title: Proteolytic activity from an alkali-thermotolerant Streptomyces gulbargensis sp. nov.
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).
authors.affiliation: Korea Research Institute of Bioscience and Biotechnology, 52 Oeundong, Yusong, Daejeon 305-333, Republic of Korea. syed_micro@rediffmail.com
authors.forename: S G
authors.initials: SG
authors.lastname: Dastager
authors.forename: Agasar
authors.initials: A
authors.lastname: Dayanand
authors.forename: Wen-Jun
authors.initials: WJ
authors.lastname: Li
authors.forename: Chang-Jin
authors.initials: CJ
authors.lastname: Kim
authors.forename: Jae-Chan
authors.initials: JC
authors.lastname: Lee
authors.forename: Dong-Jin
authors.initials: DJ
authors.lastname: Park
authors.forename: Xin-Peng
authors.initials: XP
authors.lastname: Tian
authors.forename: Q S
authors.initials: QS
authors.lastname: Raziuddin
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D020543:Proteome / Q000032:analysis; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D020543:Proteome; D010447:Peptide Hydrolases