Ca. Reddy, AN OVERVIEW OF THE RECENT ADVANCES ON THE PHYSIOLOGY AND MOLECULAR-BIOLOGY OF LIGNIN PEROXIDASES OF PHANEROCHAETE-CHRYSOSPORIUM, Journal of biotechnology, 30(1), 1993, pp. 91-107
The lignin-degrading white-rot fungus Phanerochaete chrysosporium prod
uces two families of extracellular peroxidases designated lignin perox
idases (LIPs) and manganese-dependent peroxidases (MNPs) which are com
ponents of the lignin degradation system of this organism. The number
and types of LIP and MNP isozymes produced vary dramatically in respon
se to changes in culture conditions. Protease-mediated degradation of
LIPs was shown to be the major cause for the decay of LIP activity in
idiophasic cultures of P. chrysosporium. Use of biochemical mutants ha
s not only yielded information on the relative importance of LIPs and
MNPs in lignin degradation but has given us insights into the regulati
on of production of LIPs and MNPs. The genes encoding the major LIPs h
ave been cloned and sequenced and were shown to have a high degree of
homology to each other. Karyotyping studies indicated that heterokaryo
tic strains contain ten chromosomes and that the LIP genes are distrib
uted on at least two chromosomes.