Freeze Denaturation of Carp Myofibrils Compared with Thermal Denaturation

• Azuma Yumiko

  Laboratory of Food Biochemistry, Faculty of Fisheries, Hokkaido University

• Konno Kunihiko

  Laboratory of Food Biochemistry, Faculty of Fisheries, Hokkaido University

書誌事項

タイトル別名

• Freeze Denaturation of Carp Myofibrils

抄録

The Freeze denaturation mechanism of myofibrils was investigated by comparing with the thermal denaturation. Mg²⁺-ATPase activity enhancement was brought about in these two denaturation systems, whereas Ca-sensitivity loss was accompanied only in the thermal denaturation. Frozen storage slightly decreased the salt-solubility as well as myosin extractability. The latter change was rather similar to the Ca²⁺-ATPase inactivation profile. This was in contrast to the case of thermal denaturation, in which myosin extractability as well as solubility dropped very quickly preceding the Ca²⁺-ATPase inactivation. It was, therefore, concluded that the structural change of myosin caused by freezing is different from that by heating. Myosin rod, a region responsible for the salt solubility of myosin, was suggested to remain undamaged during the frozen storage. It was also found that, when once frozen, myofibrils readily lost their salt solubility upon subsequent heating. It was thus demonstrated that the thermal denaturation process was greatly affected by freezing before heating.

収録刊行物

• Ｆｉｓｈｅｒｉｅｓ　ｓｃｉｅｎｃｅ

  Ｆｉｓｈｅｒｉｅｓ　ｓｃｉｅｎｃｅ 64 (2), 287-290, 1998

  公益社団法人 日本水産学会

キーワード

• myofibril
• myosin
• ATPase
• freeze denaturation
• frozen storage

詳細情報

• CRID: 1390001204427748608
• NII論文ID: 130003742149
• NII論文ID: 10004874001
• NII書誌ID: AA10993718
• DOI: 10.2331/fishsci.64.287
• NDL書誌ID: 4462733
• ISSN: 09199268
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I4462733
• Web Site: https://www.jstage.jst.go.jp/article/fishsci1994/64/2/64_2_287/_pdf
• 本文言語コード: en
• データソース種別:
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  • NDL
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可