S. G. Dastager Æ Agasar Dayanand Æ Wen-Jun Li Æ
Chang-Jin Kim Æ Jae-Chan Lee Æ Dong-Jin Park Æ
Xin-Peng Tian Æ Q. S. Raziuddin

Received: 9 April 2007 / Accepted: 13 January 2008

Springer Science+Business Media, LLC 2008

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 45C. The enzyme preparation
exhibited activity over a broad range of pH (4–12) and
temperature (27–55C). Optimum activity was observed at
a pH of 9.0 and a temperature of 45C. 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).