Salting-in effect on muscle protein extracted from giant squid (Dosidicus gigas)

被引:29
|
作者
Zhang, Rui [1 ]
Zhou, Ru [1 ]
Pan, Weichun [1 ]
Lin, Weiwei [1 ]
Zhang, Xiuzhen [1 ]
Li, Mengya [1 ]
Li, Jianrong [2 ]
Niu, Fuge [1 ]
Li, Ang [1 ]
机构
[1] Zhejiang Gongshang Univ, Sch Food Sci & Biotechnol, Food Safety Key Lab Zhejiang Prov, Hangzhou 310018, Zhejiang, Peoples R China
[2] Bohai Univ, Coll Chem Chem Engn & Food Safety, Prov Key Lab Food Qual Safety & Funct Food, Jinzhou 121013, Liaoning, Peoples R China
基金
中国国家自然科学基金;
关键词
Salting-in effect; Myofibrillar protein; Potassium chloride; Conformation modification; Zeta-potential; Secondary virial coefficient; CIRCULAR-DICHROISM; SOLUBILITY; STABILITY; CHLORIDE; GELATION; CATIONS;
D O I
10.1016/j.foodchem.2016.07.177
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The salting-in effect on muscle protein is well-known in food science but hard to explain using conventional theories. Myofibrillar protein extracted from the giant squid (Dosidicus gigas) was selected as a model muscle protein to study this mechanism in KCl solutions. Changes in the secondary structures of myofibrillar protein molecules caused by concentrated salts, particularly in the paramyosin molecule conformation, have been reported. Zeta-potential determinations showed that these secondary structures have modified protein molecule surfaces. The zeta-potential of the myofibrillar protein molecules fell from -7.24 +/- 0.82 to -9.99 +/- 1.65 mV with increasing salt concentration from 0.1 to 0.5 M. The corresponding second virial coefficient increased from -85.43 +/- 3.8 x 10(-7) to -3.45 +/- 1.3 x 10(-7) mol mL g(-2). The extended law of corresponding states suggests that reduced attractive interactions increase the protein solubility. Solubility measurements in alternating KCl concentrations showed that the conformational change was reversible. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:256 / 262
页数:7
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