Purification and Characterization of Alkaline Proteinase from AlkalophilicBacillussp
Alkaline proteinase was purified from Bacillussp. isolated from soil. The pH optimum was 11.5 at 37°C. Calcium divalent cation was effective in stabilizing the enzyme, especially at higher temperatures. The proteolytic activity was inhibited by the specific serine proteinase inhibitor PMSF (phenylme...
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| Veröffentlicht in: | Applied biochemistry and microbiology 2001-11, Vol.37 (6), p.574 |
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| creator | Muderriszade, A Ensari, N Y Aguloglu, S Otludil, B |
| description | Alkaline proteinase was purified from Bacillussp. isolated from soil. The pH optimum was 11.5 at 37°C. Calcium divalent cation was effective in stabilizing the enzyme, especially at higher temperatures. The proteolytic activity was inhibited by the specific serine proteinase inhibitor PMSF (phenylmethylsulfonyl fluoride), and ions of Mg, Mn, Pb, Li, Zn, Ag, and Hg. The enzyme was stable in the presence of detergents, such as Triton-X100, Tween-80, SDS (sodium dodecyl sulfate), and EDTA (ethylenediaminetetraacetic acid), at pH 11.5 and 37°C for 30 min. The optimum pH was 11.5 at 37°C, and the optimum temperature was 62°C at pH 11.5.[PUBLICATION ABSTRACT] |
| doi_str_mv | 10.1023/A:1012346916124 |
| format | Article |
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| ispartof | Applied biochemistry and microbiology, 2001-11, Vol.37 (6), p.574 |
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| language | eng |
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| source | Springer Nature - Complete Springer Journals |
| subjects | Detergents Enzymes High temperature Proteinase inhibitors |
| title | Purification and Characterization of Alkaline Proteinase from AlkalophilicBacillussp |
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