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Biochemical and Conformation Changes of Actomyosin from Threadfin Bream Stored in Ice
Authors:J. Yongswawatdigul   J.W. Park
Affiliation:Author Yongsawatdigul is with the School of Food Technology at Suranaree Univ. of Technology, Nakhon Ratchasima, 30000 Thailand. Author Park is with the Oregon State Univ. Seafood Laboratory, Astoria, OR. Direct inquiries to author Yongsawatdigul. (E-mail: ).
Abstract: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 significant 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.
Keywords:Threadfin bream    post-harvest    actomyosin    protein conformation
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