[Purification and characteristics of alkaline proteinase from alkalophylic Bacillus sp].
Alkaline protease was purified from Bacillus sp. isolated from soil. The pH optimum was 11.5 at 37 degrees C. Calcium divalent cation was effective to stabilize the enzyme especially at higher temperatures. The proteolytic activity was inhibited by active site inhibitors of PMSF (Phenylmethylsulfonyl fluoride), and ions of Mg, Mn, Pb, Li, Zn, Ag, Hg. The enzyme was stable in the presence of some detergents, such as Triton-X-100, Tween-80, SDS (sodium dodecyl sulfate) and EDTA (ethylendiaminetetraacetic acid), pH 11.5 and 37 degrees C for 30 min. The optimum pH was 11.5 at 37 degrees C and the optimum temperature was 62 degrees C at pH 11.5.
Muderrizade
A
A
University of Dicle, Faculty of Science and Art, Department of Biology, Diyarbahr, Turkey.
Ensari
N Y
NY
Aguloglu
S
S
Otludil
B
B
D001407:Bacillus / Q000737:chemistry* / Q000254:growth & development; D003902:Detergents / Q000737:chemistry; D004795:Enzyme Stability; D006361:Heating; D006863:Hydrogen-Ion Concentration; D007477:Ions; D008670:Metals / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry; D012988:Soil Microbiology
D003902:Detergents; D007477:Ions; D008670:Metals; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; C032923:microbial serine proteinases
Ochistka i kharakteristika shchelochnoĭ proteinazy alkalofil'nogo shtamma Bacillus sp..