ABSTRACT
Regulation of protease and pigment production in Hypomyces rosellus by the medium components was easier than that of antibiotic production. Medium was developed. The activity of exoproteases and pigment with the use of this medium increased up to 385-800 PU/ml and 0.68-0.83 arbitrary units, respectively. The level of the antibiotic biosynthesis was insignificant.
Subject(s)
Anti-Bacterial Agents/biosynthesis , Culture Media/metabolism , Hypocreales/metabolism , Peptide Hydrolases/biosynthesis , Pigments, Biological/biosynthesis , Dose-Response Relationship, Drug , Mathematics , Methods , Research DesignABSTRACT
A protease complex with high caseinolytic activity capable of hydrolysing various protein substrates was isolated from the culture fluid of Hypomyces rosellus. The preparation is stable at pH 6.0-11.0. The temperature optimum of its activity and stability is 50 degrees C. The protease complex preserves its initial activity at 4 degrees C for a month.
Subject(s)
Hypocreales/enzymology , Peptide Hydrolases/metabolism , Albumins/metabolism , Animals , Caseins/metabolism , Exopeptidases , Fibrinolysis , Hemoglobins/metabolism , Hydrogen-Ion Concentration , Substrate Specificity , TemperatureABSTRACT
Changes are observed of 1-anylinonaphtalene-8-sulphonate probe fluorescence intensity, connected with beta-amylase in the presence of Ca(NO3)2, Mg(NO3)2, KNO3, NH4NO3 and (NH4)2SO4 at a concentration range within 10(-4)--1 M. Considerable decrease of the fluorescence intensity was observed under the addition of all the salts mentioned at concentration of 10(-3)--10(-4) M. A quantum yield increase of probe fluorescence was noted for Mg(NO3)2 (10(-4) M). High concentrations of Ca(NO3)2 and Mg(NO3)2 (0.25--1 M) also resulted in a sharp increase of the fluorescence intensity. Changes of beta-amylase activity took place simultaneously. The changes of the enzyme activity are suggested to be due to changes in the conformation of the enzyme protein under the effect of salts.
