.
[8] Torosantucci A, Chiani P, Bromuro C, et al. Protection by anti-beta-glucan antibodies is associated with restrictedβ-1,3 glucan binding specificity and inhibition of fungal growth and adherence [J]. PLoS One, 2009, 4(4): e5392.
[9] Taylor P R, Tsoni S V, Willment J A, et al. Dectin-1 is required forβ-glucan recognition and control of fungal infection [J]. Nat Immunol, 2007, 8: 31-38.
[10] Berner V K, Sura M E, Hunter K W J. Conjugation of protein antigen to microparticulate beta-glucan from Saccharomyces cerevisiae: a new adjuvant for intradermal and oral immunizations [J]. Appl Microbiol Biotechnol, 2008, 80: 1053-1061.
[11] Kimura Y, Sumiyoshi M, Suzuki T, et al. Antitumor and antimetastatic activity of a novel water-soluble low molecular weightβ-1,3-D-glucan (branchβ-1,6) isolated from Aureobasidium pullulans 1A1 strain black yeast [J]. Anticancer Res, 2006, 26: 4131-4141.
[12] Berner M D, Sura M E, Alves B N, et al. IFN-gamma primes macrophages for enhanced TNF-αexpression in response to stimulatory and non-stimulatory amounts of microparticulateβ-glucan [J]. Immunol Lett, 2005, 98: 115-122.
[13] Chan G C, Chan W K, Sze D M. The effects ofβ-glucan on human immune and cancer cells [J]. J Hematol Oncol, 2009, 2:p 25.
[14] Vandamme E J, De Baets S, Steinbüchel A. Polysaccharides I: Polysaccharides of Prokaryotes [M]. Weiheim Wiley VCH, 2004: 237-298.
[15] Mortensen N C. Composition comprisingβ-1,3/1,6-glucan for reducing weight [P]. In US Patent 20110135762. 2011.
[16] Lakshminarayanan R, Kesselman E, Cohen R, et al. Curdlan complexes as a potential food-grade delivery system: genistein case study [J]. Therapeutic Delivery, 2011, 2: 181-192.
[17] Toyoda S, Kimura M. Method for producing meat products and processed meat products coated with curdlan gel film [P]. US Patent. 7201932: 2007..
[18] Cheung N V. Therapy-enhancing glucan [P]. In US Patent App 20100216743. 2010.
[19] Cox D J. Particulate-soluble glucan preparation [P]. In US Patent App 20090036401. 2008.
[20] Kamaguchi R, Shiomi T. Thermostable capsule and process for producing the same (as amended) [P]. In US Patent App 20060286282. 2004.
[21] Kihara M S, Hiroshima. Polysaccharide thickener-containing dietray fiber composition [P]. In EP20070737368. 2009.
[22] Jung H, Lee K. Solid microstructure that enables multiple controlled release and method of maufacturing same [P]. In US Patent 20110177139. 2011.
[23] Shinya T, Menard R, Kozone I, et al. Novelβ-1,3-1,6-oligoglucan elicitor from Alternaria alternata 102 for defense responses in tobacco [J]. FEBS J, 2006, 273: 2421-2431.
[24] Cosio E G, Frey T, Verduyn R, et al. High-affinity binding of a synthetic heptaglucoside and fungal glucan phytoalexin elicitors to soybean membranes [J]. FEBS Lett, 1990, 271: 223-226.
[25] Yamaguchi T, Yamada A, Hong N, et al. Differences in the recognition of glucan elicitor signals between rice and soybean: beta-glucan fragments from the rice blast disease fungus Pyricularia oryzae that elicit phytoalexin biosynthesis in suspension-cultured rice cells [J]. Plant cell, 2000, 12: 817-826.
[26] Umemoto N, Kakitani M, Iwamatsu A, et al. The structure and function of a soybean beta-glucan-elicitor-binding protein [J]. P Natl Acad Sci USA, 1997, 94: 1029-1034.
[27] Daxberger A, Nemak A, Mithofer A, et al. Activation of members of a MAPK module in beta-glucan elicitor-mediated non-host resistance of soybean [J]. Planta, 2007, 225: 1559-1571.
[28] Miyanishi N, Iwamoto Y, Watanabe E, et al. Induction of TNF-αproduction from human peripheral blood monocytes withβ-1,3-glucan oligomer prepared from laminarin withβ-1,3-glucanase from Bacillus clausii NM-1 [J]. J Biosci Bioeng, 2003, 95: 192-195.
[29] Vetvicka V, Saraswat-Ohri S, Vashishta A, et al. New 4-deoxy-1,3-β-D-glucan-based oligosaccharides and their immunostimulating potential [J]. Carbohyd Res, 2011, 346: 2213-2221.
[30] Jamois F, Ferrieres V, Guegan J P, et al. Glucan-like synthetic oligosaccharides: iterative synthesis of linear oligo-β-(1,3)-glucans and immunostimulatory effects [J]. Glycobiology, 2005, 15: 393-407.
[31] Amemura A, Hisamatsu M, Harada T. Spontaneous mutation of polysaccharide production in Alcaligenes faecalis var. myxogenes 10C3 [J]. Appl Environ Microbiol, 1977, 34: 617-620.
[32] Lee J W, Yeomans W G, Allen A L, et al. Exopolymers from curdlan production: Incorporation of glucose-related sugars by Agrobacterium sp. strain ATCC 31749 [J]. Can J Microbiol, 1997, 43: 149-156.
[33] Ghai S K. Compositional studies on succinoglycan-like extracellular water-soluble Rhizobium polysaccharides [J]. Acta Microbiol Pol, 1981, 30: 133-141.
[34] Kenyon W J, Buller C S. Structural analysis of the curdlan-like exopolysaccharide produced by Cellulomonas flavigena KU [J]. J Ind Microbiol Biotechnol, 2002, 29: 200-203.
[35] Ohno N, Uchiyama M, Tsuzuki A, et al. Solubilization of yeast cell-wallβ-1,3-D-glucan by sodium hypochlorite oxidation and dimethyl sulfoxide extraction [J]. Carbohydr Res, 1999, 316: 161-172.
[36] Nanba H, Hamaguchi A, Kuroda H. The chemical structure of an antitumor polysaccharide in fruit bodies of Grifola frondosa (maitake) [J]. Chem Pharm Bull (Tokyo), 1987, 35: 1162-1168.
[37] Suzuki I, Hashimoto K, Oikawa S, et al. Antitumor and immunomodulating activities of a beta-glucan obtained from liquid-cultured Grifola frondosa [J]. Chem Pharm Bull, 1989, 37: 410-413.
[38] Fukuoka F, Nakanishi M, Shibata S, et al. Polysaccharides in lichens and fungi. II. Anti-tumor activities on sarcoma-180 of the polysaccharide preparations from Gyrophora esculenta miyoshi, Cetraria islandica (L.) Ach. var. orientalis asahina, and some other lichens [J]. Gann, 1968, 59: 421-432.
[39] Miyazaki T, Oikawa N, Yadomae T, et al. Relationship between the chemical structure and anti-tumour activity of glucans prepared from Grifora umbellata [J]. Carbohyd Res, 1979, 69: 165-170.
[40] Miyazaki T, Oikawa N, Yamada H, et al. Structural examination of antitumour, water-soluble glucans from Grifora umbellata by use of four types of glucanase [J]. Carbohyd Res, 1978, 65: 235-243.
[41] Zheng R, Jie S, Hanchuan D, et al. Characterization and immunomodulating activities of polysaccharide from Lentinus edodes [J]. Int Immunopharmacol, 2005, 5: 811-820.
[42] Zhang L, Surenjav U, Xu X J, et al. Effects of molecular structure on antitumor activities ofβ- (1,3) -D-glucans from different Lentinus Edodes [J]. Carbohydr Polym, 2006, 63: 97-104.
[43] Tabata K, Ito W, Kojima T, et al. Ultrasonic degradation of schizophyllan, an antitumor polysaccharide produced by Schizophyllum commune Fries [J]. Carbohydr Res, 1981, 89: 121-135.
[44] Hashimoto K, Suzuki I, Yadomae T. Oral administration of SSG, aβ-glucan obtained from Sclerotinia sclerotiorum, affects the function of Peyer's patch cells [J]. Int J Immunopharmacol, 1991, 13: 437-442.
[45] Ohno N, Suzuki I, Yadomae T. Structure and antitumor activity of a beta-1,3-glucan isolated from the culture filtrate of Sclerotinia sclerotiorum IFO 9395[J]. Chem Pharm Bull, 1986, 34: 1362-1365.
[46] Stuart I M, Loi L, Fincher G B. Development of (1,3-1,4)-β-D-glucan endohydrolase isoenzymes in isolated scutella and aleurone layers of barley (Hordeum vulgare) [J]. Plant Physiol, 1986, 80: 310-314.
[47] Tsai C M, Hassid W Z. Solubilization and separation of uridine diphospho-D-glucose:β-1, 4)-glucan and uridine diphospho-D-glucose:β-(1,3-glucan glucosyltransferases from coleoptiles of Avena sativa [J]. Plant Physiol, 1971, 47: 740-744.
[48] Lai D M, Hoj P B, Fincher G B. Purification and characterization of 1,3-1,4-β-glucan endohydrolases from germinated wheat (Triticum aestivum) [J]. Plant Mol Biol, 1993, 22: 847-859.
[49] Kim M K, Ryu K E, Choi W A, et al. Enhanced production ofβ-1 ,3-glucan by a mutant strain of Agrobacterium species [J]. Biochem Eng J, 2003, 16: 163-168.
[50] West T P. Elevated curdlan production by a mutant of Agrobacterium sp. ATCC 31749 [J]. J Basic Microb, 2009, 49: 589-592.
[51] Zheng Z Y, Lee A W, Zhan X B, et al. Effect of metabolic structures and energy requirements on curdlan production by Alcaligenes faecalis [J]. Biotechnol Bioprocess Eng, 2007, 12: 359-365.
[52] Wu J, Zhan X, Liu H, et al. Enhanced production of curdlan by Alcaligenes faecalis by selective feeding with ammonia water during the cell growth phase of fermentation [J]. Chi J Biotechnol, 2008, 24: 1035-1039.
[53] Yu L, Wu J, Liu J, et al. Enhanced curdlan production in Agrobacterium sp. ATCC 31749 by addition of low-polyphosphates [J]. Biotechnol Bioproc Eng, 2011, 16: 34-41.
[54] Zhang H T, Zhan X B, Zheng Z Y, et al. New strategy for enhancement Curdlan biosynthesis in Alcaligenes faecalis by activating gene expression [C], Bioinformat Biomed Engin, 2010:1-5.
[55] Lawford H, Keenan J, Phillips K, et al. Influence of bioreactor design on the rate and amount of curdlan-type exopolysaccharide production by Alcaligenes faecalis [J]. Biotechnol Lett, 1986, 8: 145-150.
[56]Lee J H, Lee I Y. Optimization of uracil addition for curdlan (β-1,3-glucan) production by Agrobacterium sp. [J]. Biotechnol Lett, 2001, 23: 1131-1134.
[57]Lee J H, Park Y H. Optimal production of curdlan by Agrobacterium sp. with feedback inferential control of optimal pH profile [J]. Biotechnol Lett, 2001, 23: 525-530.
