Physicochemical changes in Pacific whiting muscle proteins during iced storage

Soottawat Benjakul; Thomas A. Seymour; Michael T. Morrissey; Haejung An

doi:10.1111/j.1365-2621.1997.tb15445.x

Physicochemical changes in Pacific whiting muscle proteins during iced storage

Soottawat Benjakul
, Thomas A. Seymour
, Michael T. Morrissey
, Haejung An

Prince of Songkla University
Oregon State University

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

478 Citations (Scopus)

Abstract

No changes in actomyosin Ca²⁺-, Mg²⁺-, or Mg²⁺-Ca²⁺-ATPase activities were observed during iced storage of Pacific whiting fillets, but Mg²⁺-EGTA-ATPase increased with a loss of Ca²⁺-sensitivity. Surface hydrophobicity of actomyosin increased substantially within 2 days, but not total sulfhydryl (SH) content. During longer storage, the SH content decreased gradually, but surface hydrophobicity remained constant. Autolytic degradation products increased in fish muscle with storage time. Myosin heavy chain (MHC) was degraded by 45% within 8 days, but no noticeable difference was observed in actin. Results indicated that autolysis may be the main cause of physicochemical changes in Pacific whiting muscle proteins during iced storage.

Original language	English
Pages (from-to)	729-733
Number of pages	5
Journal	Journal of Food Science
Volume	62
Issue number	4
DOIs	https://doi.org/10.1111/j.1365-2621.1997.tb15445.x
Publication status	Published - 1997
Externally published	Yes

Keywords

ATPase
Actomyosin
Muscle proteins
Pacific whiting

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10.1111/j.1365-2621.1997.tb15445.x

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title = "Physicochemical changes in Pacific whiting muscle proteins during iced storage",

abstract = "No changes in actomyosin Ca2+-, Mg2+-, or Mg2+-Ca2+-ATPase activities were observed during iced storage of Pacific whiting fillets, but Mg2+-EGTA-ATPase increased with a loss of Ca2+-sensitivity. Surface hydrophobicity of actomyosin increased substantially within 2 days, but not total sulfhydryl (SH) content. During longer storage, the SH content decreased gradually, but surface hydrophobicity remained constant. Autolytic degradation products increased in fish muscle with storage time. Myosin heavy chain (MHC) was degraded by 45\% within 8 days, but no noticeable difference was observed in actin. Results indicated that autolysis may be the main cause of physicochemical changes in Pacific whiting muscle proteins during iced storage.",

keywords = "ATPase, Actomyosin, Muscle proteins, Pacific whiting",

author = "Soottawat Benjakul and Seymour, \{Thomas A.\} and Morrissey, \{Michael T.\} and Haejung An",

year = "1997",

doi = "10.1111/j.1365-2621.1997.tb15445.x",

language = "English",

volume = "62",

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journal = "Journal of Food Science",

issn = "0022-1147",

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TY - JOUR

T1 - Physicochemical changes in Pacific whiting muscle proteins during iced storage

AU - Benjakul, Soottawat

AU - Seymour, Thomas A.

AU - Morrissey, Michael T.

AU - An, Haejung

PY - 1997

Y1 - 1997

N2 - No changes in actomyosin Ca2+-, Mg2+-, or Mg2+-Ca2+-ATPase activities were observed during iced storage of Pacific whiting fillets, but Mg2+-EGTA-ATPase increased with a loss of Ca2+-sensitivity. Surface hydrophobicity of actomyosin increased substantially within 2 days, but not total sulfhydryl (SH) content. During longer storage, the SH content decreased gradually, but surface hydrophobicity remained constant. Autolytic degradation products increased in fish muscle with storage time. Myosin heavy chain (MHC) was degraded by 45% within 8 days, but no noticeable difference was observed in actin. Results indicated that autolysis may be the main cause of physicochemical changes in Pacific whiting muscle proteins during iced storage.

AB - No changes in actomyosin Ca2+-, Mg2+-, or Mg2+-Ca2+-ATPase activities were observed during iced storage of Pacific whiting fillets, but Mg2+-EGTA-ATPase increased with a loss of Ca2+-sensitivity. Surface hydrophobicity of actomyosin increased substantially within 2 days, but not total sulfhydryl (SH) content. During longer storage, the SH content decreased gradually, but surface hydrophobicity remained constant. Autolytic degradation products increased in fish muscle with storage time. Myosin heavy chain (MHC) was degraded by 45% within 8 days, but no noticeable difference was observed in actin. Results indicated that autolysis may be the main cause of physicochemical changes in Pacific whiting muscle proteins during iced storage.

KW - ATPase

KW - Actomyosin

KW - Muscle proteins

KW - Pacific whiting

UR - https://www.scopus.com/pages/publications/0031462866

U2 - 10.1111/j.1365-2621.1997.tb15445.x

DO - 10.1111/j.1365-2621.1997.tb15445.x

M3 - Article

AN - SCOPUS:0031462866

SN - 0022-1147

VL - 62

SP - 729

EP - 733

JO - Journal of Food Science

JF - Journal of Food Science

IS - 4

ER -

Physicochemical changes in Pacific whiting muscle proteins during iced storage

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Keywords

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