文献类型：期刊文献

英文题名：Insight into the Interaction of Malondialdehyde with Rabbit Meat Myofibrillar Protein: Fluorescence Quenching and Protein Oxidation

作者：Chen, Xiaosi[1];He, Zhifei[1,2,3];Wang, Zefu[4];Li, Hongjun[1,2,3]

机构：[1]Southwest Univ, Coll Food Sci, 2 Tiansheng Rd, Chongqing 400715, Peoples R China;[2]Chongqing Engn Res Ctr Reg Food, 2 Tiansheng Rd, Chongqing 400715, Peoples R China;[3]Chongqing Key Lab Special Food Cobuilt Sichuan & C, 2 Tiansheng Rd, Chongqing 400715, Peoples R China;[4]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524088, Peoples R China

年份：2023

卷号：12

期号：10

外文期刊名：FOODS

收录：SCI-EXPANDED(收录号：WOS:000998103900001)、、Scopus(收录号：2-s2.0-85160532252)、WOS

基金：This research was funded by Chongqing Technology Innovation and Application Development Special Key Project (CSTB2022TIAD-KPX0080), Collaborative Innovation and Key Technology of Rabbit Industry in Sichuan and Chongqing (2022YFQ0033), China Agriculture Research System of MOF and MARA (CARS-43-E-2).

语种：英文

外文关键词：mediated oxidation; structural change; addition reaction; dynamic quenching; first-order kinetics

外文摘要：This research explored the effects of oxidative modification caused by different malondialdehyde (MDA) concentrations on rabbit meat myofibrillar protein (MP) structural characteristics and the interactions between MDA and MP. The fluorescence intensity of MDA-MP adducts, and surface hydrophobicity increased, whereas the intrinsic fluorescence intensity and free-amine content of MPs decreased as MDA concentration and incubation time increased. The carbonyl content was 2.06 nmol/mg for native MPs, while the carbonyl contents increased to 5.17, 5.57, 7.01, 11.37, 13.78, and 23.24 nmol/mg for MP treated with 0.25 to 8 mM MDA, respectively. When the MP was treated with 0.25 mM MDA, the sulfhydryl content and the a-helix content decreased to 43.78 nmol/mg and 38.46%, while when MDA concentration increased to 8 mM, the contents for sulfhydryl and a-helix decreased to 25.70 nmol/mg and 15.32%. Furthermore, the denaturation temperature and ?H decreased with the increase in MDA concentration, and the peaks disappeared when the MDA concentration reached 8 mM. Those results indicate MDA modification resulted in structural destruction, thermal stability reduction, and protein aggregation. Besides, the first-order kinetics and Stern-Volmer equation fitting results imply that the quenching mechanism of MP by MDA may be mainly driven by dynamic quenching.