酶法糖基化修饰对酪蛋白结构及性质的影响
Effect of Enzymatic Glycosylation Modification on the Structure and Properties of Casein
DOI: 10.12677/HJFNS.2019.84039, PDF,  被引量   
作者: 樊永康, 项 婷, 吴晓琴, 陈玉峰：浙江大学生物系统工程与食品科学学院，浙江 杭州
关键词: 酪蛋白；壳寡糖；转谷氨酰胺酶；结构；性质；Casein； Chitosan Oligosaccharide； Transglutaminase； Structure； Nature
摘要: 以转谷氨酰胺酶为催化剂，壳寡糖为酰基受体，通过糖基化修饰酪蛋白，利用FTIR、CD、DSC对酪蛋白的结构进行分析。结果表明：酪蛋白经糖基化修饰之后的二级结构变得更加有序，DSC结果表明酪蛋白热稳定性有所增强。对酪蛋白及其修饰产物的乳化活性、乳化稳定性、表面疏水性进行分析。结果表明修饰产物的乳化活性有所降低，乳化稳定性和表面疏水性有所提高。
Abstract: The structure of casein was analyzed by FTIR, CD and DSC by using transglutaminase as catalyst and chitosan oligosaccharide as acyl receptor. The results showed that the secondary structure of casein after glycosylation modification became more orderly, and DSC results showed that the thermal stability of casein was enhanced. The emulsifying activity, emulsion stability and surface hydrophobicity of casein and its modified products were analyzed. The results showed that the emulsifying activity of the modified product was reduced, and the emulsion stability and surface hydrophobicity were improved.
文章引用：樊永康, 项婷, 吴晓琴, 陈玉峰, 沈建福. 酶法糖基化修饰对酪蛋白结构及性质的影响[J]. 食品与营养科学, 2019, 8(4): 296-303. https://doi.org/10.12677/HJFNS.2019.84039

参考文献

[1] Fox, P.F. (2003) Milk Proteins: General and Historical Aspects. In: Fox, P.F. and McSweeney, P.L.H., Eds., Advanced Dairy Chemistry-Proteins, Springer, New York, 1-48.
[Google Scholar] [CrossRef] 
[2] Zhu, D., Damodaran, S. and Lucey, J.A. (2008) Formation of Whey Protein Isolate (WPI)? Dextran Conjugates in Aqueous Solutions. Journal of Agricultural and Food Chemistry, 56, 7113-7118.
[Google Scholar] [CrossRef] [PubMed]
[3] Motoki, M. and Seguro, K. (1998) Transglutaminase and Its Use for Food Processing. Trends in Food Science & Technology, 9, 204-210.
[Google Scholar] [CrossRef] 
[4] Fu, M. (2011) Effects of TGase-Induced Chitosan Oligo-saccharide Glycosylation and Cross-Linking on the Properties of Two Proteins. Northeast Agricultural University, Haerbin.
[5] Qu, Y., Wang, X.J., Liu, X.L., et al. (2018) Effects of Enzymatic Glycosylation Modification on the Structure and Rheological Properties of Zein. Food and Machinery, 34, 11-14.
[6] Wang, X.J., Liu, X.L., Cong, W.S., et al. (2018) Glycosylation Modification and Product Properties of Corn Gluten-Soluble Protease. Journal of Chinese Institute of Food Science and Technology, 18, 141-148.
[7] Liu, F.G. (2017) Preparation of Pro-tein-Polyphenol-Carbohydrate Covalent Complex and Its Steady-State Effect on Functional Factors. China Agricultural University, Beijing.
[8] Feng, J. (2017) Preparation and Characterization of Bioactive Substance Carrier Based on Glucose Gemini Surfactant and Ovalbumin. Zhejiang University, Hangzhou.
[9] Jiang, S.J., Feng, Z. and Zhao, X.H. (2011) Casein Transglutaminase Enzymatic Glycosylation Cross-Linking Conditions and Product Properties. China Dairy Industry, No. 7, 25-28.
