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Journal of Applied Sciences
  Year: 2001 | Volume: 1 | Issue: 3 | Page No.: 405-408
DOI: 10.3923/jas.2001.405.408
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Purification and Some Properties of Acid Protease from Penicillium expansum
M. Umar Dahot

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.
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How to cite this article:

M. Umar Dahot , 2001. Purification and Some Properties of Acid Protease from Penicillium expansum. Journal of Applied Sciences, 1: 405-408.

DOI: 10.3923/jas.2001.405.408








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