Purification and characterization of alkaline proteinase from alkalophilic Bacillus sp.
[ X ]
Tarih
2001
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Maik Nauka/Interperiodica/Springer
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
Alkaline proteinase was purified from Bacillus sp. isolated from soil. The pH optimum was 11.5 at 37 degreesC. 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 degreesC for 30 min. The optimum pH was 11.5 at 37 degreesC, and the optimum temperature was 62 degreesC at pH 11.5.
Açıklama
Anahtar Kelimeler
[No Keyword]
Kaynak
Applied Biochemistry and Microbiology
WoS Q Değeri
Q4
Scopus Q Değeri
Q4
Cilt
37
Sayı
6
