真菌漆酶高效定向固定化新策略探索
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摘要
漆酶是一种含铜的多酚氧化酶,能够催化芳香胺和酚类等多种芳香化合物的氧化,同时伴随分子氧还原成水。漆酶的催化特征使其不但在木素降解、纸浆漂白、印染废水脱色与脱毒等工业和环保方面有着广泛应用,同时在生物传感器和生物燃料电池的开发上也极具应用价值。
和大多数水溶性酶一样,漆酶的固定化是实现应用价值的必要途径。
传统的酶固定化方法,大多是通过酶外表面氨基酸残基上的功能基团与载体进行作用而连接。这可能会导致酶多个位点和载体结合,破坏了酶的天然构象,使固定化酶活性大幅度下降,同时酶分子不恰当的空间取向,也可能使得固定化酶的活性位点与底物的接触受阻,使催化效率大大降低。因此,定向、高效成为酶固定化方法研究的关键。
已报道的酶定向固定化方法中,有的依靠酶与载体(修饰)之间亲和作用,有的依靠蛋白的特定的氨基酸残基与载体上对应的偶联基团之间的共价结合。目前,单一活性中心酶的定向固定化技术的研究取得了一定的进展。
漆酶是一个单链多氧化还原活性中心的大分子,这一结构特征使得固定化漆酶的催化效率在很大程度上依赖其在载体表面上的取向。就酶电极而言,不同的取向不仅影响其直接电子转移途径,还影响其生物电催化氧还原效率。因此,漆酶的高效定向固载是漆酶利用的关键。有关漆酶的定向固定化研究的报道,迄今为止仍然相对较少。因此,探索漆酶定向、高效的固定化新方法,对漆酶功能器件的开发具有重要意义。
本论文分别从漆酶自身的生物修饰和／或载体的化学修饰等不同角度,尝试建立了几种漆酶高效定向固载新策略。
一、漆酶的生物修饰
相比于蛋白本身的化学修饰,功能蛋白的定点生物修饰是实现功能蛋白定向组装的理想手段之一。目前,生物学上对漆酶基因进行克隆和序列分析已经取得了很大进展,并且实现了其高效的重组表达(或异源表达)。以此为基础,以漆酶的定向固定化为目标,本文首先利用分子生物学的方法将漆酶进行了定点生物修饰。
借助于半胱氨酸的侧链巯基和金基底形成的硫-金键常用来构建自组装修饰电极。因此在漆酶的氮端或碳端引入半胱氨酸将为漆酶的定向固定带来便利。而组氨酸的咪唑基团与金属离子的特异性亲和作用,也常常被用于蛋白的纯化和固定。
本节首先设计了一段编码Cys-(His×6)-短肽的基因序列,通过基因重组的方法,将这段序列融合到来源于Trametes sp. AH28-2的漆酶基因lacA的3'/5'端,并构建了表达载体,再经过电转化导入毕赤酵母中进行了漆酶的异源高效表达,最终成功获得了分别在N端和C端带有Cys-(His×6)-短肽的重组漆酶rLacA-N和rLacA-C。对重组漆酶进行了酶学性质表征,结果表明两种重组漆酶和非重组漆酶具有相似的酶学性质,说明对漆酶的生物修饰没有对酶本身性质产生大的影响,为后续的固定化打好了基础。
二、重组漆酶在金电极上定向固定化策略
漆酶在常规电极上的直接电子转移现象不易观察到。不仅如此,还发现随机取向漆酶的电催化氧还原伴随着中间体过氧化氢的产生,影响电子转移效率。由此可见,电极上漆酶的定向组装是提高直接电子转移效率、构建漆酶电化学生物传感器和生物燃料电池等功能器件的关键步骤。
利用重组漆酶蛋白链末端的半胱氨酸残基,与金电极形成的Au-S键,将重组漆酶定向地组装到平面金电极表面上。
酶活测量表明,固定化漆酶能够较好地保持原有的生物活性。漆酶电极的循环伏安法表征又表明,两种重组漆酶在金电极表面均发生了直接电子转移,对氧也表现出生物电催化活性。然而两种重组漆酶电极的直接电化学行为却表现出明显差异,对氧的生物电催化还原效率及其还原产物也有差异。分析表明,金电极表面上不同取向漆酶的直接电子转移途径与难易程度不一样。T1位点靠近电极表面易于漆酶对氧的生物电催化还原。
上述漆酶在电极上定向固定的研究不但有助于深化对漆酶直接电化学机制的认识,也有助于基于漆酶的生物燃料电池的研发。
三、重组漆酶在琼脂糖载体的定向固定化策略
将氮端或碳端带有His×6-短肽链的重组漆酶,通过组氨酸与Ni2+离子的螯合作用,定向地组装到氨基三乙酸-Ni2+-修饰的琼脂糖载体表面上。在这个固定化体系中,由于固定位点位于漆酶分子表面、远离漆酶活性中心,有利于漆酶结构的保持,使固定化漆酶可以保持较高的催化活性；同时多组氨酸链作为位点,也增加了固定化漆酶的稳定性；最重要的是,依靠漆酶本身定点生物修饰的氨基酸链作为固定位点,实现了漆酶取向单
一、取向可控的高效固定化。
固定化漆酶酶活测量结果表明,在相同条件下不同取向的两种固定化漆酶表现出不同的催化活性；然而酶结构的圆二色谱分析表明,不同取向漆酶的二级结构变化不大。分析表明,这可能是由于固定化T1位点的外露程度不同,导致底物的可触及性不同所致。研究结果还表明,固定化酶比游离酶有更高的热稳定性,同时具有较高的重复利用性。
四、非重组漆酶在单壁碳纳米管上亲和固定化策略
漆酶是一种糖蛋白酶,其表面的糖基可以作为固定化的位点。将固定载体——单壁碳纳米管用表面活性剂十二烷基麦芽糖苷进行表面修饰,利用伴刀豆蛋白对糖基的特异性亲和作用,同时又凭借表面活性剂对碳纳米管的分散作用,从增加碳纳米管比表面积、减少酶结构改变、增加固定化酶的稳定性等方面出发,构建了单壁碳纳米管-烷基糖苷-伴刀豆蛋白-糖蛋白酶固定化新体系。
