Effect of N-ethylmaleimide as a blocker of disulfide bonds formation on the properties of different protein-emulsion MP composite gels

被引:2
作者
Xu, Yuyu [1 ]
Yang, Jingjing [1 ]
Wu, Mangang [1 ]
Lei, Shumin [1 ]
Yin, Peipei [1 ]
Yin, Qing [1 ]
Zhu, Tianhao [1 ]
Wang, Qingling [1 ]
Zhao, Xinxin [1 ]
Jin, Duxin [1 ]
Liu, Rui [1 ]
Ge, Qingfeng [1 ]
Yu, Hai [1 ]
机构
[1] Yangzhou Univ, Coll Food Sci & Engn, Yangzhou 225127, Peoples R China
基金
中国国家自然科学基金;
关键词
Sulfhydryl blocker N-ethylmaleimide; Sulfhydryl group; Disulfide bond; Emulsion; Gel properties; SURFACE-ACTIVE PROPERTIES; HEAT-INDUCED GELATION; MYOFIBRILLAR PROTEIN; RHEOLOGICAL PROPERTIES; MICROSTRUCTURAL PROPERTIES; THERMAL-DENATURATION; SULFHYDRYL-GROUPS; WATER; MATRIX; STABILITY;
D O I
10.1016/j.fochx.2024.101831
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Three different emulsions of myofibrillar protein (MP), soy protein isolate (SPI) and egg white protein isolate (EPI) were individually mixed with MP sol to form composite gels. N-ethylmaleimide (NEM) was used as a sulfhydryl group blocker to evaluate the effects of sulfhydryl and disulfide bonds on the properties of different protein-emulsion composite gels. The results show that the disulfide bond contents in the MP (SPI, EPI) emulsion composite gel decreased from the initial 2.4 f 0.1, (2.3 f 0.2, 1.8 f 0.4) mol/kg to 0.6 f 0.1, (0.5 f 0.3, 0.7 f 0.1) mol/kg with the NEM content increased. In addition, the microstructure showed that the interfacial protein membrane of the emulsion globules were broken in different degrees, indicating that the interaction between the emulsion and the gel matrix was weakened. Meanwhile, gel strength, water distribution and elastic modulus of the composite gels were reduced with NEM contents increased.
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页数:10
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共 53 条
[51]   Thermal denaturation and aggregation of threadfin bream actomyosin [J].
Yongsawatdigul, J ;
Park, JW .
FOOD CHEMISTRY, 2003, 83 (03) :409-416
[52]   Physicochemical Effects of the Lipid Phase and Protein Level on Meat Emulsion Stability, Texture, and Microstructure [J].
Youssef, M. K. ;
Barbut, S. .
JOURNAL OF FOOD SCIENCE, 2010, 75 (02) :S108-S114
[53]   Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure [J].
Zhang, Ziye ;
Yang, Yuling ;
Tang, Xiaozhi ;
Chen, Yinji ;
You, Yuan .
FOOD CHEMISTRY, 2015, 188 :111-118