• Title/Summary/Keyword: protein denaturation under high pressure

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Denaturation of Heat Treated Lysozyme under High Pressure Conditions (고압조건에서 가열 처리된 Iysozyme의 변성)

  • Cho, Rae-Kwang;Hong, Jin-Hwan
    • Korean Journal of Food Science and Technology
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    • v.23 no.3
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    • pp.366-369
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    • 1991
  • In order to elucidate texturization mechanism of extrudated protein, egg white lysozyme was heated under high pressure conditions, and its solubility and changes of molecular weight were investigated. Under high pressure conditions of $100,\;300\;and\;600\;kg/cm^2$, solubility decreased gradually with increasing temperature in the samples heated at $70,\;120\;and\;150^{\circ}C$ and decreased notably with increasing pressure at $200^{\circ}C$. Polymerization was found in the samples heated at $150\;and\;200^{\circ}C$ while a band which located below monomer(low-molecular) could be recognized. Molecular weight of the low-molecular was estimated to be about $6,000{\sim}9,000$ and no smaller peptide was recognized. The polymerization may have occured by disulfide crosslinking in the samples heated at $120^{\circ}C$ but other crosslinking may have played a role in those at $150\;and\;200^{\circ}C$.

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