Effectiveness of L-arginine/L-lysine in retarding deterioration of structural and gelling properties of duck meat myofibrillar protein during freeze-thaw cycles  

作　　者：Mengmeng Li Shufeng He Yangying Sun Daodong Pan Changyu Zhou Jun He 

机构地区：[1]State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products,Ningbo University,Ningbo,315211,PR China [2]Key Laboratory of Animal Protein Food Deep Processing Technology of Zhejiang Province,Zhejiang-Malaysia Joint Research Laboratory for Agricultural Product Processing and Nutrition,College of Food and Pharmaceutical Sciences,Ningbo University,Ningbo,315800,PR China

出　　处：《Food Bioscience》2023年第1期737-744,共8页食品生物科学（英文）

基　　金：supported by Zhejiang Province Basic Public Welfare Research Program(LGN21C200009);China,National Modern Agriculture Industry Technology System(CARS-42-25),China.

摘　　要：This study aimed to investigate the protective effects of L-arginine(L-arg)and L-lysine(L-lys)on the structure and gel properties of myofibrillar protein(MP)in duck meat during several freeze-thaw(F-T)cycles.The analysis of the Ca2+-ATPase activity as well as total sulfhydryl and carbonyl contents demonstrated that L-arg and L-lys could slow down the oxidative denaturation of MP during F-T cycles.Circular dichroism,fluorescence spectroscopy,and rheology measurements indicated that L-arg and L-lys improved the stability of the secondary and tertiary structure of MP and preserved its gel properties.In summary,L-arg and L-lys had the potential to preserve the structural stability and gel properties of MP during F-T cycles.

关 键 词：L-ARGININE L-LYSINE Myofibrillar protein GELLING Freeze-thaw cycle Protein structure 

分 类 号：TS201[轻工技术与工程—食品科学]