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Kinetics of enzymatic lysis and disruption of yeast cells: II. A simple model of lysis kinetics
Author(s) -
Hunter J. B.,
Asenjo J. A.
Publication year - 1987
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260300404
Subject(s) - lysis , yeast , kinetics , biochemistry , chemistry , enzyme , hydrolysis , proteolysis , lytic cycle , enzyme kinetics , chromatography , biology , active site , physics , virus , quantum mechanics , virology
A simple two‐step model is proposed to describe the kinetics of the two lytic systems examined in the preceding article. The model predicts concentrations of yeast solids, soluble proteins, peptides, and carbohyrates. In the first reaction step, yeast cell mass is solubilized; in the second, the released protein can be hydrolyzed to peptides. Kinetics for both yeast lysis and the subsequent protein breakdown are based on Michaelis–Menten expressions. Terms have been included for competitive inhibition of yeast lysis by substances in the Cytophaga enzyme preparation, and for incomplete hydrolysis of cells by the Oerskovia enzyme system. Parameters have been independently determined for all reactions except Oerskovia proteolysis, where they were fit by a leastsquares method to data from model test runs. The model has been verified for yeast concentrations between 0.7 and 70 g/L yeast (dry basis) and 4–40% crude enzyme solution.