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Chickpea protein hydrolysate as a novel plant-based cryoprotectant in frozen surimi: Insights into protein structure integrity and gelling behaviors

文献类型： 外文期刊

作者： Wang, Chao 1 ; Rao, Junhui 1 ; Li, Xueyin 1 ; He, Diheng 1 ; Zhang, Ting 1 ; Xu, Jianteng 1 ; Chen, Xi 2 ; Wang, Lan 3 ; Yuan, Yue 4 ; Zhu, Xiangwei 1 ;

作者机构： 1.Hubei Univ Technol, Natl Ctr Cellular Regulat & Mol Pharmaceut 111, Key Lab Fermentat Engn, Hubei Key Lab Ind Microbiol,Minist Educ, Wuhan 430068, Peoples R China

2.Wuhan Polytech Univ, Key Lab Bulk Grain & Oil Deep Proc, Minist Educ, Wuhan 430023, Peoples R China

3.Hubei Acad Agr Sci, Inst Farm Prod Proc & Nucl Agr Technol, Wuhan 430064, Peoples R China

4.Oak Ridge Natl Lab, Ctr Nanophase Mat & Sci, Oak Ridge, TN 37830 USA

关键词： Chickpea protein hydrolysate; Cryoprotectant; Frozen surimi; Myofibrillar proteins; Denaturation; Gelling behaviors

期刊名称：FOOD RESEARCH INTERNATIONAL （ 影响因子：8.1； 五年影响因子：7.7 ）

ISSN： 0963-9969

年卷期： 2023 年 169 卷

页码：

收录情况： SCI

摘要： Chickpea protein (CP) and its enzymatic hydrolysates are one of the most widely consumed pulse ingredients manifesting versatile applications in food industry, such as binders, emulsifiers, and meat protein substitutes. Other than those well-known functionalities, however, the use of CP as a cryoprotectant remained unexplored. In this study, we prepared the chickpea protein hydrolysate (CPH) and investigated its cryoprotective effects to frozen surimi in terms of the protein structure integrity and gelling behaviors. Results indicated that CPH could inhibit myofibrillar protein (MP) denaturation and oxidation during the freeze-thaw cycling, as evidenced by their increased solubility, Ca2+-ATPase activity, sulfhydryl concentration, and declined content of disulfide bonds, carbonyl concentration and surface hydrophobicity. Freezing-induced changes on MP secondary struc-tures were also retarded. Moreover, gels prepared from CPH-protected frozen surimi demonstrated more stabi-lized microstructure, uniform water distribution, enhanced elasticity, gel strength and water holding capacity. The CPH alone, at a reducing addition content of 4% (w/w), exhibited comparable cryoprotective performance to that of the commercial formulation (4% sucrose and 4% sorbitol). Therefore, this study provides scientific in-sights for development of pulse proteins as novel and high-performance food cryoprotectants.

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