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Preparation of novel cross-linked and octylated caseinates using a biphasic enzymatic procedure and their functional properties.

Authors
  • Zhang, Yaqiong
  • Niu, Yuge
  • Yao, Fangyi
  • Dai, Bona
  • Wang, Qin
  • Yu, Liangli Lucy
Type
Published Article
Journal
Journal of Agricultural and Food Chemistry
Publisher
American Chemical Society
Publication Date
Aug 27, 2014
Volume
62
Issue
34
Pages
8655–8662
Identifiers
DOI: 10.1021/jf5024998
PMID: 25090285
Source
Medline
License
Unknown

Abstract

A novel microbial transglutaminase-catalyzed aqueous-organic biphasic reaction system was successfully developed to prepare caseinate derivatives by cross-linking and incorporating nonpolar octyl tails for the first time. SDS-PAGE and (1)H NMR analysis confirmed that cross-linking and octyl conjugation occurred simultaneously. The octyl substitution degree (SD) was measured by (1)H NMR and used as an index to determine a suitable reaction condition. It was found that at the condition of 0.125% (w/v) protein concentration and 6 h of reaction time, the modified caseinate had the highest SD of 28.96%. The modified caseinate also had an increased surface hydrophobicity, better emulsifying activity, and improved thermal and salt stabilities. However, its emulsion stability or in vitro enzymatic digestibility was slightly lower than that of the native caseinate.

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