分别以漆酶和辣根过氧化物酶为例研究,实验结果表明,这种新型固定化方法,与两种酶直接固定于碳纳米管上相比,在酶的上载量、比活力、稳定性等方面,都有很大的优势。圆二色谱和荧光光谱分析测试酶的结构变化结果表明,单壁碳纳米管-烷基糖苷-伴刀豆蛋白复合载体和单壁碳纳米管相比,对酶的结构影响较小,这也是新体系中酶的比活力较高的直接原因。
这种利用自组装方法,通过生物凝集素间接固定糖蛋白的新策略,有助于提高单壁碳纳米管上糖蛋白酶的酶学性质,为糖蛋白酶及碳纳米管的应用奠定了基础。
Laccase is a Cu-containing polyphenol oxidase, which catalyzes the oxidation of various aromatic amines and phenols with concomitant reduction of oxygen to water. The catalytic characteristics of laccase make it very useful not only in lignin degradation, pulp bleaching, dye decolorization/detoxication, and environmental protection but also in biosensor and biofuel cell development.
Similar to other enzymes, the immobilization of laccase is an important strategy for its real application. Traditionally, an enzyme is immobilized via the interaction between a support and a functional group of amino acid residue on the enzyme surface. In this way, it is possible that multiple sites of enzyme are attached on the support, resulting in a disturbed enzyme structure, decreased enzyme activity and inappropriate orientation. It may also hinder the interaction between the active site of an enzyme and its substrate, resulting in decreased activity. Therefore, the oriented and high efficient immobilization becomes the focus of recent research.
So far, some oriented immobilization strategies have been developed. Some are based on the affinity interaction between an enzyme and a support. Some are based on the covalent interaction between amino acid residue and coupling group on the support. Currently, some development on the oriented immobilization of enzymes of single active site has been achieved.
It is known that laccase is a single-chain macromolecule with multiple redox active sites. The catalytie efficiency of the immobilized laccase therefore depends largely on the strategies used for the immobilization, especially when laccase is immobilized on an electrode for the direct electron transfer and bioelectrocatalysis. It follows that high efficient and oriented immobilization of laccase is significant for the development of laccase-based functional devices. However, few works have been carried out on the oriented immobilization of laccase. This thesis presents several new strategies for high-efficient and oriented immobilization of laccase from the perspective of the bio-modification of enzyme itself and/or chemical modification of the carrier.
