Studies on the Acid-protease ofPaecilomyces variotiBainier TPR-220

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  • Studies on the Acid-protease of <i>Paecilomyces varioti</i> Bainier TPR-220
  • Part II. Some Enzymic Properties of the Crystalline Acid-protease

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Some enzymic properties of the crystalline acid-protease of Paecilomyces varioti Bainier TPR-220 were studies.<br> 1. The presend acid-protease is most active at pH 3.0 at 60°C toward casein, and can also hydrolyses egg albumin, horse hemoglobin denatured with hydrochloric acid or urea, and blood fibrin.<br> 2. This enzyme is most stable around pH 5, and when incubated at pH 3.0 and 5.0 at 55°C for four hours, it lost 95 and 45% of the activity respectively.<br> 3. No metal ion is essential to the enzymic action, and the enzyme is inhibited by some of sulfhydryl reagents but is not a papainase.<br> 4. The presence of Ca++, Co++, Cu++, Mg++, Mn++, Sr++, and Zn++ ions prevents the heat inactivation of the enzyme at pH 5.0 and 60°C to some extent but does not at pH 3.0. EDTA shows the same action.<br> 5. The enzyme decomposes casein into smaller fragments than pepsin does.

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