虾青素
小虾
铁蛋白
分子
热稳定性
溶解度
化学
化学稳定性
生物物理学
生物化学
生物
有机化学
类胡萝卜素
渔业
作者
Chenxi Zhang,Xiaoyi Tan,Chenyan Lv,Jiachen Zang,Guanghua Zhao
标识
DOI:10.1111/1750-3841.15945
摘要
The low stability of trans-astaxanthin (AX) not only limits its applications as a functional factor in food systems, but also affects the sensor quality of most shrimp products. Therefore, it is important to find an easy, effective way to improve the physical and chemical stability of AX. In this study, by taking advantage of the co-existence of AX and shrimp ferritin (Marsupenaeus japonicus ferritin, MjF), we investigated the interaction of AX with MjF. Results showed that AX molecules are able to bind on the outer surface of MjF to form complexes, and quantitative analyses demonstrated that one ferritin molecule is bound to ∼48 AX molecules. Consequently, such binding not only greatly enhances the water solubility, thermal stability, and photo stability of AX, but also protects AX from Fe2+ -induced oxidative damage, as compared to free AX. Thus, MjF could be used as a protective molecule to improve the physical and chemical stability of AX. PRACTICAL APPLICATION: Our study opens up a new avenue for improving the physicochemical properties of bioactive molecules by interacting with protein, and shrimp ferritin could be explored as a protective system for the bioactive molecules.
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