1. Bio-modification of laccase
Relatively speaking, the biological modification of functional proteins is more suitable than its chemical modification for the orientation assembly of proteins. So far, great progress has been made in the cloning and sequence analysis of the gene of laccase and in the high efficient heterologous expression of laccase. In present study, the molecular biology-based bio-modification of laccase is used to realize the oriented immobilization of laccase.
The self-assembly of the modified laccase on Au electrode is based on the Au-S band formed between side chain thiol of cysteine and gold substrate. Therefore, to facilitate the immobilization of laccase, the N-terminal or C-terminal is modified with cysteine. The coordination between the imidazole group of histidine and Ni2+ions has also frequently been used for purification and immobilization of protein.
In the present study, a DNA sequence of Cys-(His×6)-was first designed and then fused to the3'/5'DNA terminus of laccase from Trameters sp. AH28-2. After that an expression vector was built and electroporated into Pichia pastoris for expression. Finally, the N-terminus and C-terminus of laccase was successfully modified with Cys-(His×6)-oligopeptide.
The enzymatic property of the recombinant laccase was analyzed. The results show that the two recombinant laccases exhibit similar enzymatic properties, indicating that the biological modification has no big effect on enzyme properties and the modified laccase can be used for further immobilization.
2. Oriented immobilization of recombinant laccase on gold electrode
The direct electron transfer of laccase on common electrodes is hardly observed. It was also found that for non-oriented immobilized laccase electrode, the electrocatalytic reduction of oxygen is accompanied by the production of the intermediate H2O2, which decreases the electron transfer efficiency. Thus, the oriented immobilization of laccase on electrode is a key step for enhancing the electron transfer efficiency, and constructing high-performance biosensors and biofuel cells.
Based on the Au-S band between the cysteine residue of the recombinant laccase and gold electrode, the recombinant laccase is assembled orientationally on the gold electrode.
Enzyme activity test shows that the activity of the immobilized laccase is well-retained. Cyclic voltammetry test shows that the direct electron transfer and the bioelectroreduction of oxygen are achieved on both the electrodes modified the recombinant laccases. However, the two electrodes show different direct electrochemical behaviors. Analysis shows that laccase with different orientation on gold electrode have different electron transfer pathways and different direct electron transfer efficiency. Bioelectrocatalytic reduction of oxygen is easier for laccase modified electrode where the T1site is more close to the electrode surface. The above research is helpful to the in-depth understanding of the direct electrochemistry of laccase and also to the development of laccase-based biofuel cells.
3. Oriented immobilization of recombinant laccase on agarose
The recombinant laccase with Cysteine-6×Histidine tag at N-terminus and C-terminus is immobilized on the surface of NTA-Ni2+-modified agarose via the chelation between the histidine residue and Ni2+ion. In this system, the immobilization site is close to laccase surface but distant away from laccase active site, which is beneficial for the structure retention and high catalytic activity. The multiple immobilization sites also enhance the stability. More importantly, the bio-modified amino acid chain realizes the oriented immobilization with adjustable orientation.
The enzyme activity test shows that the laccases with different orientations show different activities under the same testing conditions. Circular dichroism spectrum shows that the secondary structure changes little for the two recombinants prior to or after the immobilization. Analysis shows that it is the orientation that makes the exposure of T1site of laccase to the outer solution different, which results in different accessibility of the same substrate to the T1site and therefore different activity. It is also found after immobilization, thermal stability enhances and reusableility is high.
4. Efficient immobilization of non-recombinant laccase on single wall carbon nanotube
Laccase is one of the glucoproteinases. The glycosyl on the surface can be used as sites for immobilization. In the present study, the single wall carbon nanotube is first modified with surfactant (alkyl polyglucoside) to disperse the nano tubes and increase the specific surface area. Based on the affinity between concanavalin A and glycosyl, laccase is then immobilized on carbon nanotubes, forming a new conjugate of single wall carbon nanotube-(n-dodecyl β-D-maltoside)-concanavalin A-glucoproteinases with little structure change and high stability.
