Thermal Inactivation of Crude Papain and Papaya Peroxidase

Papaya중의 단백질 분해 효소와 Peroxidase의 열 불활성화

  • Park, Kwan-Hwa (Department of Food Technology, College of Agriculture, Seoul National University) ;
  • Kim, Ze-Uook (Department of Food Technology, College of Agriculture, Seoul National University) ;
  • Shin, Jae-Doo (Department of Food Technology, College of Agriculture, Seoul National University) ;
  • Noh, Bong-Soo (Department of Food Technology, College of Agriculture, Seoul National University)
  • 박관화 (서울대학교 농과대학 식품공학과) ;
  • 김재욱 (서울대학교 농과대학 식품공학과) ;
  • 신재두 (서울대학교 농과대학 식품공학과) ;
  • 노봉수 (서울대학교 농과대학 식품공학과)
  • Published : 1979.09.15

Abstract

Thermal properties of crude papain and crude peroxidase from domestic papaya were investigated. The crude extract of papaya was inactivated at the temperature range of $60^{\circ}{\sim}90^{\circ}C$ at pH 7.0 and the rest of the activities of papain and peroxidase were determined, respectively. The heat inactivation of papain and papaya peroxidase was biphasic at low temperature. For the thermal inactivation of papain extract, the enthalpy of activation was 91.4 kJ/mol, the entropy of activation, -49.6 J/mol K, and the free energy of activation, 108.5 kJ/mol. The activation energy for the inactivation of papaya peroxidase was 168.5 kJ/mol, the entropy of activation, $200.4\;J/mol{\cdot}K$ and the free energy of activation, 99.7 kJ/mol. The thermal stability of papain showed that it has a possibility for use as a meat tenderizer. It was also discussed that papaya peroxidase could be more suitable as a biochemical criteria for heat treatment than papaya catalase.

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