Evaluating endogenous protease of salting exudates during the salting process of Jinhua ham. (March 2019)

• Record Type: Journal Article
• Authors: Zhou, Chang-Yu; Pan, Dao-Dong; Bai, Yun; Li, Chun-Bao; Xu, Xing-Lian; Zhou, Guang-Hong; Cao, Jin-Xuan
• Is Part Of: Lebensmittel-Wissenschaft + Technologie =. Volume 101(2019)
• Page Start: 76
• Page End: 82
• Publication Date: 2019-03
• Subjects: Jinhua ham -- NaCl levels -- Salting exudates -- Protease activities -- Western blot; Food industry and trade -- Periodicals; Food -- Composition -- Periodicals; Microbiology -- Periodicals; Nutrition -- Periodicals; 664.005
• DOI: 10.1016/j.lwt.2018.11.026
• Languages: English
• ISSNs: 0023-6438

Abstract

Abstract: Strategies are being pursued with the aim of reducing salt content of dry-cured ham. To evaluate the effect of salting on protease activities, sixteen hams were randomly assigned into two groups (LS group and HS group), and two different levels of NaCl were used to dry-cure green ham. The LS group of 8 hams were salted with 6% salt (w/w), whereas the HS group of 8 hams were salted with 8% salt. The exudates were collected separately at 1, 2 and 7 d of the salting stage. The activities and contents of protease in the exudates were investigated. The intense activities of calpains, cathepsin B and L were observed at 1, 2 and 7 d of salting stage in both LS and HS group. The increased contents of 80 and 76 kDa fragments implied that there was a dramatic release of calpain from ham tissues; lower release rates of cathepsin B and cathepsin L led to high residues in LS group, which may be responsible for the intense degradation of proteins and flavor development of dry-cured ham. This paper provides new insights into the study of biochemical changes of Jinhua ham induced by endogenous protease during the salting stage. Highlights: Salting accelerated the formation of protein-rich exudates. Calpains, cathepsin B, H and L were the main endogenous proteases of the exudates. The changes of 80 and 76 kDa explained the difference of calpains activities between LS and HS. High residues of cathepsin B and L imply the key role in degrading proteins.