Comparative studies on physicochemical properties of bovine serum albumin-glucose and bovine serum albumin-mannose conjugates formed via Maillard reaction

被引:59
作者
Jian, Wenjie [1 ,2 ]
He, Jing [3 ]
Sun, Yuanming [1 ]
Pang, Jie [4 ]
机构
[1] South China Agr Univ, Coll Food Sci, Guangzhou 510642, Guangdong, Peoples R China
[2] Xiamen Med Coll, Dept Pharm, Xiamen 361008, Peoples R China
[3] Fujian Agr & Forestry Univ, Coll Food Sci, Fuzhou 350002, Peoples R China
[4] Harvard Univ, Dept Phys, Oxford St, Cambridge, MA 02138 USA
基金
中国博士后科学基金; 中国国家自然科学基金;
关键词
Glycation; Glucose; Mannose; Physicochemical properties; Bovine serum albumin; EMULSIFYING PROPERTIES; CONFORMATIONAL FLEXIBILITY; FOOD PROTEINS; SOY PROTEIN; GLYCATION; PRODUCTS; DEXTRAN; VICILINS; FRUCTOSE; GLYCOSYLATION;
D O I
10.1016/j.lwt.2015.11.061
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Glucose and mannose are important factors and ingredients in glycation of bovine serum albumin (BSA). We aimed to study the effect of glucose and mannose on the physicochemical properties of BSA. In this research BSA-glucose conjugate (GBSA) and BSA-mannose conjugate (MBSA) were prepared by Maillard reaction under neutral pH at moderate temperature (45 degrees C). Our results showed the conjugation ratio between mannose and BSA was significantly higher than the ratio between glucose and BSA. All foaming stability and emulsifying activity were substantially-decreased in GBSA and MBSA. However, an increase in foaming capacity was observed in GBSA. The fluorescent spectra of both GBSA and MBSA indicated their decreased surface hydrophobicity. These changes were attributed to their reduced emulsifying activity. In addition, circular dichroism spectra shown GBSA presented a relative flexible and loosened conformation, whereas MBSA remained compact and rigid conformation. These alterations in molecular structure were responsible for their different foaming capacity. Our study provided principle knowledge to understand the structure-functions relationships of BSA glycation by mannose and glucose. These results can be used to provide theoretical guidance for protein modification. (C) 2016 Published by Elsevier Ltd.
引用
收藏
页码:358 / 364
页数:7
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