化学
肌原纤维
Ⅰ型胶原
肌球蛋白
溶解度
防御工事
生物物理学
氨基酸
食品科学
化学工程
生物化学
有机化学
医学
生物
工程类
病理
作者
Yadong Zhao,Kunyu Lu,Xinyue Piao,Yan Song,Libin Wang,Rusen Zhou,Pingping Gao,Heng Yen Khong
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2022-12-06
卷期号:407: 135157-135157
被引量:20
标识
DOI:10.1016/j.foodchem.2022.135157
摘要
Surimi products have unsatisfactory gel properties. Hence, this study evaluates the effect of collagen-adding on surimi gel properties and provides the first observation results regarding collagen type influence. With higher water solubility and more charged amino acids than type II, collagen type I intertwines with surimi myofibrillar proteins better to induce higher exposure of protein functional domains, more sufficient conformational changes of myosin and greater formation of chemical forces among proteins. These enhancements accelerate the gelation rate, leading to a well-stabilized surimi gel. The collagen I-containing surimi gels show more compact structures with uniformly distributed smaller pores than those containing collagen II, thereby providing the final products with higher water holding capacity and better textural profiles. As such, the surimi gel fortification performance of collagen I and the well-elucidated collagen-myofibrillar protein interaction mechanism will guide the further exploitation of collagen as an effective additive in the food industry.
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