The kinetics of the initial stages of autolysis of the yeast Saccharomyces cerevisiae was studied and the following kinetic parameters were determined: induction period, steady-state rate of the enzyme-induced effect, and steady-state concentration of intermediate products. It was shown that appropriate inducers were able to cause a more than fourfold increase in the rate of reactions catalyzed by proteinases and almost a tenfold increase in the concentration of intermediate peptides. The mean length of the peptide molecules formed in the process was determined and dependence of this value on the degree of hydrolysis was demonstrated.
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