Abstract
The present study shows the isolation, partial purification and characterization of alkaline protease from the seeds of Cucumis melo var agrestis, by a four step purification process. Its molecular weight was estimated to be 54KDa. Enzyme showed maximum activity at p H 9.0 and optimum temperature at40 o Cwith casein as substrate. The enzyme exhibited homogeneity as attested by a single protein band on both native PAGE and SDS PAGE. It is a monomeric enzyme and nonglycoprotein in nature. The km value of enzyme for casein as determined by double reciprocal plot was 2.5 mg/ml. It was strongly inhibited by PMSF but not by EDTA. The results indicate that the alkaline protease is a serine protease, similar to cucumisin from sarcocarp of melon fruit.
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