| Literature DB >> 18810538 |
S G Dastager1, Agasar Dayanand, Wen-Jun Li, Chang-Jin Kim, Jae-Chan Lee, Dong-Jin Park, Xin-Peng Tian, Q S Raziuddin.
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).Entities:
Mesh:
Substances:
Year: 2008 PMID: 18810538 DOI: 10.1007/s00284-008-9257-y
Source DB: PubMed Journal: Curr Microbiol ISSN: 0343-8651 Impact factor: 2.188