Gelation of low salt soluble proteins from scallop adductor muscle in relation to its freshness.

• NIKI TOMOMI

  Laboratory of Food Biochemistry, Graduate School of Fisheries Sciences, Hokkaido University

• KATO YUKO

  Laboratory of Food Biochemistry, Graduate School of Fisheries Sciences, Hokkaido University

• NOZAWA HISANORI

  Laboratory of Food Biochemistry, Graduate School of Fisheries Sciences, Hokkaido University

• SEKI NOBUO

  Laboratory of Food Biochemistry, Graduate School of Fisheries Sciences, Hokkaido University

Abstract

The low salt extract from scallop striated adductor muscle contained extra proteins in addition to sarcoplasmic proteins and was turned into a gel upon standing or immediately by the addition of Ca²⁺. The amount of extra protein, which was composed of a large amount of actin and a small amount of myosin, decreased with a decrease in adenosine triphosphate (ATP) content in the muscle during storage at 5°C. Actin was easily extracted from scallop myofibrils in low salt solution with ATP at 1 mM or above. Furthermore, ATP was required to induce the gelation of the low salt extract. A visual observation of the gelation of low salt extract is therefore a simple and easy method to inspect prerigor state of scallop adductor muscle.

Journal

• Fisheries science

  Fisheries science 68 (3), 688-693, 2002

  The Japanese Society of Fisheries Science

Keywords

• actin
• adductor muscle
• adenosine triphosphate
• extract
• freshness
• gelation
• rigor
• scallop
• storage

Details

• CRID: 1390001204428926720
• NII Article ID: 10008558449
• NII Article ID: 30014677887
• NII Book ID: AA10993718
• DOI: 10.1046/j.1444-2906.2002.00478.x
• ISSN: 14442906
• ISSN: 09199268
• NDL BIB ID: 6195165
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6195165
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed