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Proteolytic Activity from an Alkali-Thermotolerant Streptomyces gulbargensis sp. nov.

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Abstract

Multiple proteases were produced and partially purified from an alkali-thermotolerant novel species of Streptomyces (i.e., Streptomyces gulbargensis DAS 131) after 48 h of growth at 45°C. The enzyme preparation exhibited activity over a broad range of pH (4–12) and temperature (27–55°C). Optimum activity was observed at a pH of 9.0 and a temperature of 45°C. Starch and protease peptone was found to be a good source of carbon and nitrogen to enhance the enzyme activity. Two active zones in the range of 19 to 35 kDa were detected on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE).

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Acknowledgment

This work was supported by the 21C Frontier Microbial Genomics and Application Centre program, Ministry of Science and Technology, Republic of Korea.

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Correspondence to Agasar Dayanand.

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Dastager, S.G., Dayanand, A., Li, WJ. et al. Proteolytic Activity from an Alkali-Thermotolerant Streptomyces gulbargensis sp. nov.. Curr Microbiol 57, 638–642 (2008). https://doi.org/10.1007/s00284-008-9257-y

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  • DOI: https://doi.org/10.1007/s00284-008-9257-y

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