[Purification and physico-chemical properties of proteolytic complex Bacillus sp].
The schemes of isolation and purification of proteolytic complex of Bacillus sp. have been developed, which include fractionation by ammonium sulphate and separation on TSK-gels: ion-exchange chromatography on Toyopearl DEAE-650 (M) and gel-filtration on Toyopearl HW-50. It has been established that the proteolytic complex Bacillus sp. is presented by neutral and alkali proteases (pH optimum at 6.0-8.0 and 10.0), which hydrolyse a number of protein substrates: casein, gelatin, hemoglobin, fibrin, and elastin. Two proteolytic complexes with dominating fibrinolytic and elastase activity and molecular weight 28.7 and 22.7 kDd were isolated as a result of purification. It was found out that the obtained enzymatic preparations belong to the group of serine protease which need metal ions for development of their activity.
Levishko
A S
AS
Matseliukh
O V
OV
Varbanets'
L D
LD
D000838:Anions / Q000737:chemistry; D001407:Bacillus / Q000201:enzymology*; D002412:Cations / Q000737:chemistry; D002627:Chemistry, Physical; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000737:chemistry; D057057:Serine Proteases / Q000737:chemistry* / Q000302:isolation & purification*; D013379:Substrate Specificity
D000838:Anions; D002412:Cations; D008670:Metals; D057057:Serine Proteases