[58] West T P. Pyrimidine base supplementation effects curdlan production in Agrobacterium sp. ATCC 31749 [J]. J Basic Microb, 2006, 46: 153-157.
[59]Lee I Y, Kim M K, Lee J H, et al. Influence of agitation speed on production of curdlan by Agrobacterium species[J]. Bioprocess Eng, 1999, 20: 283-287.
[60]Lawford H, Keenan J, Phillips K, et al. Influence of bioreactor design on the rate and amount of curdlan-type exopolysaccharide production by Alcaligenes faecalis[J]. Biotechnol lett, 1986, 8: 145-150.
[61]Lakhwala F,Sofer S. Design considerations for an immobilized cell bioreactor operating in a batch recirculation mode[J]. J Chem Technol Biotechnol, 1991, 52: 499-509.
[62]Weyand B, Israelowitz M, von Schroeder H P, et al. Fluid dynamics in bioreactor design: considerations for the theoretical and practical approach[J]. Adv Biochem Eng Biotechnol, 2009, 112: 251-268.
[63] Yu P, Lee T S, Yan Z, Low Ho T. Fluid dynamics and oxygen transport in a micro-bioreactor with a tissue engineering scaffold[J]. Int J Heat Mass Transf, 2009, 52:316-327
[64] Mischnick P, Evers B, Thiem J. Analysis of oligosaccharides containing 2-deoxy-alpha-D-arabino-hexosyl residues by the reductive-cleavage method [J]. Carbohydr Res, 1994, 264: 293-304.
[65] Sasaki A. Isolation and characterization of serologically active phosphatidylinositol oligomannosides of Mycobacterium tuberculosis [J]. J Biochem-Tokyo, 1975, 78: 547-554.
[66] Anumula K R, Taylor P B. A comprehensive procedure for preparation of partially methylated alditol acetates from glycoprotein carbohydrates [J]. Anal Biochem, 1992, 203: 101-108.
[67] Rudd P M, Marino K, Lane J A, et al. Method for milk oligosaccharide profiling by 2-aminobenzamide labeling and hydrophilic interaction chromatography [J]. Glycobiology, 2011, 21: 1317-1330.
[68] Hayes B K,Varki A. Fractionation and analysis of neutral oligosaccharides by HPLC [J]. Curr Protoc Mol Biol, 2001, 17.21.9–17.21.13
[69] Lo-Guidice J M, Lhermitte M. HPLC of oligosaccharides in glycobiology [J]. Biomed Chromatogr, 1996, 10: 290-296.
[70] Montgomery H, Tanaka K, Belgacem O. Glycation pattern of peptides condensed with maltose, lactose and glucose determined by ultraviolet matrix-assisted laser desorption/ionization tandem mass spectrometry [J]. Rapid Commun Mass Spectrom, 2010, 24: 841-848.
[71] An H J, Lebrilla C B. Structure elucidation of native N- and O-linked glycans by tandem mass spectrometry (tutorial) [J]. Mass Spectrom Rev, 2011, 30: 560-578.
[72] Laremore T N, Leach F E, Solakyildirim K, et al. Glycosaminoglycan characterization by electrospray ionization mass spectrometry including fourier transform mass spectrometry [J]. Methods Enzymol, 2010, 478: 79-108.
[73] Chen S, Xu J, Xue C, et al. Sequence determination of a non-sulfated glycosaminoglycan-like polysaccharide from melanin-free ink of the squid Ommastrephes bartrami by negative-ion electrospray tandem mass spectrometry and NMR spectroscopy [J]. Glycoconj J, 2008, 25: 481-492.
[74] Yu G, Zhao X, Yang B, et al. Sequence determination of sulfated carrageenan-derived oligosaccharides by high-sensitivity negative-ion electrospray tandem mass spectrometry [J]. Anal Chem, 2006, 78: 8499-8505.
[75] Zanetta J P, Pons A, Richet C, et al. Sequential GC/MS analysis of sialic acids, monosaccharides, and amino acids of glycoproteins on a single sample as heptafluorobutyrate derivatives [J]. Biochemistry, 2003, 42: 8342-8353.
[76] Kacurakova M, Mathlouthi M. FTIR and laser-Raman spectra of oligosaccharides in water: characterization of the glycosidic bond [J]. Carbohyd Res, 1996, 284: 145-157.
[77] Kanou M, Nakanishi K, Hashimoto A, et al. Influences of monosaccharides and its glycosidic linkage on infrared spectral characteristics of disaccharides in aqueous solutions [J]. Appl Spectrosc, 2005, 59: 885-892.
[78] Furuki T. Effect of molecular structure on thermodynamic properties of carbohydrates. A calorimetric study of aqueous di- and oligosaccharides at subzero temperatures [J]. Carbohyd Res, 2002, 337: 441-450.
[79] Tul'chinsky V M, Zurabyan S E, Asankozhoev K A, et al. Study of the infrared spectra of oligosaccharides in the region 1,000-40 cm-1 [J]. Carbohyd Res, 1976, 51: 1-8.
[80] Domenech J, Prieto A, Gomez-Miranda B, et al. Structure of fungal polysaccharides isolated from the cell-wall of three strains of Verticillium fungicola [J]. Carbohydr Polym, 2002, 50: 209-212.
[81] Roslund M U, Sawen E, Landstrom J, et al. Complete 1H and 13C NMR chemical shift assignments of mono-, di-, and trisaccharides as basis for NMR chemical shift predictions of polysaccharides using the computer program casper [J]. Carbohyd Res, 2011, 346: 1311-1319.
[82] Lundborg M,Widmalm G. Structural analysis of glycans by NMR chemical shift prediction [J]. Anal Chem, 2011,83:1514-1517
[83] Feizi T, Fazio F, Chai W, et al. Carbohydrate microarrays - a new set of technologies at the frontiers of glycomics [J]. Curr Opin Struct Biol, 2003, 13: 637-645.
[84] Palma A S, Feizi T, Zhang Y, et al. Ligands for the beta-glucan receptor, Dectin-1, assigned using "designer" microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides [J]. J Biol Chem, 2006, 281: 5771-5779.
[85] Ruffing A, Mao Z, Chen R R Z. Metabolic engineering of Agrobacterium sp. for UDP-galactose regeneration and oligosaccharide synthesis [J]. Metab Eng, 2006, 8: 465-473.
[86] Dussap, C. G., De Vita, D. and Pons, A. Modeling growth and succinoglucan production by Agrobacterium radiobacter NCIB 9042 in batch cultures[J]. Biotechnol Bioeng, 1991,38: 65–74.
[87] Lee I Y, Seo W T, Kim G J, et al. Production of curdlan using sucrose or sugar cane molasses by two-step fed-batch cultivation of Agrobacterium species [J]. J Ind Microbiol Biotechnol, 1997, 18: 255-259.
[8] Jin L H, Um H J, Yin C J, et al. Proteomic analysis of curdlan-producing Agrobacterium sp. in response to pH downshift [J]. J Biotechnol, 2008, 138: 80-87.
[89] Trubitsin B V, Ptushenko V V, Koksharova O A, et al. EPR study of electron transport in the cyanobacterium Synechocystis sp. PCC 6803: Oxygen-dependent interrelations between photosynthetic and respiratory electron transport chains [J]. BBA-Bioenergetics, 2005, 1708: 238-249.
[90] Awai K, Kakimoto T, Awai C, et al. Comparative genomic analysis revealed a gene for monoglucosyldiacylglycerol synthase, an enzyme for photosynthetic membrane lipid synthesis in cyanobacteria [J]. Plant Physiol, 2006, 141: 1120-1127.
[91] Johnston M, Cliften P F, Hillier L W, et al. Surveying Saccharomyces genomes to identify functional elements by comparative DNA sequence analysis [J]. Genome Res, 2001, 11: 1175-1186.
[92] Rinner O, Morgenstern B. AGenDA: gene prediction by comparative sequence analysis [J]. In Silico Biol, 2002, 2: 195-205.
[93] Wood D W, Setubal J C, Kaul R, et al. The genome of the natural genetic engineer Agrobacterium tumefaciens C58 [J]. Science, 2001, 294: 2317-2323.
[94] Slater S C, Goldman B S, Goodner B, et al. Genome sequences of three Agrobacterium biovars help elucidate the evolution of multichromosome genomes in bacteria [J]. J Bacteriol, 2009, 191: 2501-2511.
[95] Wheatcroft R,Watson R J. A positive strain identification method for Rhizobium meliloti [J]. Appl Environ Microbiol, 1988, 54: 574-576.
[96] Altschul S, Madden T, Schaffer A, et al. Gapped BLAST and PSI-BLAST: A new generation of proteindatabase search programs [J]. FASEB J, 1998, 12: A1326-A1326.
[97]Wu M, Eisen J A. A simple, fast, and accurate method of phylogenomic inference [J]. Genome Biology, 2008, 9: R151.
[98] Dereeper A, Guignon V, Blanc G, et al. Phylogeny.fr: robust phylogenetic analysis for the non-specialist [J]. Nucleic Acids Res, 2008, 36: W465-W469.
[99] Alpes I, Scherer S, B?ger P. The respiratory NADH dehydrogenase of the cyanobacterium Anabaena variabilis: purification and characterization [J]. BBA-Bioenergetics, 1989, 973: 41-46.
[100]Steimle S, Pohl T,Friedrich T. Assembly of the Escherichia coli NADH: ubiquinone oxidoreductase (complex I) [J]. BBA-Bioenergetics, 2010, 1797: 23-23.
[101] Braun M, Bungert S, Friedrich T. Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli[J].Biochem, 1998, 37:1861-1867.
[102]Friedrich T, Schneider D, Pohl T, et al. Assembly of the Escherichia coli NADH: ubiquinone oxidoreductase (complex I) [J]. BBA-Bioenergetics, 2008, 1777: 735-739.
[103]Cecchini G, Schroder I, Gunsalus R P, et al. Succinate dehydrogenase and fumarate reductase from Escherichia coli [J]. BBA-Bioenergetics, 2002, 1553: 140-157.
[104]Westenberg D J, Guerinot M L. Succinate dehydrogenase (Sdh) from Bradyrhizobium japonicum is closely related to mitochondrial Sdh [J]. J Bacteriol, 1999, 181: 4676-4679.
[105]Meganathan R. Ubiquinone biosynthesis in microorganisms [J]. FEMS Microbiol Lett, 2001, 203: 131-139.
[106]Poon W W, Davis D E, Ha H T, et al. Identification of Escherichia coli ubiB, a gene required for the first monooxygenase step in ubiquinone biosynthesis [J]. J Bacteriol, 2000, 182: 5139-5146.
[107]Rubin H, Kana B D, Weinstein E A, et al. Characterization of the cydAB-encoded cytochrome bd oxidase from Mycobacterium smegmatis [J]. J Bacteriol, 2001, 183: 7076-7086.
[108]Smith A, Hill S, Anthony C. The purification, characterization and role of the d-type cytochrome oxidase of Klebsiella pneumoniae during nitrogen fixation [J]. J Gen Microbiol, 1990, 136: 171-180.
[109]Chepuri V, Lemieux L, Au D C T, et al. The sequence of the cyo operon indicates substantial structural similarities between the cytochrome-o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome-c oxidases [J]. J Biol Chem, 1990, 265: 11185-11192.
[110]Mogi T, Saiki K, Anraku Y. Biosynthesis and functional role of haem O and haem A [J]. Mol Microbiol, 1994, 14: 391-398.
[111]Williams H D, Hubbard J A M, Nugent J H A, et al. Functional size measurements of the ubiquinol oxidase activity of the cytochrome-o terminal oxidase complex of Escherichia coli [J]. Biochem J, 1991, 276: 555-557.
[112]Preisig O, Zufferey R, Thony-Meyer L, et al. A high-affinity cbb3-type cytochrome oxidase terminates the symbiosis-specific respiratory chain of Bradyrhizobium japonicum [J]. J Bacteriol, 1996, 178: 1532-1538.
[113]Saraste M, Metso T, Nakari T, et al. The Bacillus subtilis cytochrome-c oxidase: variations on a conserved protein theme [J]. Eur J Biochem/FEBS, 1991, 195: 517-525.
[114]Bott M, Niebisch A. The respiratory chain of corynebacterium glutamicum [J]. J Biotechnol, 2003, 104: 129-153.
[115]Hill B C, Greenwood C. The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature: evidence for new pathways of electron transfer [J]. Biochem J, 1984, 218: 913-921.
[116]Bott M, Bolliger M, Hennecke H. Genetic analysis of the cytochrome c-aa3 branch of the Bradyrhizobium japonicum respiratory chain [J]. Mol Microbiol, 1990, 4: 2147-2157.
[117]Richter O M,Ludwig B. Electron transfer and energy transduction in the terminal part of the respiratory chain - lessons from bacterial model systems [J]. Biochim Biophys Acta, 2009, 1787: 626-634.
[118]Yumoto I. Bioenergetics of alkaliphilic Bacillus spp [J]. J Biosci Bioeng, 2002, 93: 342-353.
[119]Slater S C, Goldman B S, Goodner B, et al. Genome sequences of three Agrobacterium biovars help elucidate the evolution of multichromosome genomes in bacteria [J]. J Bacteriol, 2009, 191: 2501-2511.
[120]Minghetti K C, Gennis R B. The two terminal oxidases of the aerobic respiratory chain of Escherichia coli each yield water and not peroxide as a final product [J]. Biochem Bioph Res Co, 1988, 155: 243-248.
[121]Matsushita K, Ohnishi T,Kaback H R. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain [J]. Biochemistry, 1987, 26: 7732-7737.
[122]Miller M J, Gennis R B. The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli [J]. J Biol Chem, 1985, 260: 14003-14008.
[123]Miller M J, Gennis R B. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain [J]. J Biol Chem, 1983, 258: 9159-9165.
[124]Arslan E, Kannt A, Thony-Meyer L, et al. The symbiotically essential cbb3-type oxidase of Bradyrhizobium japonicum is a proton pump [J]. FEBS Lett, 2000, 470: 7-10.
[125]Bundschuh F A, Hoffmeier K, Ludwig B. Two variants of the assembly factor Surf1 target specific terminal oxidases in Paracoccus denitrificans [J]. Biochim Biophys Acta, 2008, 1777: 1336-1343.
[126]de Gier J W, Lubben M, Reijnders W N, et al. The terminal oxidases of Paracoccus denitrificans [J]. Mol Microbiol, 1994, 13: 183-196.
[127]Karnezis T, Epa V C, Stone B A, et al. Topological characterization of an inner membraneβ-1,3 -D-glucan (curdlan) synthase from Agrobacterium sp. strain ATCC31749 [J]. Glycobiology, 2003, 13: 693-706.
[128]Ruffing A M, Castro-Melchor M, Hu W S, et al. Genome sequence of the curdlan-producing Agrobacterium sp. strain ATCC 31749 [J]. J Bacteriol, 2011, 193: 4294-4295.
[129]Zhang Z, Qu Y, Zhang X, et al. Effects of oxygen limitation on xylose fermentation, intracellularmetabolites, and key enzymes of Neurospora crassa AS3.1602 [J]. Appl Biochem Biotechnol, 2008, 145: 39-51.
[130]Verbelen P J, Saerens S M, Van Mulders S E, et al. The role of oxygen in yeast metabolism during high cell density brewery fermentations [J]. Appl Microbiol Biotechnol, 2009, 82: 1143-1156.
[131]Yang S, Tschaplinski T J, Engle N L, et al. Transcriptomic and metabolomic profiling of Zymomonas mobilis during aerobic and anaerobic fermentations [J]. BMC Genomics, 2009, 10: 34.
[132]Sandoval-Basurto E A, Gosset G, Bolivar F, et al. Culture of Escherichia coli under dissolved oxygen gradients simulated in a two-compartment scale-down system: metabolic response and production of recombinant protein[J]. Biotechnol Bioeng, 2005, 89: 453-463.
[133]Portilho M, Matioli G, Zanin G M, et al. Production of insoluble exopolysaccharide of Agrobacterium sp. (ATCC 31749 and IFO 13140) [J]. Appl Biochem Biotechnol, 2006, 129-132: 864-869.
[134]West T P. Pyrimidine base supplementation effects curdlan production in Agrobacterium sp. ATCC 31749 [J]. J Basic Microb, 2006, 46: 153-157.
[135]Lawford H, Rousseau J. Effect of oxygen on the rate ofβ-1,3-glucan microbial exopolysaccharide production [J]. Biotechnol Lett, 1989, 11: 125-130.
[136]Lawford H, Rousseau J. Production ofβ-1,3-glucan exopolysaccharide in low shear systems [J]. Appl Biochem Biotechnol, 1992, 34-35: 597-612.
[137]Pitcher D G, Saunders N A, Owen R J. Rapid extraction of bacterial genomic DNA with guanidium thiocyanate [J]. Lett Appl Microbiol, 1989, 8: 151-156.
[138]Zhang H, Setubal J C, Zhan X, et al. Component identification of electron transport chains in curdlan-producing Agrobacterium sp. ATCC 31749 and its genome-specific prediction using comparative genome and phylogenetic trees analysis [J]. J Ind Microbiol Biotechnol, 2011, 38: 667-677.
[139]Kongruang S, Han M J, Breton C I, et al. Quantitative analysis of cellulose-reducing ends [J]. Appl Biochem Biotechnol, 2004, 113-116: 213-231.
[140]Rau U, Gura E, Olszewski E, et al. Enhanced glucan formation of filamentous fungi by effective mixing, oxygen limitation and fed-batch processing[J]. J Ind Microbiol, 1992, 9: 19-25.
[141]Gummadi S N, Kumar K. Production of extracellular water insolubleβ-1,3-glucan (curdlan) from Bacillus sp. SNC07 [J]. Biotechnol Bioprocess Eng, 2005, 10: 546-551.
[142]Unden G, Trageser M. Oxygen regulated gene expression in Escherichia coli: control of anaerobic respiration by the FNR protein [J]. Antonie Van Leeuwenhoek, 1991, 59: 65-76.
[143]Cotter P A, Chepuri V, Gennis R B, et al. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product [J]. J Bacteriol, 1990, 172: 6333-6338.
[144]Mengin-Lecreulx D,van Heijenoort J. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli [J]. J Biol Chem, 1996, 271: 32-39.
[145]Thoden J B, Holden H M. The molecular architecture of glucose-1-phosphate uridylyltransferase [J].Protein Sci, 2007, 16: 432-440.
[146]Lara A R, Leal L, Flores N, et al. Transcriptional and metabolic response of recombinant Escherichia coli to spatial dissolved oxygen tension gradients simulated in a scale-down system [J]. Biotechnol Bioeng, 2006, 93: 372-385.
[147]Shalel-Levanon S, San K Y, Bennett G N. Effect of oxygen, and ArcA and FNR regulators on the expression of genes related to the electron transfer chain and the TCA cycle in Escherichia coli [J]. Metab Eng, 2005, 7: 364-374.
[148]Kim M K, Lee I Y, Lee J H, et al. Residual phosphate concentration under nitrogen-limiting conditions regulates curdlan production inAgrobacterium species[J]. J Ind Microbiol Biotechnol, 2000, 25: 180-183.
[149]Crosson S, McGrath P T, Stephens C, et al. Conserved modular design of an oxygen sensory/signaling network with species-specific output [J]. P Natl Acad Sci USA, 2005, 102: 8018-8023.
[150]Biel A J, Marrs B L. Transcriptional regulation of several genes for Bacteriochlorophyll biosynthesis in Rhodopseudomonas capsulata in response to oxygen [J]. J Bacteriol, 1983, 156: 686-694.
[151]Kwast K E, Burke P V,Poyton R O. Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast [J]. J Exp Biol, 1998, 201: 1177-1195.
[152]Uziel O, Borovok I, Schreiber R, et al. Transcriptional regulation of the Staphylococcus aureus thioredoxin and thioredoxin reductase genes in response to oxygen and disulfide stress [J]. J Bacteriol, 2004, 186: 326-334.
[153]Czyzyk-Krzeska M F. Molecular aspects of oxygen sensing in physiological adaptation to hypoxia [J]. Respir Physiol, 1997, 110: 99-111.
[154]Bunn H F, Poyton R O. Oxygen sensing and molecular adaptation to hypoxia [J]. Physiol Rev, 1996, 76: 839-885.
[155]Lois A F, Ditta G S, Helinski D R. The oxygen sensor FixL of Rhizobium meliloti is a membrane protein containing four possible transmembrane segments [J]. J Bacteriol, 1993, 175: 1103-1109.
[156]Willems A, Collins M D. Phylogenetic analysis of rhizobia and agrobacteria based on 16S rRNA gene sequences [J]. Int J Syst Bacteriol, 1993, 43: 305-313.
[157]Young J M, Kuykendall L D, Martinez-Romero E, et al. A revision of Rhizobium Frank 1889, with an emended description of the genus, and the inclusion of all species of Agrobacterium Conn 1942 and Allorhizobium undicola de Lajudie et al. 1998 as new combinations: Rhizobium radiobacter, R. rhizogenes, R. rubi, R. undicola and R. vitis [J]. Int J Syst Evol Microbiol, 2001, 51: 89-103.
[158]Liu Y S, Wu H Y, Ho K P. Characterization of oxygen transfer conditions and their effects on Phaffia rhodozyma growth and carotenoid production in shake-flask cultures [J]. Biochem Eng J, 2006, 27: 331-335.
[159]Kaya-Celiker H, Angardi V, Calik P. Regulatory effects of oxygen transfer on overexpression of recombinant benzaldehyde lyase production by Escherichia coli BL21 (DE3) [J]. Biotechnol J, 2009,4: 1066-1076.
[160]Fazenda M L, Harvey L M, McNeil B. Effects of dissolved oxygen on fungal morphology and process rheology during fed-batch processing of Ganoderma lucidum [J]. J Microbiol Biotechnol, 2010, 20: 844-851.
[161]Calik P, Yilgor P, Ayhan P, et al. Oxygen transfer effects on recombinant benzaldehyde lyase production [J]. Chem Eng Sci, 2004, 59: 5075-5083.
[162]Fredlund E, Blank L M, Schnurer J, et al. Oxygen- and glucose-dependent regulation of central carbon metabolism in Pichia anomala [J]. Appl Environ Microb, 2004, 70: 5905-5911.
[163]Martin A B, Alcon A, Santos V E, et al. Production of a biocatalyst of Pseudomonas putida CECT5279 for DBT biodesulfurization: Influence of the operational conditions [J]. Energy Fuels, 2005, 19: 775-782.
[164]Kim B S, Jung I D, Kim J S, et al. Curdlan gels as protein drug delivery vehicles [J]. Biotechnol Lett, 2000, 22: 1127-1130.
[165]Garc?a?-Ochoa F, Castro E G,Santos V E. Oxygen transfer and uptake rates during xanthan gum production [J]. Enzyme Microb Technol, 2000, 27: 680-690.
[166]Wang Y, McNeil B. Dissolved oxygen and the scleroglucan fermentation process [J]. Biotechnol Lett, 1995, 17: 257-262.
[167]Levander F, Svensson M, Radstrom P. Enhanced exopolysaccharide production by metabolic engineering of Streptococcus thermophilus [J]. Appl Environ Microb, 2002, 68: 784-790.
[168]Chang Y K, Kim H H, Na J G, et al. Effects of dissolved oxygen control on cell growth and exopolysaccharides production in batch culture of Agaricus blazei [J]. Korean J Chem Eng, 2005, 22: 80-84.
[169]Kim M K, Lee I Y, Ko J H, et al. Higher intracellular levels of uridinemonophosphate under nitrogen-limited conditions enhance metabolic flux of curdlan synthesis in Agrobacterium species [J]. Biotechnol Bioeng, 1999, 62: 317-323.
[170]Fu Y Q, Li S, Chen Y, et al. Enhancement of fumaric acid production by Rhizopus oryzae using a two-stage dissolved oxygen control strategy [J]. Appl Biochem Biotechnol, 2010, 162: 1031-1038.
[171]Goodridge H S, Wolf A J, Underhill D M.β-glucan recognition by the innate immune system [J]. Immunol Rev, 2009, 230: 38-50.
[172]Albert O, Toubas D, Strady C, et al. Reactivity of 1,3-β-D-glucan assay in bacterial bloodstream infections [J]. Eur J Clin Microbiol Infect Dis, 2011 DOI: 10.1007/s10096-011-1244-8
[173]Marty F M, Lowry C M, Lempitski S J, et al. Reactivity ofβ-1,3 -d-glucan assay with commonly used intravenous antimicrobials [J]. Antimicrob Agents Chemother, 2006, 50: 3450-3453.
[174]Chan G C F, Chan W K, Sze D M Y. The effects ofβ-glucan on human immune and cancer cells [J]. J Hematol Oncol, 2009, 2: 25.
[175]Murphy E A, Davis J M, Carmichael M D. Immune modulating effects ofβ-glucan [J]. Curr Opin Clin Nutr Metab Care, 2010, 13: 656-661.
[176]Taylor P R, Brown G D, Reid D M, et al. Theβ-glucan receptor, dectin-1, is predominantly expressed on the surface of cells of the monocyte/macrophage and neutrophil lineages [J]. J Immunol, 2002, 169: 3876-3882.
[177]Brown G D, Taylor P R, Reid D M, et al. Dectin-1 is a majorβ-glucan receptor on macrophages [J]. J Exp Med, 2002, 196: 407-412.
[178]Xia Y, Vetvicka V, Yan J, et al. The beta-glucan-binding lectin site of mouse CR3 (CD11b/CD18) and its function in generating a primed state of the receptor that mediates cytotoxic activation in response to iC3b-opsonized target cells [J]. J Immunol, 1999, 162: 2281-2290.
[179]Cheung N K V, Modak S, Vickers A, et al. Orally administeredβ-glucans enhance anti-tumor effects of monoclonal antibodies [J]. Cancer Immunol Immun, 2002, 51: 557-564.
[180]Li B, Cai Y, Qi C, et al. Orally administered particulateβ-glucan modulates tumor-capturing dendritic cells and improves antitumor T-cell responses in cancer [J]. Clin Cancer Res, 2010, 16: 5153-5164.
[181]刘高强.灵芝多糖的抗癌构效关系及其抗癌作用机制[J].菌物学报, 2006, 25:430-438.
[182]李万坤.糖原组学研究进展——β-葡聚糖的结构和功能的研究进展[J].中国畜牧兽医, 2007, 34:152-155.
[183]Palma A S, Liu Y, Muhle-Goll C, et al. Multifaceted approaches including neoglycolipid oligosaccharide microarrays to ligand discovery for malectin [J]. Methods Enzymol, 2010, 478: 265-286.
[184]Yu G, Zhang Y, Zhang Z, et al. Effect and limitation of excess ammonium on the release of O-glycans in reducing forms from glycoproteins under mild alkaline conditions for glycomic and functional analysis [J]. Anal Chem, 2010, 82: 9534-9542.
[185]Fischer D, Geyer A, Loos E. Occurrence of glucosylsucrose [α-D-glucopyranosyl- 1,2-α-D-glucopyranosyl-1,2-β-D-fructofuranoside] and glucosylated homologues in cyanobacteria. Structural properties, cellular contents and possible function as thermoprotectants [J]. FEBS J, 2006, 273: 137-149.
[186]Roset M S, Ciocchini A E, Ugalde R A, et al. The Brucella abortus cyclicβ-1,2-glucan virulence factor is substituted with O-ester-linked succinyl residues [J]. J Bacteriol, 2006, 188: 5003-5013.
[187]Zhang P, Zhang L, Cheng S. Solution properties of anα-1,3-D-glucan from Lentinus edodes and its sulfated derivatives [J]. Carbohydr Res, 2002, 337: 155-160.
[188]Zhang L, Li X L, Xu X J, et al. Correlation between antitumor activity, molecular weight, and conformation of lentinan [J]. Carbohyd Res, 2005, 340: 1515-1521.
[189]Fischer D,Geyer A. NMR analysis of bioprotective sugars: Sucrose and oligomeric 1,2-α-D-glucopyranosyl-1,2-β-D-fructofuranosides [J]. Bioactive Conformation I, 2007, 272: 169-185.
[190]Chen S, Xu J, Xue C, et al. Sequence determination of a non-sulfated glycosaminoglycan-like polysaccharide from melanin-free ink of the squid Ommastrephes bartrami by negative-ion electrospray tandem mass spectrometry and NMR spectroscopy [J]. Glycoconjugate J, 2008, 25:481-492.
[191]Kogelberg H, Piskarev V E, Zhang Y, et al. Determination by electrospray mass spectrometry and 1H-NMR spectroscopy of primary structures of variously fucosylated neutral oligosaccharides based on the iso-lacto-N-octaose core [J]. Eur J Biochem, 2004, 271: 1172-1186.
[192]Liu Y, Chai W, Childs R A, et al. Preparation of neoglycolipids with ring-closed cores via chemoselective oxime-ligation for microarray analysis of carbohydrate-protein interactions [J]. Methods Enzymol, 2006, 415: 326-340.
[193]Fontes C M G A, Ponte P I P, Reis T C, et al. A family 6 carbohydrate-binding module potentiates the efficiency of a recombinant xylanase used to supplement cereal-based diets for poultry [J]. Br Poult Sci, 2004, 45: 648-656.
[194]Henshaw J L, Bolam D N, Pires V M R, et al. The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities [J]. J Biol Chem, 2004, 279: 21552-21559.
[195]Pires V M R, Henshaw J L, Prates J A M, et al. The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5A in complex with oligosaccharides reveals two distinct binding sites with different ligand specificities [J]. J Biol Chem, 2004, 279: 21560-21568.
[196]Leon M A, Young N M, McIntire K R. Immunochemical studies of the reaction between a mouse myeloma macroglobulin and dextrans [J]. Biochemistry, 1970, 9: 1023-1030.
[197]Crespo M S, Valera I, Ferandez N, et al. Costimulation of Dectin-1 and DC-SIGN triggers the arachidonic acid cascade in human monocyte-derived dendritic cells [J]. J Immunol, 2008, 180: 5727-5736.
[198]Holla A, Skerra A. Comparative analysis reveals selective recognition of glycans by the dendritic cell receptors DC-SIGN and Langerin [J]. Protein Eng Des Sel, 2011, 24: 659-669.
[199]Herre J, Gordon S, Brown G D. Dectin-1 and its role in the recognition of beta-glucans by macrophages [J]. Mol Immunol, 2004, 40: 869-876.
[200]Taylor P R, Brown G D, Reid D M, et al. The beta-glucan receptor, Dectin-1, is predominantly expressed on the surface of cells of the monocyte/macrophage and neutrophil lineages [J]. J Immunol, 2002, 169: 3876-3882.
[201]Apetrei N S, Calugaru A, Badulescu M M, et al. The effects of some Curdlan derivatives on Dectin-1 expression and cytokine production in human peripheral blood mononuclear cells [J]. Roum Arch Microbiol Immunol, 2010, 69: 61-66.
[202]Minari J, Mochizuki S, Matsuzaki T, et al. Enhanced cytokine secretion from primary macrophages due to Dectin-1 mediated uptake of CpG DNA/β-1,3-glucan complex [J]. Bioconjug Chem, 2011, 22: 9-15.
[203]Brown G D, Taylor P R, Tsoni S V, et al. Dectin-1 is required for beta-glucan recognition and control of fungal infection [J]. Nat Immunol, 2007, 8: 31-38
[204]Saijo S, Fujikado N, Furuta T, et al. Dectin-1 is required for host defense against Pneumocystiscarinii but not against Candida albicans [J]. Nat Immunol, 2007, 8: 39-46.
[205]Saijo S, Iwakura Y. Dectin-1 and Dectin-2 in innate immunity against fungi [J]. Int Immunol, 2011, 23: 467-472.
[206]Goodridge H S, Reyes C N, Becker C A, et al. Activation of the innate immune receptor Dectin-1 upon formation of a 'phagocytic synapse' [J]. Nature, 2011, 472: 471-475.
[207]Ferwerda B, Ferwerda G, Plantinga T S, et al. Human Dectin-1 deficiency and mucocutaneous fungal infections [J]. N Engl J Med, 2009, 361: 1760-1767.
[208]Williams D L, Adams E L, Rice P J, et al. Differential high-affinity interaction of Dectin-1 with natural or synthetic glucans is dependent upon primary structure and is influenced by polymer chain length and side-chain branching [J]. J Pharmacol Exp Ther, 2008, 325: 115-123.
[209]Geurtsen J, Chedammi S, Mesters J, et al. Identification of Mycobacterialα-glucan as a novel ligand for DC-SIGN: involvement of Mycobacterial capsular polysaccharides in host immune modulation[J]. J Immunol, 2009,183:5221-5331
[2] Descroix K, Vetvicka V, Laurent I, et al. New oligo-β-1,3-glucan derivatives as immunostimulating agents [J]. Bioorg Med Chem, 2010, 18: 348-357.
[3] Ruiz-Herrera J. Biosynthesis ofβ-glucans in fungi [J]. Antonie Van Leeuwenhoek, 1991, 60: 72-81.
[4] Yiannikouris A, Francois J, Poughon L, et al. Alkali extraction ofβ-D-glucans from Saccharomyces cerevisiae cell wall and study of their adsorptive properties toward zearalenone [J]. J Agric Food Chem, 2004, 52: 3666-3673.
[5] Masuoka J. Surface glycans of Candida albicans and other pathogenic fungi: physiological roles, clinical uses, and experimental challenges [J]. Clin Microbiol Rev, 2004, 17: 281-310.