[10] Hayakawa, S. and Nakai, S. (1985) Relationships of Hydrophobicity and Net Charge to the Solubility of Milk and Soy Proteins. Journal of Food Science, 50, 486-491.
[Google Scholar] [CrossRef] 
[11] Sheng, L., Sun, P., Han, K., et al. (2017) Synthesis and Structural Characterization of Lysozyme-Pullulanconjugates Obtained by the Maillard Reaction. Food Hydrocolloids, 71, 1-7.
[Google Scholar] [CrossRef] 
[12] Guo, X.B., Guo, X.M., Yu, S.J. and Kong, F. (2018) Influences of the Different Chemical Components of Sugar Beet Pectin on the Emulsifying Performance of Conjugates Formed between Sugar Beet Pectin and Whey Protein Isolate. Food Hydrocolloids, 82, 1-10.
[Google Scholar] [CrossRef] 
[13] Mao, L., Pan, Q.Y., Hou, Z.Q., Yuan, F. and Gao, Y.X. (2018) Development of Soy Protein Isolate-Carrageenan Conjugates through Maillard Reaction for the Microencapsu-lation of, Bifidobacterium Longum. Food Hydrocolloids, 84, 489-497.
[Google Scholar] [CrossRef] 
[14] Zha, F.C., Dong, S.Y., Rao, J.J. and Chen, B. (2019) The Structural Modification of Pea Protein Concentrate with Gum Arabic by Controlled Maillard Reaction Enhances Its Functional Properties and Flavor Attributes. Food Hydrocolloids, 92, 30-40.
[Google Scholar] [CrossRef] 
[15] Johnson, W.C. (1990) Protein Secondary Structure and Cir-cular Dichroism: A Practical Guide. Proteins Structure Function and Genetics, 7, 205-214.
[Google Scholar] [CrossRef] [PubMed]
[16] Fu, M. and Zhao, X.H. (2017) Modified Properties of a Glycated and Cross-Linked Soy Protein Isolate by Transglutaminase and an Oligochitosan of 5 kDa. Journal of the Science of Food and Agriculture, 97, 58-64.
[Google Scholar] [CrossRef] [PubMed]
[17] Yang, R., Zuo, P., Zhang, M., et al. (2019) Transglutaminase Induced Oligochitosan Glycosylation of Ferritin as a Novel Nanocarrier for Food Bioactive Molecules. Food Hydrocolloids, 94, 500-509.
[Google Scholar] [CrossRef] 
[18] Boostani, S., Aminlari, M., Moosavi-Nasab, M., Niakosari, M. and Mesbahi, G. (2017) Fabrication and Characterization of Soy Protein Isolate-Grafted Dextran Biopolymer: A Novel Ingredient in Spray-Dried Soy Beverage Formulation. International Journal of Biological Macromolecules, 102, 297-307.
[Google Scholar] [CrossRef] [PubMed]
[19] Zhang, S.Y., Zheng, L.L., Zheng, X.Y., et al. (2019) Effect of Steam Explosion Treatments on the Functional Properties and Structure of Camellia (Camellia oleifera Abel.) Seed Cake Protein. Food Hydrocolloids, 93, 189-197.
[Google Scholar] [CrossRef] 
[20] Liu, L., Li, Y., Prakash, S., Dai, X. and Meng, Y.Y. (2018) Enzymolysis and Glycosylation Synergistic Modified Ovalbumin: Functional and Structural Characteristics. International Journal of Food Properties, 21, 395-406.
[Google Scholar] [CrossRef] 
[21] Xu, W. and Zhao, X.H. (2019) Structure and Property Changes of the Soy Protein Isolate Glycated with Maltose in an Ionic Liquid through the Maillard Reaction. Food & Function, 10, 1948-1957.
[Google Scholar] [CrossRef]