Heat Inactivation of Proteolytic Enzymes in Papaya Latex

Papaya Latex에 있는 단백질분해효소(蛋白質分解酪素)들의 열불활성(熱不活性)에 관하여

  • Published : 1980.09.30

Abstract

Proteases from papaya latex were partially purified by ammonium sulfate precipitation and separated into two fractions (Fraction I and II ) by carboxymethyl cellelose column chromatography. Each fraction, mixture of the two fractions, and crude extract of the papaya latex at pH 7.0 were inactivated at the range of $60{\sim}90^{\circ}C$ and thermal properties of the enzymes were investigated. In the thermal inactivation of fraction I, the enthalpy of activation was 89.5 kJ/mol; the entropy of activation, -44.0 J/mol K; the free energy of activation, 104.6 kJ/mol; z-value, $25^{\circ}C$. For fraction II, the enthalpy of activation was 96.5 kJ,/mol; the entropy of activation, -22.0 J/mol K; the free energy of activation, 104.0 kJ/mol; z-value, $23^{\circ}C$. For the mixture of fraction I and II, the enthalpy of activation was 90.9 kJ/mol; the entropy of activation, -38.8 J/mol·K; the free energy of activation, 104.2 kJ/mol; z-value, $24.6^{\circ}C$. For crude extract, the enthalpy of activation was 113.8 kJ/mol; the entropy of activation, 22.0 J/mol·K; the free energy of activation, 106.2 kJ/mol; z-value, $23.2^{\circ}C$. It was indicated that the fraction I was more heat-stable than the fraction II and this suggested that the thermal stability of the proteases in papaya latex is probably due to the fraction I.

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