Partial Purification and Characterization of Chinook Salmon (Oncorhynchus tshawytscha) Calpains and an Evaluation of Their Role in Postmortem Proteolysis

• Published in: Journal of food science Vol. 65; no. 8; pp. 1318 - 1324
• Main Authors: Geesink, G.H., Morton, J.D., Kent, M.P., Bickerstaffe, R.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.11.2000; Institute of Food Technologists; Wiley Subscription Services, Inc
• Subjects: Biological and medical sciences; calpain; Fish; Fish and seafood industries; Food industries; Food science; Fundamental and applied biological sciences. Psychology; muscle; Muscular system; Oncorhynchus tshawytscha; proteolysis; Refrigeration; salmon; Seafood; Biodegradation; Edible fish; Oncorhynchus tshawytscha; Enzyme; Salmon; Cysteine endopeptidases; Postmortem; Calpain; Peptidases; Vertebrata; Storage; Refrigerated storage; Proteolysis; Pisces; Postmortem changes; Hydrolases
• ISSN: 0022-1147; 1750-3841
• DOI: 10.1111/j.1365-2621.2000.tb10605.x

The involvement of calpains in the proteolysis of salmon muscle during refrigerated storage was investigated. Salmon m‐calpain and μ‐calpain were purified and partially purified, respectively. Salmon μ‐calpain had similar calcium requirements and specific activity against casein as ovine m‐calpain. Salmon μ‐calpain had similar calcium requirements as ovine μ‐calpain but a lower specific activity against casein than ovine μ‐calpain. Autolysis patterns of both calpains differed from those of ovine calpains, and their activities were less than those of mammalian muscles. Calpastatin activity was relatively high and comparable to that of bovine muscles. Little proteolysis and fiber fragmentation resulted during refrigerated storage. However, proteolysis could be reproduced by incubation of myofibrils with m‐calpain.