Enzyme-catalyzed Cross-linking and Degradation of Myosin Heavy Chain in Walleye Pollack Surimi Paste during Setting

• Takeda Hirofumi

  Laboratory of Food Biochemistry, Faculty of Fisheries, Hokkaido University

• Seki Nobuo

  Laboratory of Food Biochemistry, Faculty of Fisheries, Hokkaido University

書誌事項

タイトル別名

• Enzyme-catalyzed Cross-linking and Degr

抄録

Walleye pollack surimi paste was incubated (set) at 25, 35, 45, and 55°C in the presence of either transglutaminase (TGase) inhibitor or protease inhibitor. In the absence of inhibitors, cross-linking of myosin heavy chains and formation of 150 kDa component occurred at the same time during the incubation at 25°C.<br> Inhibition of endogenous TGase resulted in complete suppression of myosin cross-linking, while it did not suppress the formation of 150 kDa component. The cross-linking was also depressed above 45°C due to the inactivation of TGase. On the other hand, the addition of E-64, a cysteine protease inhibitor, suppressed completelyand partially the formation of 150 kDa component at 25 and 55°C, respectively. Together with these results, the 150 kDa component might be a proteolytic fragment of myofibrillar proteins, possibly myosin.<br> The proteolysis as well as the cross-linking of myosin during the setting affected the textural properties of final cooked gels.

収録刊行物

• Ｆｉｓｈｅｒｉｅｓ　ｓｃｉｅｎｃｅ

  Ｆｉｓｈｅｒｉｅｓ　ｓｃｉｅｎｃｅ 62 (3), 462-467, 1996

  公益社団法人 日本水産学会

キーワード

• setting
• protease
• transglutaminase
• surimi

詳細情報

• CRID: 1390282679406793728
• NII論文ID: 130003741999
• NII論文ID: 10004866401
• NII書誌ID: AA10993718
• DOI: 10.2331/fishsci.62.462
• NDL書誌ID: 3978848
• ISSN: 09199268
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I3978848
• Web Site: https://www.jstage.jst.go.jp/article/fishsci1994/62/3/62_3_462/_pdf
• 本文言語コード: en
• データソース種別:
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  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可