[6] Kondori N, Edebo L, Mattsby-Baltzer I. A novel monoclonal antibody recognizingβ-1,3-glucans in intact cells of Candida and Cryptococcus [J]. APMIS, 2008, 116: 867-876.
[7] Ishibashi K, Yoshida M, Nakabayashi I, et al. Role of anti-beta-glucan antibody in host defense against fungi [J]. FEMS Immunol Med Microbiol, 2005, 44: 99-109.
[8] Torosantucci A, Chiani P, Bromuro C, et al. Protection by anti-beta-glucan antibodies is associated with restrictedβ-1,3 glucan binding specificity and inhibition of fungal growth and adherence [J]. PLoS One, 2009, 4(4): e5392.
[9] Taylor P R, Tsoni S V, Willment J A, et al. Dectin-1 is required forβ-glucan recognition and control of fungal infection [J]. Nat Immunol, 2007, 8: 31-38.
[10] Berner V K, Sura M E, Hunter K W J. Conjugation of protein antigen to microparticulate beta-glucan from Saccharomyces cerevisiae: a new adjuvant for intradermal and oral immunizations [J]. Appl Microbiol Biotechnol, 2008, 80: 1053-1061.
[11] Kimura Y, Sumiyoshi M, Suzuki T, et al. Antitumor and antimetastatic activity of a novel water-soluble low molecular weightβ-1,3-D-glucan (branchβ-1,6) isolated from Aureobasidium pullulans 1A1 strain black yeast [J]. Anticancer Res, 2006, 26: 4131-4141.
[12] Berner M D, Sura M E, Alves B N, et al. IFN-gamma primes macrophages for enhanced TNF-αexpression in response to stimulatory and non-stimulatory amounts of microparticulateβ-glucan [J]. Immunol Lett, 2005, 98: 115-122.
[13] Chan G C, Chan W K, Sze D M. The effects ofβ-glucan on human immune and cancer cells [J]. J Hematol Oncol, 2009, 2:p 25.
[14] Vandamme E J, De Baets S, Steinbüchel A. Polysaccharides I: Polysaccharides of Prokaryotes [M]. Weiheim Wiley VCH, 2004: 237-298.
[15] Mortensen N C. Composition comprisingβ-1,3/1,6-glucan for reducing weight [P]. In US Patent 20110135762. 2011.
[16] Lakshminarayanan R, Kesselman E, Cohen R, et al. Curdlan complexes as a potential food-grade delivery system: genistein case study [J]. Therapeutic Delivery, 2011, 2: 181-192.
[17] Toyoda S, Kimura M. Method for producing meat products and processed meat products coated with curdlan gel film [P]. US Patent. 7201932: 2007..
[18] Cheung N V. Therapy-enhancing glucan [P]. In US Patent App 20100216743. 2010.
[19] Cox D J. Particulate-soluble glucan preparation [P]. In US Patent App 20090036401. 2008.
[20] Kamaguchi R, Shiomi T. Thermostable capsule and process for producing the same (as amended) [P]. In US Patent App 20060286282. 2004.
[21] Kihara M S, Hiroshima. Polysaccharide thickener-containing dietray fiber composition [P]. In EP20070737368. 2009.
[22] Jung H, Lee K. Solid microstructure that enables multiple controlled release and method of maufacturing same [P]. In US Patent 20110177139. 2011.
[23] Shinya T, Menard R, Kozone I, et al. Novelβ-1,3-1,6-oligoglucan elicitor from Alternaria alternata 102 for defense responses in tobacco [J]. FEBS J, 2006, 273: 2421-2431.
[24] Cosio E G, Frey T, Verduyn R, et al. High-affinity binding of a synthetic heptaglucoside and fungal glucan phytoalexin elicitors to soybean membranes [J]. FEBS Lett, 1990, 271: 223-226.
[25] Yamaguchi T, Yamada A, Hong N, et al. Differences in the recognition of glucan elicitor signals between rice and soybean: beta-glucan fragments from the rice blast disease fungus Pyricularia oryzae that elicit phytoalexin biosynthesis in suspension-cultured rice cells [J]. Plant cell, 2000, 12: 817-826.
[26] Umemoto N, Kakitani M, Iwamatsu A, et al. The structure and function of a soybean beta-glucan-elicitor-binding protein [J]. P Natl Acad Sci USA, 1997, 94: 1029-1034.
[27] Daxberger A, Nemak A, Mithofer A, et al. Activation of members of a MAPK module in beta-glucan elicitor-mediated non-host resistance of soybean [J]. Planta, 2007, 225: 1559-1571.
[28] Miyanishi N, Iwamoto Y, Watanabe E, et al. Induction of TNF-αproduction from human peripheral blood monocytes withβ-1,3-glucan oligomer prepared from laminarin withβ-1,3-glucanase from Bacillus clausii NM-1 [J]. J Biosci Bioeng, 2003, 95: 192-195.
[29] Vetvicka V, Saraswat-Ohri S, Vashishta A, et al. New 4-deoxy-1,3-β-D-glucan-based oligosaccharides and their immunostimulating potential [J]. Carbohyd Res, 2011, 346: 2213-2221.
[30] Jamois F, Ferrieres V, Guegan J P, et al. Glucan-like synthetic oligosaccharides: iterative synthesis of linear oligo-β-(1,3)-glucans and immunostimulatory effects [J]. Glycobiology, 2005, 15: 393-407.
[31] Amemura A, Hisamatsu M, Harada T. Spontaneous mutation of polysaccharide production in Alcaligenes faecalis var. myxogenes 10C3 [J]. Appl Environ Microbiol, 1977, 34: 617-620.
[32] Lee J W, Yeomans W G, Allen A L, et al. Exopolymers from curdlan production: Incorporation of glucose-related sugars by Agrobacterium sp. strain ATCC 31749 [J]. Can J Microbiol, 1997, 43: 149-156.
[33] Ghai S K. Compositional studies on succinoglycan-like extracellular water-soluble Rhizobium polysaccharides [J]. Acta Microbiol Pol, 1981, 30: 133-141.
[34] Kenyon W J, Buller C S. Structural analysis of the curdlan-like exopolysaccharide produced by Cellulomonas flavigena KU [J]. J Ind Microbiol Biotechnol, 2002, 29: 200-203.
[35] Ohno N, Uchiyama M, Tsuzuki A, et al. Solubilization of yeast cell-wallβ-1,3-D-glucan by sodium hypochlorite oxidation and dimethyl sulfoxide extraction [J]. Carbohydr Res, 1999, 316: 161-172.
[36] Nanba H, Hamaguchi A, Kuroda H. The chemical structure of an antitumor polysaccharide in fruit bodies of Grifola frondosa (maitake) [J]. Chem Pharm Bull (Tokyo), 1987, 35: 1162-1168.
[37] Suzuki I, Hashimoto K, Oikawa S, et al. Antitumor and immunomodulating activities of a beta-glucan obtained from liquid-cultured Grifola frondosa [J]. Chem Pharm Bull, 1989, 37: 410-413.
[38] Fukuoka F, Nakanishi M, Shibata S, et al. Polysaccharides in lichens and fungi. II. Anti-tumor activities on sarcoma-180 of the polysaccharide preparations from Gyrophora esculenta miyoshi, Cetraria islandica (L.) Ach. var. orientalis asahina, and some other lichens [J]. Gann, 1968, 59: 421-432.
[39] Miyazaki T, Oikawa N, Yadomae T, et al. Relationship between the chemical structure and anti-tumour activity of glucans prepared from Grifora umbellata [J]. Carbohyd Res, 1979, 69: 165-170.
[40] Miyazaki T, Oikawa N, Yamada H, et al. Structural examination of antitumour, water-soluble glucans from Grifora umbellata by use of four types of glucanase [J]. Carbohyd Res, 1978, 65: 235-243.
[41] Zheng R, Jie S, Hanchuan D, et al. Characterization and immunomodulating activities of polysaccharide from Lentinus edodes [J]. Int Immunopharmacol, 2005, 5: 811-820.
[42] Zhang L, Surenjav U, Xu X J, et al. Effects of molecular structure on antitumor activities ofβ- (1,3) -D-glucans from different Lentinus Edodes [J]. Carbohydr Polym, 2006, 63: 97-104.
[43] Tabata K, Ito W, Kojima T, et al. Ultrasonic degradation of schizophyllan, an antitumor polysaccharide produced by Schizophyllum commune Fries [J]. Carbohydr Res, 1981, 89: 121-135.
[44] Hashimoto K, Suzuki I, Yadomae T. Oral administration of SSG, aβ-glucan obtained from Sclerotinia sclerotiorum, affects the function of Peyer's patch cells [J]. Int J Immunopharmacol, 1991, 13: 437-442.
[45] Ohno N, Suzuki I, Yadomae T. Structure and antitumor activity of a beta-1,3-glucan isolated from the culture filtrate of Sclerotinia sclerotiorum IFO 9395[J]. Chem Pharm Bull, 1986, 34: 1362-1365.
[46] Stuart I M, Loi L, Fincher G B. Development of (1,3-1,4)-β-D-glucan endohydrolase isoenzymes in isolated scutella and aleurone layers of barley (Hordeum vulgare) [J]. Plant Physiol, 1986, 80: 310-314.
[47] Tsai C M, Hassid W Z. Solubilization and separation of uridine diphospho-D-glucose:β-1, 4)-glucan and uridine diphospho-D-glucose:β-(1,3-glucan glucosyltransferases from coleoptiles of Avena sativa [J]. Plant Physiol, 1971, 47: 740-744.
[48] Lai D M, Hoj P B, Fincher G B. Purification and characterization of 1,3-1,4-β-glucan endohydrolases from germinated wheat (Triticum aestivum) [J]. Plant Mol Biol, 1993, 22: 847-859.
[49] Kim M K, Ryu K E, Choi W A, et al. Enhanced production ofβ-1 ,3-glucan by a mutant strain of Agrobacterium species [J]. Biochem Eng J, 2003, 16: 163-168.
[50] West T P. Elevated curdlan production by a mutant of Agrobacterium sp. ATCC 31749 [J]. J Basic Microb, 2009, 49: 589-592.
[51] Zheng Z Y, Lee A W, Zhan X B, et al. Effect of metabolic structures and energy requirements on curdlan production by Alcaligenes faecalis [J]. Biotechnol Bioprocess Eng, 2007, 12: 359-365.
[52] Wu J, Zhan X, Liu H, et al. Enhanced production of curdlan by Alcaligenes faecalis by selective feeding with ammonia water during the cell growth phase of fermentation [J]. Chi J Biotechnol, 2008, 24: 1035-1039.
[53] Yu L, Wu J, Liu J, et al. Enhanced curdlan production in Agrobacterium sp. ATCC 31749 by addition of low-polyphosphates [J]. Biotechnol Bioproc Eng, 2011, 16: 34-41.
[54] Zhang H T, Zhan X B, Zheng Z Y, et al. New strategy for enhancement Curdlan biosynthesis in Alcaligenes faecalis by activating gene expression [C], Bioinformat Biomed Engin, 2010:1-5.
[55] Lawford H, Keenan J, Phillips K, et al. Influence of bioreactor design on the rate and amount of curdlan-type exopolysaccharide production by Alcaligenes faecalis [J]. Biotechnol Lett, 1986, 8: 145-150.
