Purification and Some Properties of Acid Protease from Penicillium expansum

Research Article
Purification and Some Properties of Acid Protease from Penicillium expansum

Journal of Applied Sciences, 2001, 1(3), 405-408.

Abstract

An acid protease was isolated from the culture broth of Penicillium expansum grown on rice husk (40 mesh fine powder) mineral medium. The protease enzyme was purified on Sephadex G-100 and DEAE Sephdex A-50 with recovery of 7.52%. Purified enzyme shows a single band on SDS polyacrylamide gel electrophoresis. The optimum activity of protease was found at pH 3.5 and temperature 30ºC. The activation energy for the hydrolysis of casien by acid protease was 93 KJ/mol. The enzyme activity was highly increased in the presence of CoCl₂ (71.57%), cysteine (54.23%), mercaptoethanol (44.70%), ZnCl₂ (34.78%) but slightly activated by CaCl₂ (10.24%) and MnCl₂ (1.37%). Whereas protease activity was reduced on the addition of EDTA (55.88%), AgNo₃ (67.85%) and HgNO₃)₂ (64.71%). The thermal stability of protease was increased in the presence of ZnCl₂. The half-life of acid protease in the absence and presence of ZnCl₂ at 50ºC was determined 17 and 28 minutes respectively.

ASCI-ID: 35-192

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