文献类型：期刊文献

英文题名：Mechanism of protein digestion inhibition by malondialdehyde-mediated oxidation in terms of molecular actions and structural changes

作者：Wang, Zefu[1,2];Chen, Guanyi[1];Xu, Chencai[1];Chen, Chunbei[1];Chen, Xiaosi[1];Liu, Shucheng[1,2]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Prov Engn Technol Res Ctr Seafood, Guangdong Prov Key Lab Aquat Prod Proc & Safety,Gu, Zhanjiang 524088, Peoples R China;[2]Dalian Polytech Univ, Collaborat Innovat Ctr Seafood Deep Proc, Dalian 116034, Peoples R China

年份：2024

卷号：205

外文期刊名：LWT-FOOD SCIENCE AND TECHNOLOGY

收录：SCI-EXPANDED(收录号：WOS:001281018900001)、、EI(收录号：20243016755561)、WOS

基金：We thank the National Key R & D Program of China (2023YFD2401404) , GuangDong Basic and Applied Basic Research Foundation (2023A1515110246) and the scientific research start-up funds of Guangdong Ocean University (060302042108) for the financial support for the research.

语种：英文

外文关键词：Myofibrillar protein; Multispectra; Molecular docking

外文摘要：This study investigated the molecular mechanism of malondialdehyde (MDA)-mediated oxidation affecting the digestive properties of myofibrillar proteins (MP) in golden pomfret using an in vitro static digestion model combined with multispectral and molecular docking techniques. It has been found that MDA hinders the digestion of proteins, resulting in a tendency to show a decrease in the digestibility of proteins. Using a multispectral technique, it was found that MDA could disrupt the structure of proteins, causing aggregation and precipitation of proteins. Moreover, static quenching occurred during the interaction between MDA and MP, as well as changes in the microenvironment of MP. In addition, thermodynamically analyzed, the type of binding force between the two is hydrophobic. However, the binding of MDA to MP was not stable. Using the molecular docking technique, it was found that MDA could bind to the enzymatic site on MP. These results suggest that MDA is hindering digestion by disrupting the enzymatic site on MP. This work contributes to the understanding of the relationship between changes in protein properties during meat processing and the variability of digestion, thereby improving the meat quality of aquatic products.