The experimental results show that the new immobilization strategy has some advantages over the direct immobilization in terms of enzyme loading, specific activity and stability. Circular dichroism and fluorescence spectra show that single wall carbon nanotube-(n-dodecyl β-D-maltoside)-concanavalin A hybrid support has a smaller effect on the enzyme structure compared with bare carbon nanotube, demonstrating that the present self-assembly strategy is effective for laccase immobilization.
和大多数水溶性酶一样,漆酶的固定化是实现应用价值的必要途径。
传统的酶固定化方法,大多是通过酶外表面氨基酸残基上的功能基团与载体进行作用而连接。这可能会导致酶多个位点和载体结合,破坏了酶的天然构象,使固定化酶活性大幅度下降,同时酶分子不恰当的空间取向,也可能使得固定化酶的活性位点与底物的接触受阻,使催化效率大大降低。因此,定向、高效成为酶固定化方法研究的关键。
已报道的酶定向固定化方法中,有的依靠酶与载体(修饰)之间亲和作用,有的依靠蛋白的特定的氨基酸残基与载体上对应的偶联基团之间的共价结合。目前,单一活性中心酶的定向固定化技术的研究取得了一定的进展。
漆酶是一个单链多氧化还原活性中心的大分子,这一结构特征使得固定化漆酶的催化效率在很大程度上依赖其在载体表面上的取向。就酶电极而言,不同的取向不仅影响其直接电子转移途径,还影响其生物电催化氧还原效率。因此,漆酶的高效定向固载是漆酶利用的关键。有关漆酶的定向固定化研究的报道,迄今为止仍然相对较少。因此,探索漆酶定向、高效的固定化新方法,对漆酶功能器件的开发具有重要意义。
本论文分别从漆酶自身的生物修饰和／或载体的化学修饰等不同角度,尝试建立了几种漆酶高效定向固载新策略。
一、漆酶的生物修饰
相比于蛋白本身的化学修饰,功能蛋白的定点生物修饰是实现功能蛋白定向组装的理想手段之一。目前,生物学上对漆酶基因进行克隆和序列分析已经取得了很大进展,并且实现了其高效的重组表达(或异源表达)。以此为基础,以漆酶的定向固定化为目标,本文首先利用分子生物学的方法将漆酶进行了定点生物修饰。
借助于半胱氨酸的侧链巯基和金基底形成的硫-金键常用来构建自组装修饰电极。因此在漆酶的氮端或碳端引入半胱氨酸将为漆酶的定向固定带来便利。而组氨酸的咪唑基团与金属离子的特异性亲和作用,也常常被用于蛋白的纯化和固定。
本节首先设计了一段编码Cys-(His×6)-短肽的基因序列,通过基因重组的方法,将这段序列融合到来源于Trametes sp. AH28-2的漆酶基因lacA的3'/5'端,并构建了表达载体,再经过电转化导入毕赤酵母中进行了漆酶的异源高效表达,最终成功获得了分别在N端和C端带有Cys-(His×6)-短肽的重组漆酶rLacA-N和rLacA-C。对重组漆酶进行了酶学性质表征,结果表明两种重组漆酶和非重组漆酶具有相似的酶学性质,说明对漆酶的生物修饰没有对酶本身性质产生大的影响,为后续的固定化打好了基础。
二、重组漆酶在金电极上定向固定化策略
漆酶在常规电极上的直接电子转移现象不易观察到。不仅如此,还发现随机取向漆酶的电催化氧还原伴随着中间体过氧化氢的产生,影响电子转移效率。由此可见,电极上漆酶的定向组装是提高直接电子转移效率、构建漆酶电化学生物传感器和生物燃料电池等功能器件的关键步骤。
利用重组漆酶蛋白链末端的半胱氨酸残基,与金电极形成的Au-S键,将重组漆酶定向地组装到平面金电极表面上。
酶活测量表明,固定化漆酶能够较好地保持原有的生物活性。漆酶电极的循环伏安法表征又表明,两种重组漆酶在金电极表面均发生了直接电子转移,对氧也表现出生物电催化活性。然而两种重组漆酶电极的直接电化学行为却表现出明显差异,对氧的生物电催化还原效率及其还原产物也有差异。分析表明,金电极表面上不同取向漆酶的直接电子转移途径与难易程度不一样。T1位点靠近电极表面易于漆酶对氧的生物电催化还原。
上述漆酶在电极上定向固定的研究不但有助于深化对漆酶直接电化学机制的认识,也有助于基于漆酶的生物燃料电池的研发。
三、重组漆酶在琼脂糖载体的定向固定化策略
将氮端或碳端带有His×6-短肽链的重组漆酶,通过组氨酸与Ni2+离子的螯合作用,定向地组装到氨基三乙酸-Ni2+-修饰的琼脂糖载体表面上。在这个固定化体系中,由于固定位点位于漆酶分子表面、远离漆酶活性中心,有利于漆酶结构的保持,使固定化漆酶可以保持较高的催化活性；同时多组氨酸链作为位点,也增加了固定化漆酶的稳定性；最重要的是,依靠漆酶本身定点生物修饰的氨基酸链作为固定位点,实现了漆酶取向单
一、取向可控的高效固定化。
固定化漆酶酶活测量结果表明,在相同条件下不同取向的两种固定化漆酶表现出不同的催化活性；然而酶结构的圆二色谱分析表明,不同取向漆酶的二级结构变化不大。分析表明,这可能是由于固定化T1位点的外露程度不同,导致底物的可触及性不同所致。研究结果还表明,固定化酶比游离酶有更高的热稳定性,同时具有较高的重复利用性。
四、非重组漆酶在单壁碳纳米管上亲和固定化策略
漆酶是一种糖蛋白酶,其表面的糖基可以作为固定化的位点。将固定载体——单壁碳纳米管用表面活性剂十二烷基麦芽糖苷进行表面修饰,利用伴刀豆蛋白对糖基的特异性亲和作用,同时又凭借表面活性剂对碳纳米管的分散作用,从增加碳纳米管比表面积、减少酶结构改变、增加固定化酶的稳定性等方面出发,构建了单壁碳纳米管-烷基糖苷-伴刀豆蛋白-糖蛋白酶固定化新体系。
