ABSTRACT
Properties of a protease preparation obtained by ethanol precipitation of a concentrate of the culture fluid of Bacillus subtilis R (1 : 4 v/v; 4 degrees C) grown under the conditions of deep cultivation were studied. The use of specific inhibitors, EDTA and phenylmethylsulfonyl fluoride, made it possible to show that the enzyme belongs to the group of serine proteases. The preparation exhibited high stability in alkaline medium and thermostability; it hydrolyzed protein substrates and retained catalytic properties in the presence of a multicomponent detergent system. The preparation is recommended for use in those branches of industry where proteolysis is required and in the production of detergents (as a biological additive).
Subject(s)
Bacillus subtilis/enzymology , Serine Endopeptidases/isolation & purification , Serine Endopeptidases/metabolism , Bacterial Proteins/isolation & purification , Bacterial Proteins/metabolism , Catalysis , Enzyme Stability , Hydrolysis , Substrate SpecificityABSTRACT
The use of enzymic preparations of the cellulolytic and macerating effect was studied as applied to the isolation of diosgenine from rhizomes of Dioscorea caucasica Lypsky. The enzymic treatment of the steroid containing raw material prior to acid hydrolysis increased the yield of diosgenine by 30-48%. It is suggested that additional extraction of diosgenine takes place due to: 1) enzymic hydrolysis of structural polysaccharide components of the plant tissue and intercellular binding materials and 2) disintegration of glycoside bonds of saponins.
