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Efficiency of bovine liver catalase as a catalyst to cleave H 2 O 2 added continually to buffer solutions
Author(s) -
Ibrahim M.,
Schlegel H. G.
Publication year - 1980
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.260220909
Subject(s) - catalase , steady state (chemistry) , chemistry , enzyme , cleave , hydrogen peroxide , kinetics , biochemistry , chromatography , organic chemistry , physics , quantum mechanics
Empirical estimations of H 2 O 2 concentration in a system containing bovine liver catalase and continually supplied with H 2 O 2 were done to evaluate the efficiency of the enzyme to cleave H 2 O 2 . It was found that the continuous addition of H 2 O 2 leads to the formation of steady‐state concentrations of H 2 O 2 in the medium. At a constant catalase concentration both the level and the duration of the steady state are dependent on the flow rate of H 2 O 2 . The increase of the catalase concentration in the medium does not change the steady‐state level, it merely leads to the maintenance of the steady state for longer durations. At higher flow rates of H 2 O 2 , no steady state could be maintained, even when catalase was present in high excess. The incomplete cleavage of H 2 O 2 by catalase under these conditions is due to the low affinity of catalase toward H 2 O 2 (high K m value, apparent K m = 0.1 M H 2 O 2 ) and to the rapid inactivation of the enzyme during the continuous addition of H 2 O 2 .