[56]Lee J H, Lee I Y. Optimization of uracil addition for curdlan (β-1,3-glucan) production by Agrobacterium sp. [J]. Biotechnol Lett, 2001, 23: 1131-1134.
[57]Lee J H, Park Y H. Optimal production of curdlan by Agrobacterium sp. with feedback inferential control of optimal pH profile [J]. Biotechnol Lett, 2001, 23: 525-530.
[58] West T P. Pyrimidine base supplementation effects curdlan production in Agrobacterium sp. ATCC 31749 [J]. J Basic Microb, 2006, 46: 153-157.
[59]Lee I Y, Kim M K, Lee J H, et al. Influence of agitation speed on production of curdlan by Agrobacterium species[J]. Bioprocess Eng, 1999, 20: 283-287.
[60]Lawford H, Keenan J, Phillips K, et al. Influence of bioreactor design on the rate and amount of curdlan-type exopolysaccharide production by Alcaligenes faecalis[J]. Biotechnol lett, 1986, 8: 145-150.
[61]Lakhwala F,Sofer S. Design considerations for an immobilized cell bioreactor operating in a batch recirculation mode[J]. J Chem Technol Biotechnol, 1991, 52: 499-509.
[62]Weyand B, Israelowitz M, von Schroeder H P, et al. Fluid dynamics in bioreactor design: considerations for the theoretical and practical approach[J]. Adv Biochem Eng Biotechnol, 2009, 112: 251-268.
[63] Yu P, Lee T S, Yan Z, Low Ho T. Fluid dynamics and oxygen transport in a micro-bioreactor with a tissue engineering scaffold[J]. Int J Heat Mass Transf, 2009, 52:316-327
[64] Mischnick P, Evers B, Thiem J. Analysis of oligosaccharides containing 2-deoxy-alpha-D-arabino-hexosyl residues by the reductive-cleavage method [J]. Carbohydr Res, 1994, 264: 293-304.
[65] Sasaki A. Isolation and characterization of serologically active phosphatidylinositol oligomannosides of Mycobacterium tuberculosis [J]. J Biochem-Tokyo, 1975, 78: 547-554.
[66] Anumula K R, Taylor P B. A comprehensive procedure for preparation of partially methylated alditol acetates from glycoprotein carbohydrates [J]. Anal Biochem, 1992, 203: 101-108.
[67] Rudd P M, Marino K, Lane J A, et al. Method for milk oligosaccharide profiling by 2-aminobenzamide labeling and hydrophilic interaction chromatography [J]. Glycobiology, 2011, 21: 1317-1330.
[68] Hayes B K,Varki A. Fractionation and analysis of neutral oligosaccharides by HPLC [J]. Curr Protoc Mol Biol, 2001, 17.21.9–17.21.13
[69] Lo-Guidice J M, Lhermitte M. HPLC of oligosaccharides in glycobiology [J]. Biomed Chromatogr, 1996, 10: 290-296.
[70] Montgomery H, Tanaka K, Belgacem O. Glycation pattern of peptides condensed with maltose, lactose and glucose determined by ultraviolet matrix-assisted laser desorption/ionization tandem mass spectrometry [J]. Rapid Commun Mass Spectrom, 2010, 24: 841-848.
[71] An H J, Lebrilla C B. Structure elucidation of native N- and O-linked glycans by tandem mass spectrometry (tutorial) [J]. Mass Spectrom Rev, 2011, 30: 560-578.
[72] Laremore T N, Leach F E, Solakyildirim K, et al. Glycosaminoglycan characterization by electrospray ionization mass spectrometry including fourier transform mass spectrometry [J]. Methods Enzymol, 2010, 478: 79-108.
[73] Chen S, Xu J, Xue C, et al. Sequence determination of a non-sulfated glycosaminoglycan-like polysaccharide from melanin-free ink of the squid Ommastrephes bartrami by negative-ion electrospray tandem mass spectrometry and NMR spectroscopy [J]. Glycoconj J, 2008, 25: 481-492.
[74] Yu G, Zhao X, Yang B, et al. Sequence determination of sulfated carrageenan-derived oligosaccharides by high-sensitivity negative-ion electrospray tandem mass spectrometry [J]. Anal Chem, 2006, 78: 8499-8505.
[75] Zanetta J P, Pons A, Richet C, et al. Sequential GC/MS analysis of sialic acids, monosaccharides, and amino acids of glycoproteins on a single sample as heptafluorobutyrate derivatives [J]. Biochemistry, 2003, 42: 8342-8353.
[76] Kacurakova M, Mathlouthi M. FTIR and laser-Raman spectra of oligosaccharides in water: characterization of the glycosidic bond [J]. Carbohyd Res, 1996, 284: 145-157.
[77] Kanou M, Nakanishi K, Hashimoto A, et al. Influences of monosaccharides and its glycosidic linkage on infrared spectral characteristics of disaccharides in aqueous solutions [J]. Appl Spectrosc, 2005, 59: 885-892.
[78] Furuki T. Effect of molecular structure on thermodynamic properties of carbohydrates. A calorimetric study of aqueous di- and oligosaccharides at subzero temperatures [J]. Carbohyd Res, 2002, 337: 441-450.
[79] Tul'chinsky V M, Zurabyan S E, Asankozhoev K A, et al. Study of the infrared spectra of oligosaccharides in the region 1,000-40 cm-1 [J]. Carbohyd Res, 1976, 51: 1-8.
[80] Domenech J, Prieto A, Gomez-Miranda B, et al. Structure of fungal polysaccharides isolated from the cell-wall of three strains of Verticillium fungicola [J]. Carbohydr Polym, 2002, 50: 209-212.
[81] Roslund M U, Sawen E, Landstrom J, et al. Complete 1H and 13C NMR chemical shift assignments of mono-, di-, and trisaccharides as basis for NMR chemical shift predictions of polysaccharides using the computer program casper [J]. Carbohyd Res, 2011, 346: 1311-1319.
[82] Lundborg M,Widmalm G. Structural analysis of glycans by NMR chemical shift prediction [J]. Anal Chem, 2011,83:1514-1517
[83] Feizi T, Fazio F, Chai W, et al. Carbohydrate microarrays - a new set of technologies at the frontiers of glycomics [J]. Curr Opin Struct Biol, 2003, 13: 637-645.
[84] Palma A S, Feizi T, Zhang Y, et al. Ligands for the beta-glucan receptor, Dectin-1, assigned using "designer" microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides [J]. J Biol Chem, 2006, 281: 5771-5779.
[85] Ruffing A, Mao Z, Chen R R Z. Metabolic engineering of Agrobacterium sp. for UDP-galactose regeneration and oligosaccharide synthesis [J]. Metab Eng, 2006, 8: 465-473.
[86] Dussap, C. G., De Vita, D. and Pons, A. Modeling growth and succinoglucan production by Agrobacterium radiobacter NCIB 9042 in batch cultures[J]. Biotechnol Bioeng, 1991,38: 65–74.
[87] Lee I Y, Seo W T, Kim G J, et al. Production of curdlan using sucrose or sugar cane molasses by two-step fed-batch cultivation of Agrobacterium species [J]. J Ind Microbiol Biotechnol, 1997, 18: 255-259.
[8] Jin L H, Um H J, Yin C J, et al. Proteomic analysis of curdlan-producing Agrobacterium sp. in response to pH downshift [J]. J Biotechnol, 2008, 138: 80-87.
[89] Trubitsin B V, Ptushenko V V, Koksharova O A, et al. EPR study of electron transport in the cyanobacterium Synechocystis sp. PCC 6803: Oxygen-dependent interrelations between photosynthetic and respiratory electron transport chains [J]. BBA-Bioenergetics, 2005, 1708: 238-249.
[90] Awai K, Kakimoto T, Awai C, et al. Comparative genomic analysis revealed a gene for monoglucosyldiacylglycerol synthase, an enzyme for photosynthetic membrane lipid synthesis in cyanobacteria [J]. Plant Physiol, 2006, 141: 1120-1127.
[91] Johnston M, Cliften P F, Hillier L W, et al. Surveying Saccharomyces genomes to identify functional elements by comparative DNA sequence analysis [J]. Genome Res, 2001, 11: 1175-1186.
[92] Rinner O, Morgenstern B. AGenDA: gene prediction by comparative sequence analysis [J]. In Silico Biol, 2002, 2: 195-205.
[93] Wood D W, Setubal J C, Kaul R, et al. The genome of the natural genetic engineer Agrobacterium tumefaciens C58 [J]. Science, 2001, 294: 2317-2323.
[94] Slater S C, Goldman B S, Goodner B, et al. Genome sequences of three Agrobacterium biovars help elucidate the evolution of multichromosome genomes in bacteria [J]. J Bacteriol, 2009, 191: 2501-2511.
[95] Wheatcroft R,Watson R J. A positive strain identification method for Rhizobium meliloti [J]. Appl Environ Microbiol, 1988, 54: 574-576.
[96] Altschul S, Madden T, Schaffer A, et al. Gapped BLAST and PSI-BLAST: A new generation of proteindatabase search programs [J]. FASEB J, 1998, 12: A1326-A1326.
[97]Wu M, Eisen J A. A simple, fast, and accurate method of phylogenomic inference [J]. Genome Biology, 2008, 9: R151.
[98] Dereeper A, Guignon V, Blanc G, et al. Phylogeny.fr: robust phylogenetic analysis for the non-specialist [J]. Nucleic Acids Res, 2008, 36: W465-W469.
[99] Alpes I, Scherer S, B?ger P. The respiratory NADH dehydrogenase of the cyanobacterium Anabaena variabilis: purification and characterization [J]. BBA-Bioenergetics, 1989, 973: 41-46.
[100]Steimle S, Pohl T,Friedrich T. Assembly of the Escherichia coli NADH: ubiquinone oxidoreductase (complex I) [J]. BBA-Bioenergetics, 2010, 1797: 23-23.
[101] Braun M, Bungert S, Friedrich T. Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli[J].Biochem, 1998, 37:1861-1867.
[102]Friedrich T, Schneider D, Pohl T, et al. Assembly of the Escherichia coli NADH: ubiquinone oxidoreductase (complex I) [J]. BBA-Bioenergetics, 2008, 1777: 735-739.
[103]Cecchini G, Schroder I, Gunsalus R P, et al. Succinate dehydrogenase and fumarate reductase from Escherichia coli [J]. BBA-Bioenergetics, 2002, 1553: 140-157.
[104]Westenberg D J, Guerinot M L. Succinate dehydrogenase (Sdh) from Bradyrhizobium japonicum is closely related to mitochondrial Sdh [J]. J Bacteriol, 1999, 181: 4676-4679.
[105]Meganathan R. Ubiquinone biosynthesis in microorganisms [J]. FEMS Microbiol Lett, 2001, 203: 131-139.
[106]Poon W W, Davis D E, Ha H T, et al. Identification of Escherichia coli ubiB, a gene required for the first monooxygenase step in ubiquinone biosynthesis [J]. J Bacteriol, 2000, 182: 5139-5146.
[107]Rubin H, Kana B D, Weinstein E A, et al. Characterization of the cydAB-encoded cytochrome bd oxidase from Mycobacterium smegmatis [J]. J Bacteriol, 2001, 183: 7076-7086.
