Glycation of β-lactoglobulin under dynamic high pressure microfluidization treatment: Effects on IgE-binding capacity and conformation

被引:50
作者
Chen, Yuan [1 ]
Tu, Zongcai [1 ,2 ]
Wang, Hui [2 ]
Zhang, Lu [1 ]
Sha, Xiaomei [1 ]
Pang, Juanjuan [1 ]
Yang, Ping [1 ]
Liu, Guangxian [1 ]
Yang, Wenhua [2 ]
机构
[1] Jiangxi Normal Univ, Key Lab Funct Small Organ Mol, Ministy Educ, Nanchang 330022, Peoples R China
[2] Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Peoples R China
基金
中国国家自然科学基金; 国家高技术研究发展计划(863计划);
关键词
beta-lactoglobulin; DHPM; Glycation; IgE-binding capacity; Conformation; BOVINE SERUM-ALBUMIN; MAILLARD REACTION; FUNCTIONAL-PROPERTIES; INDUCED AGGREGATION; SECONDARY STRUCTURE; FOAMING PROPERTIES; WHEY PROTEINS; MILK ALLERGY; HEAT; ANTIGENICITY;
D O I
10.1016/j.foodres.2016.10.020
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The effects of dynamic high-pressure microfluidization (DHPM) (80, 120, and 160 MPa) treatment and glycation with galactose on the IgE-binding capacity and conformation of beta-lactoglobulin (beta-Lg) were investigated. The binding capacity of immunoglobulin E (IgE) from patients' sera with cow's milk allergy on beta-Lg glycated with galactose decreased after DHPM treatment. beta-Lg treated after different DHPM methods and pressures yielded a significant discrepancy in IgE-binding capacity. When beta-Lg was pretreated by DHPM, the IgE-binding capacity of beta-Lg-galactose conjugates decreased with increasing pressure; however, the conjugates showed higher IgE-binding capacity at 120 MPa than that at 80 and 160 MPa when the beta-Lg-galactose mixture was treated by DHPM. Results of thermal properties, intrinsic fluorescence spectroscopy, surface hydrophobicity, and circular dichroism (CD) spectra indicated the occurrence of protein unfolding, as well as the tertiary and secondary structural changes of beta-Lg. The results suggested pretreatment by DHPM and glycation with galactose was a promising approach for eliminating the IgE binding capacity of beta-Lg. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:882 / 888
页数:7
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