Proteolytic activity from an alkali-thermotolerant Streptomyces gulbargensis sp. nov.
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).
Dastager
S G
SG
Korea Research Institute of Bioscience and Biotechnology, 52 Oeundong, Yusong, Daejeon 305-333, Republic of Korea. syed_micro@rediffmail.com
Dayanand
Agasar
A
Li
Wen-Jun
WJ
Kim
Chang-Jin
CJ
Lee
Jae-Chan
JC
Park
Dong-Jin
DJ
Tian
Xin-Peng
XP
Raziuddin
Q S
QS
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
D001426:Bacterial Proteins; D020543:Proteome; D010447:Peptide Hydrolases