[108]Smith A, Hill S, Anthony C. The purification, characterization and role of the d-type cytochrome oxidase of Klebsiella pneumoniae during nitrogen fixation [J]. J Gen Microbiol, 1990, 136: 171-180.
[109]Chepuri V, Lemieux L, Au D C T, et al. The sequence of the cyo operon indicates substantial structural similarities between the cytochrome-o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome-c oxidases [J]. J Biol Chem, 1990, 265: 11185-11192.
[110]Mogi T, Saiki K, Anraku Y. Biosynthesis and functional role of haem O and haem A [J]. Mol Microbiol, 1994, 14: 391-398.
[111]Williams H D, Hubbard J A M, Nugent J H A, et al. Functional size measurements of the ubiquinol oxidase activity of the cytochrome-o terminal oxidase complex of Escherichia coli [J]. Biochem J, 1991, 276: 555-557.
[112]Preisig O, Zufferey R, Thony-Meyer L, et al. A high-affinity cbb3-type cytochrome oxidase terminates the symbiosis-specific respiratory chain of Bradyrhizobium japonicum [J]. J Bacteriol, 1996, 178: 1532-1538.
[113]Saraste M, Metso T, Nakari T, et al. The Bacillus subtilis cytochrome-c oxidase: variations on a conserved protein theme [J]. Eur J Biochem/FEBS, 1991, 195: 517-525.
[114]Bott M, Niebisch A. The respiratory chain of corynebacterium glutamicum [J]. J Biotechnol, 2003, 104: 129-153.
[115]Hill B C, Greenwood C. The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature: evidence for new pathways of electron transfer [J]. Biochem J, 1984, 218: 913-921.
[116]Bott M, Bolliger M, Hennecke H. Genetic analysis of the cytochrome c-aa3 branch of the Bradyrhizobium japonicum respiratory chain [J]. Mol Microbiol, 1990, 4: 2147-2157.
[117]Richter O M,Ludwig B. Electron transfer and energy transduction in the terminal part of the respiratory chain - lessons from bacterial model systems [J]. Biochim Biophys Acta, 2009, 1787: 626-634.
[118]Yumoto I. Bioenergetics of alkaliphilic Bacillus spp [J]. J Biosci Bioeng, 2002, 93: 342-353.
[119]Slater S C, Goldman B S, Goodner B, et al. Genome sequences of three Agrobacterium biovars help elucidate the evolution of multichromosome genomes in bacteria [J]. J Bacteriol, 2009, 191: 2501-2511.
[120]Minghetti K C, Gennis R B. The two terminal oxidases of the aerobic respiratory chain of Escherichia coli each yield water and not peroxide as a final product [J]. Biochem Bioph Res Co, 1988, 155: 243-248.
[121]Matsushita K, Ohnishi T,Kaback H R. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain [J]. Biochemistry, 1987, 26: 7732-7737.
[122]Miller M J, Gennis R B. The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli [J]. J Biol Chem, 1985, 260: 14003-14008.
[123]Miller M J, Gennis R B. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain [J]. J Biol Chem, 1983, 258: 9159-9165.
[124]Arslan E, Kannt A, Thony-Meyer L, et al. The symbiotically essential cbb3-type oxidase of Bradyrhizobium japonicum is a proton pump [J]. FEBS Lett, 2000, 470: 7-10.
[125]Bundschuh F A, Hoffmeier K, Ludwig B. Two variants of the assembly factor Surf1 target specific terminal oxidases in Paracoccus denitrificans [J]. Biochim Biophys Acta, 2008, 1777: 1336-1343.
[126]de Gier J W, Lubben M, Reijnders W N, et al. The terminal oxidases of Paracoccus denitrificans [J]. Mol Microbiol, 1994, 13: 183-196.
[127]Karnezis T, Epa V C, Stone B A, et al. Topological characterization of an inner membraneβ-1,3 -D-glucan (curdlan) synthase from Agrobacterium sp. strain ATCC31749 [J]. Glycobiology, 2003, 13: 693-706.
[128]Ruffing A M, Castro-Melchor M, Hu W S, et al. Genome sequence of the curdlan-producing Agrobacterium sp. strain ATCC 31749 [J]. J Bacteriol, 2011, 193: 4294-4295.
[129]Zhang Z, Qu Y, Zhang X, et al. Effects of oxygen limitation on xylose fermentation, intracellularmetabolites, and key enzymes of Neurospora crassa AS3.1602 [J]. Appl Biochem Biotechnol, 2008, 145: 39-51.
[130]Verbelen P J, Saerens S M, Van Mulders S E, et al. The role of oxygen in yeast metabolism during high cell density brewery fermentations [J]. Appl Microbiol Biotechnol, 2009, 82: 1143-1156.
[131]Yang S, Tschaplinski T J, Engle N L, et al. Transcriptomic and metabolomic profiling of Zymomonas mobilis during aerobic and anaerobic fermentations [J]. BMC Genomics, 2009, 10: 34.
[132]Sandoval-Basurto E A, Gosset G, Bolivar F, et al. Culture of Escherichia coli under dissolved oxygen gradients simulated in a two-compartment scale-down system: metabolic response and production of recombinant protein[J]. Biotechnol Bioeng, 2005, 89: 453-463.
[133]Portilho M, Matioli G, Zanin G M, et al. Production of insoluble exopolysaccharide of Agrobacterium sp. (ATCC 31749 and IFO 13140) [J]. Appl Biochem Biotechnol, 2006, 129-132: 864-869.
[134]West T P. Pyrimidine base supplementation effects curdlan production in Agrobacterium sp. ATCC 31749 [J]. J Basic Microb, 2006, 46: 153-157.
[135]Lawford H, Rousseau J. Effect of oxygen on the rate ofβ-1,3-glucan microbial exopolysaccharide production [J]. Biotechnol Lett, 1989, 11: 125-130.
[136]Lawford H, Rousseau J. Production ofβ-1,3-glucan exopolysaccharide in low shear systems [J]. Appl Biochem Biotechnol, 1992, 34-35: 597-612.
[137]Pitcher D G, Saunders N A, Owen R J. Rapid extraction of bacterial genomic DNA with guanidium thiocyanate [J]. Lett Appl Microbiol, 1989, 8: 151-156.
[138]Zhang H, Setubal J C, Zhan X, et al. Component identification of electron transport chains in curdlan-producing Agrobacterium sp. ATCC 31749 and its genome-specific prediction using comparative genome and phylogenetic trees analysis [J]. J Ind Microbiol Biotechnol, 2011, 38: 667-677.
[139]Kongruang S, Han M J, Breton C I, et al. Quantitative analysis of cellulose-reducing ends [J]. Appl Biochem Biotechnol, 2004, 113-116: 213-231.
[140]Rau U, Gura E, Olszewski E, et al. Enhanced glucan formation of filamentous fungi by effective mixing, oxygen limitation and fed-batch processing[J]. J Ind Microbiol, 1992, 9: 19-25.
[141]Gummadi S N, Kumar K. Production of extracellular water insolubleβ-1,3-glucan (curdlan) from Bacillus sp. SNC07 [J]. Biotechnol Bioprocess Eng, 2005, 10: 546-551.
[142]Unden G, Trageser M. Oxygen regulated gene expression in Escherichia coli: control of anaerobic respiration by the FNR protein [J]. Antonie Van Leeuwenhoek, 1991, 59: 65-76.
[143]Cotter P A, Chepuri V, Gennis R B, et al. Cytochrome o (cyoABCDE) and d (cydAB) oxidase gene expression in Escherichia coli is regulated by oxygen, pH, and the fnr gene product [J]. J Bacteriol, 1990, 172: 6333-6338.
[144]Mengin-Lecreulx D,van Heijenoort J. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli [J]. J Biol Chem, 1996, 271: 32-39.
[145]Thoden J B, Holden H M. The molecular architecture of glucose-1-phosphate uridylyltransferase [J].Protein Sci, 2007, 16: 432-440.
[146]Lara A R, Leal L, Flores N, et al. Transcriptional and metabolic response of recombinant Escherichia coli to spatial dissolved oxygen tension gradients simulated in a scale-down system [J]. Biotechnol Bioeng, 2006, 93: 372-385.
[147]Shalel-Levanon S, San K Y, Bennett G N. Effect of oxygen, and ArcA and FNR regulators on the expression of genes related to the electron transfer chain and the TCA cycle in Escherichia coli [J]. Metab Eng, 2005, 7: 364-374.
[148]Kim M K, Lee I Y, Lee J H, et al. Residual phosphate concentration under nitrogen-limiting conditions regulates curdlan production inAgrobacterium species[J]. J Ind Microbiol Biotechnol, 2000, 25: 180-183.
[149]Crosson S, McGrath P T, Stephens C, et al. Conserved modular design of an oxygen sensory/signaling network with species-specific output [J]. P Natl Acad Sci USA, 2005, 102: 8018-8023.
[150]Biel A J, Marrs B L. Transcriptional regulation of several genes for Bacteriochlorophyll biosynthesis in Rhodopseudomonas capsulata in response to oxygen [J]. J Bacteriol, 1983, 156: 686-694.
[151]Kwast K E, Burke P V,Poyton R O. Oxygen sensing and the transcriptional regulation of oxygen-responsive genes in yeast [J]. J Exp Biol, 1998, 201: 1177-1195.
[152]Uziel O, Borovok I, Schreiber R, et al. Transcriptional regulation of the Staphylococcus aureus thioredoxin and thioredoxin reductase genes in response to oxygen and disulfide stress [J]. J Bacteriol, 2004, 186: 326-334.
[153]Czyzyk-Krzeska M F. Molecular aspects of oxygen sensing in physiological adaptation to hypoxia [J]. Respir Physiol, 1997, 110: 99-111.
[154]Bunn H F, Poyton R O. Oxygen sensing and molecular adaptation to hypoxia [J]. Physiol Rev, 1996, 76: 839-885.
[155]Lois A F, Ditta G S, Helinski D R. The oxygen sensor FixL of Rhizobium meliloti is a membrane protein containing four possible transmembrane segments [J]. J Bacteriol, 1993, 175: 1103-1109.
[156]Willems A, Collins M D. Phylogenetic analysis of rhizobia and agrobacteria based on 16S rRNA gene sequences [J]. Int J Syst Bacteriol, 1993, 43: 305-313.
[157]Young J M, Kuykendall L D, Martinez-Romero E, et al. A revision of Rhizobium Frank 1889, with an emended description of the genus, and the inclusion of all species of Agrobacterium Conn 1942 and Allorhizobium undicola de Lajudie et al. 1998 as new combinations: Rhizobium radiobacter, R. rhizogenes, R. rubi, R. undicola and R. vitis [J]. Int J Syst Evol Microbiol, 2001, 51: 89-103.
[158]Liu Y S, Wu H Y, Ho K P. Characterization of oxygen transfer conditions and their effects on Phaffia rhodozyma growth and carotenoid production in shake-flask cultures [J]. Biochem Eng J, 2006, 27: 331-335.
[159]Kaya-Celiker H, Angardi V, Calik P. Regulatory effects of oxygen transfer on overexpression of recombinant benzaldehyde lyase production by Escherichia coli BL21 (DE3) [J]. Biotechnol J, 2009,4: 1066-1076.