分别以漆酶和辣根过氧化物酶为例研究,实验结果表明,这种新型固定化方法,与两种酶直接固定于碳纳米管上相比,在酶的上载量、比活力、稳定性等方面,都有很大的优势。圆二色谱和荧光光谱分析测试酶的结构变化结果表明,单壁碳纳米管-烷基糖苷-伴刀豆蛋白复合载体和单壁碳纳米管相比,对酶的结构影响较小,这也是新体系中酶的比活力较高的直接原因。
这种利用自组装方法,通过生物凝集素间接固定糖蛋白的新策略,有助于提高单壁碳纳米管上糖蛋白酶的酶学性质,为糖蛋白酶及碳纳米管的应用奠定了基础。
Laccase is a Cu-containing polyphenol oxidase, which catalyzes the oxidation of various aromatic amines and phenols with concomitant reduction of oxygen to water. The catalytic characteristics of laccase make it very useful not only in lignin degradation, pulp bleaching, dye decolorization/detoxication, and environmental protection but also in biosensor and biofuel cell development.
Similar to other enzymes, the immobilization of laccase is an important strategy for its real application. Traditionally, an enzyme is immobilized via the interaction between a support and a functional group of amino acid residue on the enzyme surface. In this way, it is possible that multiple sites of enzyme are attached on the support, resulting in a disturbed enzyme structure, decreased enzyme activity and inappropriate orientation. It may also hinder the interaction between the active site of an enzyme and its substrate, resulting in decreased activity. Therefore, the oriented and high efficient immobilization becomes the focus of recent research.
So far, some oriented immobilization strategies have been developed. Some are based on the affinity interaction between an enzyme and a support. Some are based on the covalent interaction between amino acid residue and coupling group on the support. Currently, some development on the oriented immobilization of enzymes of single active site has been achieved.
It is known that laccase is a single-chain macromolecule with multiple redox active sites. The catalytie efficiency of the immobilized laccase therefore depends largely on the strategies used for the immobilization, especially when laccase is immobilized on an electrode for the direct electron transfer and bioelectrocatalysis. It follows that high efficient and oriented immobilization of laccase is significant for the development of laccase-based functional devices. However, few works have been carried out on the oriented immobilization of laccase. This thesis presents several new strategies for high-efficient and oriented immobilization of laccase from the perspective of the bio-modification of enzyme itself and/or chemical modification of the carrier.
