Effect of ultrasound on the structure and functional properties of transglutaminase-crosslinked whey protein isolate exposed to prior heat treatment

被引:63
|
作者
Jiang, Zhanmei [1 ,2 ]
Wang, Chunyan [1 ]
Li, Tong [1 ]
Sun, Dongxue [1 ]
Gao, Hao [1 ]
Gao, Zengli [2 ]
Mu, Zhishen [2 ]
机构
[1] Northeast Agr Univ, Key Lab Dairy Sci, Minist Educ, Harbin 150030, Heilongjiang, Peoples R China
[2] Inner Mongolia Mengniu Dairy Grp Co Ltd, Hohhot 011517, Peoples R China
基金
黑龙江省自然科学基金;
关键词
HIGH-INTENSITY ULTRASOUND; MICROBIAL TRANSGLUTAMINASE; BETA-LACTOGLOBULIN; MILK-PROTEINS; EMULSIFYING PROPERTIES; PHYSICAL-PROPERTIES; FOAMING PROPERTIES; LINKING; CONCENTRATE; SOLUBILITY;
D O I
10.1016/j.idairyj.2018.08.007
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Effects of ultrasound treatment (20 kHz, 41-45 W cm(-2), 0, 20, 40 or 60 min) on the physicochemical, functional properties and elements of the secondary structure of transglutaminase (TGase)-crosslinked whey protein isolate (WPI) exposed to prior thermal treatment (75 degrees C, 15 min) were investigated. The largest molecular size of proteins in the TGase-crosslinked WPI was observed after the ultrasound and thermal pre-treatment (HU-WPI-TGase). HU-WPI-TGase had the maximum intrinsic fluorescence intensity, with highest loss of free amino groups. Ultrasound-treated WPI (U-WPI) showed more (13%) emulsifying activity and more (63%) foaming ability than untreated WPI, but HU-WPI-TGase had higher foam stability and lower emulsifying activity than U-WPI. FTIR analysis indicated that ultrasound, heat treatment and TGase cross-linking had effects on the beta-sheet, beta-turn and random coil of WPI. The outcomes from this study show a potential application in providing novel functional ingredients for the dairy industry. (C) 2018 Elsevier Ltd. All rights reserved.
引用
收藏
页码:79 / 88
页数:10
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