[160]Fazenda M L, Harvey L M, McNeil B. Effects of dissolved oxygen on fungal morphology and process rheology during fed-batch processing of Ganoderma lucidum [J]. J Microbiol Biotechnol, 2010, 20: 844-851.
[161]Calik P, Yilgor P, Ayhan P, et al. Oxygen transfer effects on recombinant benzaldehyde lyase production [J]. Chem Eng Sci, 2004, 59: 5075-5083.
[162]Fredlund E, Blank L M, Schnurer J, et al. Oxygen- and glucose-dependent regulation of central carbon metabolism in Pichia anomala [J]. Appl Environ Microb, 2004, 70: 5905-5911.
[163]Martin A B, Alcon A, Santos V E, et al. Production of a biocatalyst of Pseudomonas putida CECT5279 for DBT biodesulfurization: Influence of the operational conditions [J]. Energy Fuels, 2005, 19: 775-782.
[164]Kim B S, Jung I D, Kim J S, et al. Curdlan gels as protein drug delivery vehicles [J]. Biotechnol Lett, 2000, 22: 1127-1130.
[165]Garc?a?-Ochoa F, Castro E G,Santos V E. Oxygen transfer and uptake rates during xanthan gum production [J]. Enzyme Microb Technol, 2000, 27: 680-690.
[166]Wang Y, McNeil B. Dissolved oxygen and the scleroglucan fermentation process [J]. Biotechnol Lett, 1995, 17: 257-262.
[167]Levander F, Svensson M, Radstrom P. Enhanced exopolysaccharide production by metabolic engineering of Streptococcus thermophilus [J]. Appl Environ Microb, 2002, 68: 784-790.
[168]Chang Y K, Kim H H, Na J G, et al. Effects of dissolved oxygen control on cell growth and exopolysaccharides production in batch culture of Agaricus blazei [J]. Korean J Chem Eng, 2005, 22: 80-84.
[169]Kim M K, Lee I Y, Ko J H, et al. Higher intracellular levels of uridinemonophosphate under nitrogen-limited conditions enhance metabolic flux of curdlan synthesis in Agrobacterium species [J]. Biotechnol Bioeng, 1999, 62: 317-323.
[170]Fu Y Q, Li S, Chen Y, et al. Enhancement of fumaric acid production by Rhizopus oryzae using a two-stage dissolved oxygen control strategy [J]. Appl Biochem Biotechnol, 2010, 162: 1031-1038.
[171]Goodridge H S, Wolf A J, Underhill D M.β-glucan recognition by the innate immune system [J]. Immunol Rev, 2009, 230: 38-50.
[172]Albert O, Toubas D, Strady C, et al. Reactivity of 1,3-β-D-glucan assay in bacterial bloodstream infections [J]. Eur J Clin Microbiol Infect Dis, 2011 DOI: 10.1007/s10096-011-1244-8
[173]Marty F M, Lowry C M, Lempitski S J, et al. Reactivity ofβ-1,3 -d-glucan assay with commonly used intravenous antimicrobials [J]. Antimicrob Agents Chemother, 2006, 50: 3450-3453.
[174]Chan G C F, Chan W K, Sze D M Y. The effects ofβ-glucan on human immune and cancer cells [J]. J Hematol Oncol, 2009, 2: 25.
[175]Murphy E A, Davis J M, Carmichael M D. Immune modulating effects ofβ-glucan [J]. Curr Opin Clin Nutr Metab Care, 2010, 13: 656-661.
[176]Taylor P R, Brown G D, Reid D M, et al. Theβ-glucan receptor, dectin-1, is predominantly expressed on the surface of cells of the monocyte/macrophage and neutrophil lineages [J]. J Immunol, 2002, 169: 3876-3882.
[177]Brown G D, Taylor P R, Reid D M, et al. Dectin-1 is a majorβ-glucan receptor on macrophages [J]. J Exp Med, 2002, 196: 407-412.
[178]Xia Y, Vetvicka V, Yan J, et al. The beta-glucan-binding lectin site of mouse CR3 (CD11b/CD18) and its function in generating a primed state of the receptor that mediates cytotoxic activation in response to iC3b-opsonized target cells [J]. J Immunol, 1999, 162: 2281-2290.
[179]Cheung N K V, Modak S, Vickers A, et al. Orally administeredβ-glucans enhance anti-tumor effects of monoclonal antibodies [J]. Cancer Immunol Immun, 2002, 51: 557-564.
[180]Li B, Cai Y, Qi C, et al. Orally administered particulateβ-glucan modulates tumor-capturing dendritic cells and improves antitumor T-cell responses in cancer [J]. Clin Cancer Res, 2010, 16: 5153-5164.
[181]刘高强.灵芝多糖的抗癌构效关系及其抗癌作用机制[J].菌物学报, 2006, 25:430-438.
[182]李万坤.糖原组学研究进展——β-葡聚糖的结构和功能的研究进展[J].中国畜牧兽医, 2007, 34:152-155.
[183]Palma A S, Liu Y, Muhle-Goll C, et al. Multifaceted approaches including neoglycolipid oligosaccharide microarrays to ligand discovery for malectin [J]. Methods Enzymol, 2010, 478: 265-286.
[184]Yu G, Zhang Y, Zhang Z, et al. Effect and limitation of excess ammonium on the release of O-glycans in reducing forms from glycoproteins under mild alkaline conditions for glycomic and functional analysis [J]. Anal Chem, 2010, 82: 9534-9542.
[185]Fischer D, Geyer A, Loos E. Occurrence of glucosylsucrose [α-D-glucopyranosyl- 1,2-α-D-glucopyranosyl-1,2-β-D-fructofuranoside] and glucosylated homologues in cyanobacteria. Structural properties, cellular contents and possible function as thermoprotectants [J]. FEBS J, 2006, 273: 137-149.
[186]Roset M S, Ciocchini A E, Ugalde R A, et al. The Brucella abortus cyclicβ-1,2-glucan virulence factor is substituted with O-ester-linked succinyl residues [J]. J Bacteriol, 2006, 188: 5003-5013.
[187]Zhang P, Zhang L, Cheng S. Solution properties of anα-1,3-D-glucan from Lentinus edodes and its sulfated derivatives [J]. Carbohydr Res, 2002, 337: 155-160.
[188]Zhang L, Li X L, Xu X J, et al. Correlation between antitumor activity, molecular weight, and conformation of lentinan [J]. Carbohyd Res, 2005, 340: 1515-1521.
[189]Fischer D,Geyer A. NMR analysis of bioprotective sugars: Sucrose and oligomeric 1,2-α-D-glucopyranosyl-1,2-β-D-fructofuranosides [J]. Bioactive Conformation I, 2007, 272: 169-185.
[190]Chen S, Xu J, Xue C, et al. Sequence determination of a non-sulfated glycosaminoglycan-like polysaccharide from melanin-free ink of the squid Ommastrephes bartrami by negative-ion electrospray tandem mass spectrometry and NMR spectroscopy [J]. Glycoconjugate J, 2008, 25:481-492.
[191]Kogelberg H, Piskarev V E, Zhang Y, et al. Determination by electrospray mass spectrometry and 1H-NMR spectroscopy of primary structures of variously fucosylated neutral oligosaccharides based on the iso-lacto-N-octaose core [J]. Eur J Biochem, 2004, 271: 1172-1186.
[192]Liu Y, Chai W, Childs R A, et al. Preparation of neoglycolipids with ring-closed cores via chemoselective oxime-ligation for microarray analysis of carbohydrate-protein interactions [J]. Methods Enzymol, 2006, 415: 326-340.
[193]Fontes C M G A, Ponte P I P, Reis T C, et al. A family 6 carbohydrate-binding module potentiates the efficiency of a recombinant xylanase used to supplement cereal-based diets for poultry [J]. Br Poult Sci, 2004, 45: 648-656.
[194]Henshaw J L, Bolam D N, Pires V M R, et al. The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities [J]. J Biol Chem, 2004, 279: 21552-21559.
[195]Pires V M R, Henshaw J L, Prates J A M, et al. The crystal structure of the family 6 carbohydrate binding module from Cellvibrio mixtus endoglucanase 5A in complex with oligosaccharides reveals two distinct binding sites with different ligand specificities [J]. J Biol Chem, 2004, 279: 21560-21568.
[196]Leon M A, Young N M, McIntire K R. Immunochemical studies of the reaction between a mouse myeloma macroglobulin and dextrans [J]. Biochemistry, 1970, 9: 1023-1030.
[197]Crespo M S, Valera I, Ferandez N, et al. Costimulation of Dectin-1 and DC-SIGN triggers the arachidonic acid cascade in human monocyte-derived dendritic cells [J]. J Immunol, 2008, 180: 5727-5736.
[198]Holla A, Skerra A. Comparative analysis reveals selective recognition of glycans by the dendritic cell receptors DC-SIGN and Langerin [J]. Protein Eng Des Sel, 2011, 24: 659-669.
[199]Herre J, Gordon S, Brown G D. Dectin-1 and its role in the recognition of beta-glucans by macrophages [J]. Mol Immunol, 2004, 40: 869-876.
[200]Taylor P R, Brown G D, Reid D M, et al. The beta-glucan receptor, Dectin-1, is predominantly expressed on the surface of cells of the monocyte/macrophage and neutrophil lineages [J]. J Immunol, 2002, 169: 3876-3882.
[201]Apetrei N S, Calugaru A, Badulescu M M, et al. The effects of some Curdlan derivatives on Dectin-1 expression and cytokine production in human peripheral blood mononuclear cells [J]. Roum Arch Microbiol Immunol, 2010, 69: 61-66.
[202]Minari J, Mochizuki S, Matsuzaki T, et al. Enhanced cytokine secretion from primary macrophages due to Dectin-1 mediated uptake of CpG DNA/β-1,3-glucan complex [J]. Bioconjug Chem, 2011, 22: 9-15.
[203]Brown G D, Taylor P R, Tsoni S V, et al. Dectin-1 is required for beta-glucan recognition and control of fungal infection [J]. Nat Immunol, 2007, 8: 31-38
[204]Saijo S, Fujikado N, Furuta T, et al. Dectin-1 is required for host defense against Pneumocystiscarinii but not against Candida albicans [J]. Nat Immunol, 2007, 8: 39-46.
[205]Saijo S, Iwakura Y. Dectin-1 and Dectin-2 in innate immunity against fungi [J]. Int Immunol, 2011, 23: 467-472.
[206]Goodridge H S, Reyes C N, Becker C A, et al. Activation of the innate immune receptor Dectin-1 upon formation of a 'phagocytic synapse' [J]. Nature, 2011, 472: 471-475.
[207]Ferwerda B, Ferwerda G, Plantinga T S, et al. Human Dectin-1 deficiency and mucocutaneous fungal infections [J]. N Engl J Med, 2009, 361: 1760-1767.
[208]Williams D L, Adams E L, Rice P J, et al. Differential high-affinity interaction of Dectin-1 with natural or synthetic glucans is dependent upon primary structure and is influenced by polymer chain length and side-chain branching [J]. J Pharmacol Exp Ther, 2008, 325: 115-123.
[209]Geurtsen J, Chedammi S, Mesters J, et al. Identification of Mycobacterialα-glucan as a novel ligand for DC-SIGN: involvement of Mycobacterial capsular polysaccharides in host immune modulation[J]. J Immunol, 2009,183:5221-5331