A1 Journal article – refereed
Oxidation of Crocein Orange G by lignin peroxidase isoenzymes. Kinetics and effect of H2O2.




List of Authors: Ollikka P, Harjunpää T, Palmu K, Mäntsälä P, Suominen I
Publication year: 1998
Journal: Applied Biochemistry and Biotechnology
Volume number: 75
Issue number: 2-3

Abstract

The ligninolytic enzyme system of Phanerochaete chrysosporium is able to
decolorize several recalcitrant dyes. Three lignin peroxidase
isoenzymes, LiP 3.85, LiP 4.15, and LiP 4.65, were purified by
preparative isoelectric focusing from the carbon-limited culture medium
of P. chrysosporium. Based on amino terminal sequences, the purified
isoenzymes correspond to the isoenzymes H8, H6, and H2, respectively,
from the N-limited culture. The purified isoenzymes were used for
decolorization of an azo dye, Crocein Orange G (COG). According to the
kinetic data obtained, the oxidation of COG by lignin peroxidase
appeared to follow Michaelis-Menten kinetics. Kinetic parameters for
each isoenzyme were determined. The inactivating effect of ascending
H2O2 concentrations on COG oxidation is shown to be exponential within
the used concentration range. The best degree of decolorization of 100
microM COG was obtained when the H2O2 concentration was 150 microM. This
was also the lowest H2O2 concentration for maximal decolorization of
100 microM COG, regardless of the amount of lignin peroxidase used in
the reaction.


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