Changes of Hydrophobicity, Solubility, SH Group and Protein-Protein Interaction in Yellowtail Myosin and Whelk Paramyosin During Thermal Denaturation

가열 변성에 따른 방어 Myosin과 갈색띠 매물고둥 Paramyosin의 소수성, 용해도, SH기 및 단백질간 상호작용의 변화

  • Choi, Yeung-Joon (Department of Nutrition and Food Science, National Fisheries University) ;
  • Pyeun, Jae-Hyeung (Department of Nutrition and Food Science, National Fisheries University)
  • 최영준 (부산수산대학 식품영양학과) ;
  • 변재형 (부산수산대학 식품영양학과)
  • Published : 1987.04.01


The denaturation mechanism of the protein during heating of myosin and paramyosin extracted from the ordinary muscle of yellowtail (Seriola qrinqueradits) and the adductor muscle of whelk (Neptunea arthritica cuming) were investigated by analyzing the hydrophobicity, solubility, SH group and protein-protein interaction. The free hydrophobic residue of the two proteins were increased by increase of heating temperature up to $65^{\circ}C$ and then decreased for further temperature raise. The protein-protein interaction was proportional to the increment of the free hydrophobic residue. The aggregation of protein was begun from $65^{\circ}C$ with the decrease of the free hydrophobic residues. The results of Arrhenius equation for the data on proteinprotein interaction showed that the denaturation course was made up with multi-steps in the myosin and two-steps in the paramyosin. The number of free hydrophobic residue and SH group, solubility and protein-protein interaction were significantly differed with the denaturation temperature (p<0.01).