Suppr超能文献

解冻滴的出现:肌原纤维蛋白复性的作用。

On the emerging of thawing drip: Role of myofibrillar protein renaturation.

机构信息

Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; Unit of Food Science and Formulation, Gembloux Agro-Bio Tech, University of Liège, Gembloux B-5030, Belgium.

Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China.

出版信息

Food Chem. 2022 Nov 1;393:133398. doi: 10.1016/j.foodchem.2022.133398. Epub 2022 Jun 4.

Abstract

This study aimed to facilitate the understanding on the origin of thawing drip under different freezing rate. Eventually we observed significantly greater thaw loss produced by slow freezing (8.58%) as compared to fast freezing (6.41%) after 24 h of thawing. Back to the freezing, ice crystallization induced decline in pH and the cold denaturation of myofibrillar protein. However, independent of freezing rate, we noticed protein renaturation with pH restoring during thawing, evidenced by the decreasing surface hydrophobicity, increasing solubility and thermal stability, and gradually stabilized secondary structure. Meanwhile, the water-holding of myofibrils increased with thawing process along with the rising water mobility. Under fast freezing, the results indicated less extensive protein cold denaturation and lower water mobility during thawing. Besides, we proposed that the microenvironment of lower ionic strength in fast freezing should benefit the protein renaturation and water re-absorption, ultimately contributed to lower thaw loss.

摘要

本研究旨在深入了解不同冻结速率下解冻液滴的形成机制。最终发现,在解冻 24 小时后,慢速冻结(8.58%)比快速冻结(6.41%)产生了更大的解冻损失。回溯到冻结过程,冰晶的形成会导致 pH 值下降和肌原纤维蛋白的冷变性。然而,无论冻结速率如何,我们都注意到在解冻过程中伴随着 pH 值的恢复发生了蛋白质复性,这表现在表面疏水性降低、溶解度和热稳定性增加,以及二级结构逐渐稳定。同时,肌原纤维的保水性随着解冻过程的进行而增加,水的流动性也随之增加。在快速冻结下,结果表明在解冻过程中,蛋白质的冷变性程度较轻,水的流动性较低。此外,我们提出在快速冻结中较低的离子强度的微环境有利于蛋白质复性和水的再吸收,最终导致较低的解冻损失。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验