1. Bio-modification of laccase
Relatively speaking, the biological modification of functional proteins is more suitable than its chemical modification for the orientation assembly of proteins. So far, great progress has been made in the cloning and sequence analysis of the gene of laccase and in the high efficient heterologous expression of laccase. In present study, the molecular biology-based bio-modification of laccase is used to realize the oriented immobilization of laccase.
The self-assembly of the modified laccase on Au electrode is based on the Au-S band formed between side chain thiol of cysteine and gold substrate. Therefore, to facilitate the immobilization of laccase, the N-terminal or C-terminal is modified with cysteine. The coordination between the imidazole group of histidine and Ni2+ions has also frequently been used for purification and immobilization of protein.
In the present study, a DNA sequence of Cys-(His×6)-was first designed and then fused to the3'/5'DNA terminus of laccase from Trameters sp. AH28-2. After that an expression vector was built and electroporated into Pichia pastoris for expression. Finally, the N-terminus and C-terminus of laccase was successfully modified with Cys-(His×6)-oligopeptide.
The enzymatic property of the recombinant laccase was analyzed. The results show that the two recombinant laccases exhibit similar enzymatic properties, indicating that the biological modification has no big effect on enzyme properties and the modified laccase can be used for further immobilization.
2. Oriented immobilization of recombinant laccase on gold electrode
The direct electron transfer of laccase on common electrodes is hardly observed. It was also found that for non-oriented immobilized laccase electrode, the electrocatalytic reduction of oxygen is accompanied by the production of the intermediate H2O2, which decreases the electron transfer efficiency. Thus, the oriented immobilization of laccase on electrode is a key step for enhancing the electron transfer efficiency, and constructing high-performance biosensors and biofuel cells.
Based on the Au-S band between the cysteine residue of the recombinant laccase and gold electrode, the recombinant laccase is assembled orientationally on the gold electrode.
Enzyme activity test shows that the activity of the immobilized laccase is well-retained. Cyclic voltammetry test shows that the direct electron transfer and the bioelectroreduction of oxygen are achieved on both the electrodes modified the recombinant laccases. However, the two electrodes show different direct electrochemical behaviors. Analysis shows that laccase with different orientation on gold electrode have different electron transfer pathways and different direct electron transfer efficiency. Bioelectrocatalytic reduction of oxygen is easier for laccase modified electrode where the T1site is more close to the electrode surface. The above research is helpful to the in-depth understanding of the direct electrochemistry of laccase and also to the development of laccase-based biofuel cells.
3. Oriented immobilization of recombinant laccase on agarose
The recombinant laccase with Cysteine-6×Histidine tag at N-terminus and C-terminus is immobilized on the surface of NTA-Ni2+-modified agarose via the chelation between the histidine residue and Ni2+ion. In this system, the immobilization site is close to laccase surface but distant away from laccase active site, which is beneficial for the structure retention and high catalytic activity. The multiple immobilization sites also enhance the stability. More importantly, the bio-modified amino acid chain realizes the oriented immobilization with adjustable orientation.
The enzyme activity test shows that the laccases with different orientations show different activities under the same testing conditions. Circular dichroism spectrum shows that the secondary structure changes little for the two recombinants prior to or after the immobilization. Analysis shows that it is the orientation that makes the exposure of T1site of laccase to the outer solution different, which results in different accessibility of the same substrate to the T1site and therefore different activity. It is also found after immobilization, thermal stability enhances and reusableility is high.
4. Efficient immobilization of non-recombinant laccase on single wall carbon nanotube
Laccase is one of the glucoproteinases. The glycosyl on the surface can be used as sites for immobilization. In the present study, the single wall carbon nanotube is first modified with surfactant (alkyl polyglucoside) to disperse the nano tubes and increase the specific surface area. Based on the affinity between concanavalin A and glycosyl, laccase is then immobilized on carbon nanotubes, forming a new conjugate of single wall carbon nanotube-(n-dodecyl β-D-maltoside)-concanavalin A-glucoproteinases with little structure change and high stability.
The experimental results show that the new immobilization strategy has some advantages over the direct immobilization in terms of enzyme loading, specific activity and stability. Circular dichroism and fluorescence spectra show that single wall carbon nanotube-(n-dodecyl β-D-maltoside)-concanavalin A hybrid support has a smaller effect on the enzyme structure compared with bare carbon nanotube, demonstrating that the present self-assembly strategy is effective for laccase immobilization.
引文
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