低温保护剂
水解物
食品科学
化学
结构完整性
凝结
植物蛋白
生物化学
生物
细胞生物学
低温保存
工程类
水解
胚胎
结构工程
物理
热力学
作者
Chao Wang,Junhui Rao,Xueyin Li,Diheng He,Ting Zhang,Jianteng Xu,Xi Chen,Lan Wang,Yue Yuan,Xiangwei Zhu
标识
DOI:10.1016/j.foodres.2023.112871
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 structures were also retarded. Moreover, gels prepared from CPH-protected frozen surimi demonstrated more stabilized 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 insights for development of pulse proteins as novel and high-performance food cryoprotectants.
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