期刊
LWT-FOOD SCIENCE AND TECHNOLOGY
卷 59, 期 1, 页码 35-42出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.lwt.2014.06.013
关键词
Maillard reaction products; Bovine casein peptides; Angiotensin-I-converting enzyme inhibitory activity; Size exclusion chromatography
资金
- National Twelfth Five-Year Plan for Science and Technology Support Program of China [2013BAD18B06]
- Innovative Research Team of Higher Education of Heilongjiang Province [2010td11]
- Project for National Nature Science [31000801]
The purpose of this study was to evaluate the impact of temperature and pH on aginotensin-l-converting enzyme (ACE) inhibitory activity, free amino group, browning intensity, fluorescence intensity and molecular weight distribution of galactose-bovine casein peptide (BCP) Maillard reaction products (MRPs). With increased heating temperature and pH, browning intensity of Galactose-BCP MRPs increased, while free amino groups of Galactose-BCP MRPs decreased. The fluorescence intensity of Galactose-BCP MRPs reached its maximum value at 100 degrees C and thereafter gradually decreased, while fluorescence intensity of Galactose-BCP MRPs showed the maximum value at pH 10.0 and thereafter gradually decreased. Size exclusion chromatography of Galactose-BCP MRPs indicated molecular rearrangements and production of new smaller molecules as a function of the heating temperature and pH. Galactose-BCP MRPs had the lowest angiotensin-I-converting enzyme (ACE) inhibitory activity at 120 degrees C. BCP lost 29.13% ACE inhibitory activity at pH 12.0 by Maillard reaction with galactose. High temperature and alkaline condition of Maillard reaction lead to the loss of ACE inhibitory activities and changes of characteristics of bovine casein peptides. (C) 2014 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据