盐(化学)
化学
肌原纤维
贮藏蛋白
原肌球蛋白
色谱法
食品科学
生物化学
有机化学
肌球蛋白
基因
作者
Yongfang Gao,Can Luo,Junyao Zhang,Huijuan Wei,Zan Lin-sen,Jie Zhu
出处
期刊:Food Chemistry
[Elsevier]
日期:2022-11-01
卷期号:393: 133400-133400
被引量:62
标识
DOI:10.1016/j.foodchem.2022.133400
摘要
Improving the characteristics of low salt proteins is the key to the gel properties of low-salt meat products which are demanded by people nowadays. The present study focused on the effects of KGM concentrations on the changes in structure and gelling properties of low-salt myofibrillar protein (MP). KGM addition (≤0.75 %) irrespective of salt concentration modified secondary and tertiary structures of MPs, enhanced the binding capacity of Troponin-T and Tropomyosin, augmented the gelling behavior of proteins, and remarkably improved the storage modulus (G') and gel strength of heat-induced MP gels. Interestingly, KGM addition in low salt condition showed the transformation of the all-gauche SS conformation into gauche-gauche-trans and trans-gauche-trans, and the partial transformation of α-helices into β-sheets. overall, KGM modified the structure of low salt MPs and thus improved the gel properties of low salt MPs. Therefore, KGM is recommended for low-salt meat processing to enhance the MP gelling potential.
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