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Effect of curdlan on the gel properties and interactions of whey protein isolate gels
被引:9
|作者:
Hu, Wenmei
[1
,2
]
Xu, Xindong
[3
,4
,5
]
Wang, Xingyan
[1
,2
]
Ma, Tinghong
[1
,2
]
Li, Yuting
[1
,2
]
Qin, Xianglin
[1
,2
]
Wei, Jibin
[1
,2
]
Chen, Shan
[1
,2
]
机构:
[1] Guangxi Univ, Coll Light Ind & Food Engn, Nanning 530004, Peoples R China
[2] Guangxi Univ, Collaborat Innovat Ctr Guangxi Sugar Ind, Nanning 530004, Peoples R China
[3] South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510641, Peoples R China
[4] Foshan Univ, Guangdong Prov Key Lab Intelligent Food Mfg, Foshan 528225, Peoples R China
[5] China Singapore Int Joint Res Inst, Guangzhou 510700, Peoples R China
基金:
中国国家自然科学基金;
关键词:
Whey protein isolate;
Curdlan;
Gel properties;
Interaction;
LOTUS ROOT AMYLOPECTIN;
GELATION;
D O I:
10.1016/j.ijbiomac.2024.134161
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
This study investigated the influence of curdlan on the gel properties of whey protein isolate (WPI). Results demonstrated that curdlan significantly improved the water-holding capacity, gel strength and rheological properties of the WPI gels. Moreover, it promoted the unfolding of the molecular structures of WPI, which was manifested by the transition from alpha-helix to beta-sheet, an increase in free sulfhydryl content and a decrease in surface hydrophobicity. Furthermore, 4 % curdlan promoted the formation of WPI with uniform and compact elastic gel network structures, primarily attributed to disulphide bonds, hydrogen bonds and hydrophobic interactions. However, when the addition of curdlan exceeds 4 %, excessive entanglement of curdlan chains and steric hindrance effects hinder the unfolding and folding of protein structures, weaken their interaction, result in a loose network structure and affect the gel properties. In conclusion, this study demonstrates that curdlan can effectively improve the gelling properties of WPI, suggesting its potential application in low-calorie gel-based dairy products.
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页数:12
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