Investigation of conformational changes of cathepsin B as a feasibility assessment for NaCl reduction in Jinhua ham  

作　　者：Shiqi Hu Guanghong Zhou Xinglian Xu Wangang Zhang Chunbao Li 

机构地区：[1]Key Laboratory of Meat Processing and Quality Control,Ministry of Education,Key Laboratory of Meat Processing,Ministry of Agriculture and Rural Affairs,Jiangsu Synergetic Innovation Center of Meat Processing and Quality Control,College of Food Science and Technology,Nanjing Agricultural University,Nanjing 210095,China [2]School of Life Science and Food Engineering,Huaiyin Institute of Technology,Huai’an 223003,China

出　　处：《Food Science and Human Wellness》2025年第2期429-438,共10页食品科学与人类健康(英文)

基　　金：supported by the National Natural Science Foundation of China(31972097);Jiangsu Key Research and Development Plan(Modern Agriculture)(BE2020302);the Natural Science Foundation of the Jiangsu Higher Education Institutions of China(24KJB550003);2024 Huaiyin Institute of Technology Talent Recruitment Research Startup Fund Project(Z301B24521)。

摘　　要：To regulate the sodium chloride content in Jinhua ham,the impact of NaCl on the activity and conformation of cathepsin B was investigated using spectroscopy and computational methods.The results showed that the activity of cathepsin B decreased with an increase in Na^(+)cation content and temperature.Additionally,decreasedα-helix content and increasedβ-sheet content were observed.The increase in sulfhydryl group content was attributed to the breaking of original disulfide bonds in the molecular structure or the release of embedded groups.Furthermore,the surface hydrophobicity gradually declined,which was consistent with the analysis of endogenous fluorescence spectroscopy.At the molecular level,the number of hydrogen bonds formed in NaCl-treated samples decreased,and the interactions between the hydrogen bonding were less powerful,which caused instability in the binding of the protein and substrate.The conformation of cathepsin B accurately characterized its activity,and the structural changes had a macroscopic effect on the decrease in protease activity.

关 键 词：Protein conformation Cathepsin B activity Jinhua ham Molecular docking Molecular dynamics 

分 类 号：O62[理学—有机化学]