Optimization, Characterization, and Potential Industrial Applications of Alkaline Protease isolated from Alkaliphilic Actinobacteria BACC-15

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Date

2014-07

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Addis Ababa University

Abstract

Microbial alkaline proteases are stimulating tremendous interests in the research and enzyme market since there is a great demand for developing biotechnological alternatives for many industrial processes. Hence, this study was conducted with the aim of screening for the best alkaline protease producing alkaliphilic Actinobacteria, optimizing enzyme production in SSF; characterizing and investigation of the different industrial applications. One best producer isolate (Actinobacteria BACC-15) was selected based on different parameters. Alkaline protease production by BACC-15 in SSF was maximum at 37 (591.67±12.99 U/g) and 1:1.8 initial moisture content (595.75±9.60 U/g). The enzyme was active and stable in the pH ranges of 6.0-11.5, with optimum activity at pH 10.0 and stability at pH 7.5-9.5. It was active in temperature range of 35-75 , with optimum activity at 60 and 65 in presence of 5mM Ca2+ and highly stable at 30-50 . The enzyme was active and stable in presence of NaCl, and 8.62% enhancement was observed at 3M. Presence of high concentrations of H2O2, NaBO3.H2O, SDS, Tween-80, Triton X-100, sodium citrate and saponins had no effect on enzyme stability. The protease (84.21U/g) alone or 25% protease + 75% endod preparation in combination completely removed proteinaceous stains. Using 1% w/v E/S ratio, BACC-15 alkaline protease hydrolyzed SBPI (DH, 77.09%) and MSPI (DH, 66.19%). SBPH and MSPH were suitably used for growing pathogenic bacteria with PR of 1 compared to commercial peptone. Therefore, BACC-15 alkaline protease is potential candidate in many industrial applications as alternative to environmentally unfriendly hemicals and production of valuable products. Key words: Alkaline protease; biodetergent formulation; isolates BACC-15; protein hydrolysates; SSF;

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Alkaline protease; biodetergent formulation; isolates BACC-15; protein hydrolysates; SSF;

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