Setting of flesh sol induced by ethylsulfonylation.

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  • エチルスルホニル化による坐りの促進
  • エチルスルホニル化による坐りの促進〔英文〕
  • エチルスルホニルカ ニヨル スワリ ノ ソクシン エイブン

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In order to investigate the role apolar aliphatic amino acid residues of the muscle protein in the setting (the relatively low temperature gelation observed in the flesh sol from some species of fish), the elasticity of the actomyosin and flesh sols from some slow-setting species was measured after ethylsulfonylation or the addition of ethylsulfonyl chloride (ESCI), respectively. After ethysulfonylation, chicken actomyosin lost its salt-solubility and ATP-sensitivity. On heating at 40°C, the ethylsulfonylated chicken actomyosin sol first set to a gel and then the elastic modulus of the resulting gel increased, while the control actomyosin sol did not set to a gel. Sucrose suppressed the increase in the elastic modulus of the ethylsulfonylated actomyosin sol.<br> The breaking stress increased more extensively for the chicken and beef flesh sols containing ESCI (0.3 or 0.1% of the flesh mince) than for those without it during heating at 40°C. The stress in the chicken flesh sol containing ESCI 0.3% increased more than that in the chicken flesh sol containing ESCI 0.1%. On the addition of ESCI 0.1%, the expressible water of chicken flesh sol decreased gradually during heating at 40°C. Preheating the chicken and dolphinfish flesh sols further heating at 90°C for 25 min. However, no effect of preheating was observed for the gels without ESCI.

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