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Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: I. First‐order behaviour
Author(s) -
Lencki Robert W.,
Arul Joseph,
Neufeld Ronald J.
Publication year - 1992
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.260401117
Subject(s) - kinetics , chemistry , denaturation (fissile materials) , dissociation (chemistry) , first order , reversible reaction , decomposition , protein subunit , biophysics , biochemistry , organic chemistry , catalysis , biology , physics , mathematics , quantum mechanics , gene , nuclear chemistry
Enzyme inactivation kinetics typically follows what would appear to be simple first‐order behavior. However, the inactivation process is known to involve a number of reversible (decomposition, denaturation) as well as irreversible (decomposition, aggregation, and coagulation) reactions. These reactions can combine to form a wide variety of reaction pathways which can potentially demonstrate complex inactivation kinetics. However, it was shown that with appropriate assumptions with regard to the relative magnitudes of the various reaction rates, many complex inactivation pathways can demonstrate apparent first‐order behavior. Thus, with this analysis, a more accurate interpretation of the slope of an activity versus time semi‐log plot can be obtained. © 1992 John Wiley & Sons, Inc.