Biochemical and conformation changes of actomyosin from threadfin bream stored in ice

J. Yongswawatdigul; J. W. Park

doi:10.1111/j.1365-2621.2002.tb09440.x

Biochemical and conformation changes of actomyosin from threadfin bream stored in ice

J. Yongswawatdigul, J. W. Park

Department of Food Technology

Research output: Contribution to journal › Article › peer-review

31 Citations (Scopus)

Abstract

Biochemical and conformational changes of actomyosin stored in ice were investigated. The K-value of threadfin bream increased from 9% to 40% after storage for 12 d. Ca²⁺-, EDTA-, Mg²⁺-, and Mg²⁺-Ca²⁺-ATPase activities of actomyosin decreased, whereas Mg²⁺-EGTA ATPase activities increased. Total SH content of actomyosin increased after 3 d and decreased thereafter. Surface hydrophobicity gradually increased within 6 d. Protein loss during washing increased with storage time. A signifcant reduction (50%) of breaking force of thrice-washed mince was observed in fish stored in ice for 6 d. There was no evidence of proteolysis of muscle proteins stored up to 9 d as shown with SDS-PAGE.

Original language	English
Pages (from-to)	985-990
Number of pages	6
Journal	Journal of Food Science
Volume	67
Issue number	3
DOIs	https://doi.org/10.1111/j.1365-2621.2002.tb09440.x
Publication status	Published - 2002

Keywords

Actomyosin
Post-harvest
Protein conformation
Threadfin bream

ASJC Scopus subject areas

Food Science

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10.1111/j.1365-2621.2002.tb09440.x

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title = "Biochemical and conformation changes of actomyosin from threadfin bream stored in ice",

abstract = "Biochemical and conformational changes of actomyosin stored in ice were investigated. The K-value of threadfin bream increased from 9% to 40% after storage for 12 d. Ca2+-, EDTA-, Mg2+-, and Mg2+-Ca2+-ATPase activities of actomyosin decreased, whereas Mg2+-EGTA ATPase activities increased. Total SH content of actomyosin increased after 3 d and decreased thereafter. Surface hydrophobicity gradually increased within 6 d. Protein loss during washing increased with storage time. A signifcant reduction (50%) of breaking force of thrice-washed mince was observed in fish stored in ice for 6 d. There was no evidence of proteolysis of muscle proteins stored up to 9 d as shown with SDS-PAGE.",

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T1 - Biochemical and conformation changes of actomyosin from threadfin bream stored in ice

AU - Yongswawatdigul, J.

AU - Park, J. W.

PY - 2002

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N2 - Biochemical and conformational changes of actomyosin stored in ice were investigated. The K-value of threadfin bream increased from 9% to 40% after storage for 12 d. Ca2+-, EDTA-, Mg2+-, and Mg2+-Ca2+-ATPase activities of actomyosin decreased, whereas Mg2+-EGTA ATPase activities increased. Total SH content of actomyosin increased after 3 d and decreased thereafter. Surface hydrophobicity gradually increased within 6 d. Protein loss during washing increased with storage time. A signifcant reduction (50%) of breaking force of thrice-washed mince was observed in fish stored in ice for 6 d. There was no evidence of proteolysis of muscle proteins stored up to 9 d as shown with SDS-PAGE.

AB - Biochemical and conformational changes of actomyosin stored in ice were investigated. The K-value of threadfin bream increased from 9% to 40% after storage for 12 d. Ca2+-, EDTA-, Mg2+-, and Mg2+-Ca2+-ATPase activities of actomyosin decreased, whereas Mg2+-EGTA ATPase activities increased. Total SH content of actomyosin increased after 3 d and decreased thereafter. Surface hydrophobicity gradually increased within 6 d. Protein loss during washing increased with storage time. A signifcant reduction (50%) of breaking force of thrice-washed mince was observed in fish stored in ice for 6 d. There was no evidence of proteolysis of muscle proteins stored up to 9 d as shown with SDS-PAGE.

KW - Actomyosin

KW - Post-harvest

KW - Protein conformation

KW - Threadfin bream

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Biochemical and conformation changes of actomyosin from threadfin bream stored in ice

Abstract

Keywords

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