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虾铁蛋白极大地提高了虾青素的物理和化学稳定性。

Shrimp ferritin greatly improves the physical and chemical stability of astaxanthin.

作者信息

Zhang Chenxi, Tan Xiaoyi, Lv Chenyan, Zang Jiachen, Zhao Guanghua

机构信息

College of Food Science and Nutritional Engineering, Key Laboratory of Functional Dairy, Ministry of Education, China Agricultural University, Beijing, China.

出版信息

J Food Sci. 2021 Dec;86(12):5295-5306. doi: 10.1111/1750-3841.15945. Epub 2021 Oct 29.

Abstract

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 Fe -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.

摘要

反式虾青素(AX)的低稳定性不仅限制了其作为食品系统中功能因子的应用,还影响了大多数虾类产品的感官品质。因此,找到一种简单有效的方法来提高AX的物理和化学稳定性非常重要。在本研究中,利用AX与虾铁蛋白(日本对虾铁蛋白,MjF)的共存,我们研究了AX与MjF的相互作用。结果表明,AX分子能够结合在MjF的外表面形成复合物,定量分析表明一个铁蛋白分子与约48个AX分子结合。因此,与游离AX相比,这种结合不仅大大提高了AX的水溶性、热稳定性和光稳定性,还保护AX免受铁诱导的氧化损伤。因此,MjF可作为一种保护分子来提高AX的物理和化学稳定性。实际应用:我们的研究为通过与蛋白质相互作用改善生物活性分子的物理化学性质开辟了一条新途径,虾铁蛋白可作为生物活性分子的保护系统进行探索。

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