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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.
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页码:79 / 88
页数:10
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