Effect of Cathepsins B, L, L-Like and Calpain on the Protein Degradation of Surimi View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1999

AUTHORS

Shann-Tzong Jiang , Gen-Hung Chen

ABSTRACT

When the purified cathepsins B, L and L-like were subjected to freezing and 8 weeks frozen storage at -40°C, there were still more than 80% activities of cathepsins B and L, and 40% of cathepsin L-like left. Furthermore, over 80% activities of cathepsins B + L + L-like and cal-pain were left in surimi, and these proteases were responsible for most of the protein degradation in surimi during storage and the setting process. Addition of cystatin or E-64 substantially inhibited the proteolytic changes. These phenomena suggested that cathepsins B, L, L-like and calpain in fish muscle were very difficult to remove through washing treatment and also very stable during frozen storage. Protein degradation caused by these enzymes during storage deteriorated the network structure of surimi gel formed during setting process. This paper aims to report the properties of these endogenous proteinases, their effects on the protein degradation during storage, and deterioration of the protein network structure formed on setting of minced fish products. More... »

PAGES

393-405

Book

TITLE

Quality Attributes of Muscle Foods

ISBN

978-1-4613-7144-1
978-1-4615-4731-0

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-4731-0_26

DOI

http://dx.doi.org/10.1007/978-1-4615-4731-0_26

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012181188


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59 schema:description When the purified cathepsins B, L and L-like were subjected to freezing and 8 weeks frozen storage at -40°C, there were still more than 80% activities of cathepsins B and L, and 40% of cathepsin L-like left. Furthermore, over 80% activities of cathepsins B + L + L-like and cal-pain were left in surimi, and these proteases were responsible for most of the protein degradation in surimi during storage and the setting process. Addition of cystatin or E-64 substantially inhibited the proteolytic changes. These phenomena suggested that cathepsins B, L, L-like and calpain in fish muscle were very difficult to remove through washing treatment and also very stable during frozen storage. Protein degradation caused by these enzymes during storage deteriorated the network structure of surimi gel formed during setting process. This paper aims to report the properties of these endogenous proteinases, their effects on the protein degradation during storage, and deterioration of the protein network structure formed on setting of minced fish products.
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