ABSTRACT
Proteolytic enzymes of microorganisms have been studied for the possibility to create their polyenzymic composition in order to rise a degree of protein hydrolysis and to lower the process duration. Optimal action conditions are selected and a hydrolysis of a number of globular and fibrillar proteins is conducted by a polyenzymic system of Streptomyces griseus and Acremonium chrysogenum proteases.
Subject(s)
Acremonium/enzymology , Multienzyme Complexes/isolation & purification , Peptide Hydrolases/isolation & purification , Streptomyces griseus/enzymology , HydrolysisABSTRACT
The immobilized form of proteases complex of Str. griseus actinomycete is obtained by means of glutaric aldehyde with aminoethyl cellulose. Hydrolysis of synthetic substrates showed that the system of peptide hydrolases is bound, but the ratio of activities as compared to the initial proteolytic complex changes, pH-optimum of the total proteolytic activity, pH- and temperature optima of stability are not changed with immobilization. On the whole no essential stabilization of the complex was observed. After five repeated cycles of the immobilized form utilization of the activity loss accounts for 40-60%.