Cross-linking reaction of myosin in the fish paste during setting (Suwari).

DOI JASI Web Site 63 Citations
  • NUMAKURA Tadahiro
    Training Factory for Food Processing, Faculty of Fisheries, Hokkaido University
  • SEKI Nobuo
    Laboratory of Biochemistry, Faculty of Fisheries, Hokkaido University
  • KIMURA Ikuo
    Central Research Laboratory, Nippon Suisan Co., Ltd.
  • TOYODA Kyohei
    Central Research Laboratory, Nippon Suisan Co., Ltd.
  • FUJITA Takao
    Central Research Laboratory, Nippon Suisan Co., Ltd.
  • TAKAMA Kozo
    Training Factory for Food Processing, Faculty of Fisheries, Hokkaido University
  • ARAI Ken-ichi
    Laboratory of Biochemistry, Faculty of Fisheries, Hokkaido University

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Other Title
  • すわりによる肉のりのゲル形成とミオシンの交差結合反応
  • 坐りによる肉糊のゲル形成とミオシンの交差結合反応
  • スワリ ニ ヨル ニクノリ ノ ゲル ケイセイ ト ミオシン ノ コウサ ケツ

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Abstract

The frozen surimi of Alaska pollack was ground with 3% salt. The salted paste was submitted to setting, so-called “SUWARI”, at a fixed temperature of 20°or 30°C. During the setting, a portion of the paste was taken out to assess the gel strength before and after heat treatment at 90°C for 40min. Another portion was used to solubilize protein of the paste with a medium containing SDS, urea and 2-mercaptoethanol, and to analyze the soluble protein by SDS-poly- acrylamide gel electrophoresis.<br>The solubility of the paste slightly decreased with the prolonged setting, whereas the disappearance of myosin heavy chain in it became evident when still in high solubility.<br>The increase in gel strength of both gels with and without heat treatment was accompanied by the decrease in myosin heavy chain and a concomitant produce of cross-linked myosin heavy chain with large molecular sizes. It was thus proposed that the cross-likning of myosin in salted fish paste is responsible for textural changes of the gels.

Journal

  • NIPPON SUISAN GAKKAISHI

    NIPPON SUISAN GAKKAISHI 51 (9), 1559-1565, 1985

    The Japanese Society of Fisheries Science

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