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Updated: Jun 30, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Proteolytic activity from an alkali-thermotolerant Streptomyces gulbargensis sp. nov
S G Dastager1, Agasar Dayanand, Wen-Jun Li
1Korea Research Institute of Bioscience and Biotechnology, 52 Oeundong, Yusong, Daejeon 305-333, Republic of Korea. syed_micro@rediffmail.com
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 degrees C. The enzyme preparation exhibited activity over a broad range of pH (4-12) and temperature (27-55 degrees C). Optimum activity was observed at a pH of 9.0 and a temperature of 45 degrees 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).
