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

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Quality Attributes of Muscle Foods

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.

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Authors and Affiliations

  1. Department of Food Science, National Taiwan Ocean University, Keelung, 202, Taiwan,ROC

    Shann-Tzong Jiang & Gen-Hung Chen

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  1. Shann-Tzong Jiang
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  1. University of Kentucky, Lexington, Kentucky, USA

    Youling L. Xiong

  2. The State University of New Jersey, Rutgers New Brunswick, New Jersey, USA

    Ho Chi-Tang

  3. Memorial University of Newfoundland, St. John’s, Newfoundland, Canada

    Fereidoon Shahidi

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Jiang, ST., Chen, GH. (1999). Effect of Cathepsins B, L, L-Like and Calpain on the Protein Degradation of Surimi. In: Xiong, Y.L., Chi-Tang, H., Shahidi, F. (eds) Quality Attributes of Muscle Foods. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4731-0_26

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  • DOI: https://doi.org/10.1007/978-1-4615-4731-0_26

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