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Calpain activation and proteolysis in postmortem goose muscles.
Anim Sci J. 2020 Jan; 91(1):e13423.AS

Abstract

Meat tenderness is considered as the most important criterion for meat quality by consumers and can be improved by the actions of endogenous proteases, mainly calpains, during postmortem storage at 0-5°C. The purpose of this study, therefore, was to examine the postmortem calpain activation and proteolysis in breast (BM) and leg and thigh (LM) muscles of White Roman goose. BM and LM were taken from goose carcasses (n = 15) at 0 (10-15 min postmortem), 1, 3, and 7 days of storage at 5°C. The decrease in postmortem pH, calpain-1 and -11 activities, and contents of the calpain-1 80 kDa subunit and desmin was more rapid (p < .05) in BM than in LM. Our results show that postmortem proteolysis was more extensive in BM than in LM of White Roman goose, not only because the difference in fiber type composition between two muscles, but because the rate and extent of calpain activation were greater in BM as well. These results may provide useful information to optimize meat processing for different muscles in goose industry.

Authors+Show Affiliations

Department of Animal Science, Chinese Culture University, Taipei City, Taiwan.Department of Animal Science, National Chiayi University, Chiayi City, Taiwan.Department of Animal Science, Iowa State University, Ames, IA, USA.Department of Animal Science, National Chiayi University, Chiayi City, Taiwan.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32648277

Citation

Chang, Ya-Shiou, et al. "Calpain Activation and Proteolysis in Postmortem Goose Muscles." Animal Science Journal = Nihon Chikusan Gakkaiho, vol. 91, no. 1, 2020, pp. e13423.
Chang YS, Wu SY, Stromer MH, et al. Calpain activation and proteolysis in postmortem goose muscles. Anim Sci J. 2020;91(1):e13423.
Chang, Y. S., Wu, S. Y., Stromer, M. H., & Chou, R. R. (2020). Calpain activation and proteolysis in postmortem goose muscles. Animal Science Journal = Nihon Chikusan Gakkaiho, 91(1), e13423. https://doi.org/10.1111/asj.13423
Chang YS, et al. Calpain Activation and Proteolysis in Postmortem Goose Muscles. Anim Sci J. 2020;91(1):e13423. PubMed PMID: 32648277.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Calpain activation and proteolysis in postmortem goose muscles. AU - Chang,Ya-Shiou, AU - Wu,Shin-Yi, AU - Stromer,Marvin H, AU - Chou,Rong-Ghi R, PY - 2020/02/10/received PY - 2020/05/24/revised PY - 2020/06/04/accepted PY - 2020/7/11/entrez KW - calpain KW - goose muscle KW - postmortem proteolysis KW - tenderization SP - e13423 EP - e13423 JF - Animal science journal = Nihon chikusan Gakkaiho JO - Anim. Sci. J. VL - 91 IS - 1 N2 - Meat tenderness is considered as the most important criterion for meat quality by consumers and can be improved by the actions of endogenous proteases, mainly calpains, during postmortem storage at 0-5°C. The purpose of this study, therefore, was to examine the postmortem calpain activation and proteolysis in breast (BM) and leg and thigh (LM) muscles of White Roman goose. BM and LM were taken from goose carcasses (n = 15) at 0 (10-15 min postmortem), 1, 3, and 7 days of storage at 5°C. The decrease in postmortem pH, calpain-1 and -11 activities, and contents of the calpain-1 80 kDa subunit and desmin was more rapid (p < .05) in BM than in LM. Our results show that postmortem proteolysis was more extensive in BM than in LM of White Roman goose, not only because the difference in fiber type composition between two muscles, but because the rate and extent of calpain activation were greater in BM as well. These results may provide useful information to optimize meat processing for different muscles in goose industry. SN - 1740-0929 UR - https://www.unboundmedicine.com/medline/citation/32648277/Calpain_activation_and_proteolysis_in_postmortem_goose_muscles L2 - https://doi.org/10.1111/asj.13423 DB - PRIME DP - Unbound Medicine ER -
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