Open AccessLignin peroxidase from Phanerochaete‐chrysosporium
Author(s) -
GLUMOFF Tuomo,
HARVEY Patricia J.,
MOLINARI Sergio,
GOBLE Martin,
FRANK Gerhard,
PALMER John M.,
SMIT Jan Derk G.,
LEISOLA Matti S. A.
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb15333.x
Subject(s) - phanerochaete , chrysosporium , isozyme , peroxidase , lignin , lignin peroxidase , biochemistry , chemistry , isoelectric point , substrate (aquarium) , isoelectric focusing , enzyme , organic chemistry , biology , ecology
Five isozymes of lignin peroxidase from Phanerochaete chrysosporium were purified and their physical, molecular and kinetic properties determined. The isozymes differ from each other in terms of their isoelectric point, molecular mass, sugar content, spectral characteristics, substrate specificity and stability. The N‐terminal sequence of amino acids was different for each isozyme suggesting they are different gene products. The isozyme with the highest carbohydrate level was most sensitive to changes in environmental factors. The kinetic behaviour of the isozymes varied clearly when tert ‐butyl hydroperoxide instead of hydrogen peroxide was used as the oxidant. Two out of five isozymes had very similar substrate specificity. The results are discussed in relation to the role which lignin peroxidase isozymes may play in lignin biodegradation.