期刊
INTERNATIONAL DAIRY JOURNAL
卷 83, 期 -, 页码 43-51出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.idairyj.2018.03.006
关键词
-
资金
- Fonterra
- New Zealand Ministry for Primary Industries via the Primary Growth Partnership programme
Chaperon-like action of caseins during milk protein denaturation has not been comprehensively investigated in commercial dairy mixtures. Gel electrophoresis and FTIR spectroscopy were therefore used to assess the interactions and mechanisms of casein mediation in whey protein (WP) heat-denaturation. Milk protein concentrate and WP isolate were used to prepare 10% dispersions with high (30: 70), low (5: 95) and control (0: 100) casein to WP ratios. After pH adjustment to 6.7 or 7.5, samples were heat-treated at 100 degrees C for 1 min. Gel electrophoresis revealed that higher casein content increased fractions of non-covalently associated protein complexes. Secondary conformations of WPs were least affected by the heating process at pH 7.5 with the high casein inclusion as indicated by FTIR spectroscopy. Hydrophobic associations predominated in controlling the WP heat-aggregation. Caseins appeared to form heat-induced hydrophobic associations to terminate the denaturation and aggregation process of WPs at a certain stage. (C) 2018 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