控制性打开二硫键-葡聚糖修饰对大豆分离蛋白表面活性性能及结构的影响
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摘要
为提高大豆分离蛋白的表面活性,试验采用过氧乙酸控制性的打开蛋白质的二硫键,并在此基础上加入葡聚糖进行复合修饰。结果表明:随着二硫键断开程度的增加,接枝度明显提升,褐变度与其有相同的变化趋势。当二硫键断开率为46%时,表面活性最理想。其中乳化性和乳化稳定性提高107.56%和175%;起泡性和起泡稳定性提高83.63%和105%;荧光图谱表明随着二硫键断开率的增加,荧光强度出现先升高后降低的趋势,而糖基化复合产物荧光强度依次降低;SDS-PAGE进一步证实,在糖基化过程中7S亚基最先消失,二硫键断开后,可以加速11S酸性亚基与葡聚糖发生糖基化反应。
In order to improve the surface activity of soy protein isolate,the experiment used peracetic acid to partially cleaving the disulfide bonds of the protein,and based on this, dextran was added for compound modification. The experimental results showed that with the increase of the degree of disulfide bond disconnection,the degree of grafting was obviously improved,and the browning degree had the same trend.When the disulfide bond breaking rate was 46%,the surface activity was most desirable. The emulsifying and emulsifying stability increased by 107.56% and 175%;the foaming and foaming stability increased by 83.63%and 105%;the fluorescence spectrum showed that the fluorescence intensity first rise and then decrease with the increase of the disulfide bond breaking rate. The fluorescence intensity of glycosylated composite products decreased in turn;SDS-PAGE further confirmed that the 7 S subunit disappeared first during the glycosylation process,and the 11 S acidic subunit and the portuguese could be accelerated after the disulfide bond was broken. The glycan underwent a glycosylation reaction.
In order to improve the surface activity of soy protein isolate,the experiment used peracetic acid to partially cleaving the disulfide bonds of the protein,and based on this, dextran was added for compound modification. The experimental results showed that with the increase of the degree of disulfide bond disconnection,the degree of grafting was obviously improved,and the browning degree had the same trend.When the disulfide bond breaking rate was 46%,the surface activity was most desirable. The emulsifying and emulsifying stability increased by 107.56% and 175%;the foaming and foaming stability increased by 83.63%and 105%;the fluorescence spectrum showed that the fluorescence intensity first rise and then decrease with the increase of the disulfide bond breaking rate. The fluorescence intensity of glycosylated composite products decreased in turn;SDS-PAGE further confirmed that the 7 S subunit disappeared first during the glycosylation process,and the 11 S acidic subunit and the portuguese could be accelerated after the disulfide bond was broken. The glycan underwent a glycosylation reaction.
引文
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[2]王松,夏秀芳,黄莉,等.湿法糖基化改性对大豆分离蛋白功能性质的影响[J].食品科学,2014,35(9):38~42.
[3]张晋博.多糖对大豆蛋白的修饰及其界面、乳化和凝胶性质的研究[D].华南理工大学,2013.
[4] Adachi M,Kanamori J,Masuda T,et al.Crystal structure of soybean 11S globulin:glycinin A3B4 homohexamer[J].Proceedings of the National Academy of Sciences of the United States of America,2003,100(12):7395~7400.
[5] Cmj B,Majs V B.Kinetic modelling of reactions in heated disaccharide–casein systems[J].Food Chemistry,2003,83(1):13~26.
[6] Ellman G L.Tissue sulfhydryl groups.[J].Archives of Biochemistry&Biophysics,1959,82(1):70~77.
[7] Fogliano V,Monti S M,Musella T,et al.Formation of coloured Maillard reaction products in a gluten-glucose model system[J].Food Chemistry,1999,66(3):293~299.
[8] Laemmli U K.Cleavage of structural proteins during the assembly of the head of bacteriophage T4.[J].Nature,1970,227(5259):680~685.
[9] Molina E,Papadopoulou A,Ledward D A.Emulsifying properties of high pressure treated soy protein isolate and 7S and 11S globulins[J].Food Hydrocolloids,2001,15(3):263~269.
[10] Mu L,Zhao H,Zhao M,et al.Physicochemical properties of soy protein isolates-acacia gum conjugates[J].Czech Journal of Food Sciences,2011,29(2):129~136.
[11] Soichiro Nakamura, Masahiro Ogawa, Shuryo Nakai,et al.Antioxidant Activity of a Maillard-Type Phosvitin Galactomannan Conjugate with Emulsifying Properties and Heat Stability[J].J.agric.food Chem,1998,46(10):3958~3963.
[12] Wang X B,Zhang Y H,Jiang L Z.Improvement of Emulsifying Properties of Soybean Protein Isolate through Glycosylation Modification[J].Advanced Materials Research,2013,781~784:1495~1499.