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A novel serine alkaline protease from Bacillus altitudinis GVC11 and its application as a dehairing agent

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Abstract

A serine alkaline protease from a newly isolated alkaliphilic Bacillus altitudinis GVC11 was purified and characterized. The enzyme was purified to homogeneity by acetone precipitation, DEAE-cellulose anion exchange chromatography with 7.03-fold increase in specific activity and 15.25% recovery. The molecular weight of alkaline protease was estimated to be 28 kDa by SDS PAGE and activity was further assessed by zymogram analysis. The enzyme was highly active over a wide range of pH 8.5 to 12.5 with an optimum pH of 9.5. The optimum temperature of purified enzyme was 45 °C and Ca2+ further increased the thermal stability of the enzyme. The enzyme activity was enhanced by Ca2+ and Mg2+ and inhibited by Hg2+. The present study is the first report to examine and describe production of highly alkaline protease from Bacillus altitudinis and also its remarkable dehairing ability of goat hide in 18 h without disturbing the collagen and hair integrity.

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Acknowledgments

We acknowledge Council of Scientific & Industrial Research, Govt. of India for financial support to carry out this research work.

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Correspondence to Gopal Reddy.

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Vijay Kumar, E., Srijana, M., Kiran Kumar, K. et al. A novel serine alkaline protease from Bacillus altitudinis GVC11 and its application as a dehairing agent. Bioprocess Biosyst Eng 34, 403–409 (2011). https://doi.org/10.1007/s00449-010-0483-x

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  • DOI: https://doi.org/10.1007/s00449-010-0483-x

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