Abstract
An alkaline protease was produced and partially purified from a new strain of Aspergillus oryzae by using two chromatographies i.e. ion exchange chromatography on CM-Sephadex C-50 and gel filtration on Sephadex G-100 yielding an active major protein peak with ~29.29 purification fold. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) indicated that the purified alkaline protease is a monomeric enzyme with a molecular mass of ~33 kDa. The purified enzyme was completely inhibited by serine protease inhibitor, PMSF, and activated by Mg +2 & Ca +2 ions. The purified enzyme was immobilized by entrapment on Ca-alginate carrier. The optimum pH of the immobilized enzyme shifted to a more alkaline range (9.5) as compared with the free enzyme (9.0). It showed enhanced stability in acidic as well as alkaline environments in comparison to the free enzyme. The K
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