Multiple lignin peroxidases of Phanerochaete chrysosporium INA-12.

Abstract:

:Nine proteins with lignin peroxidase activity were separated from cultures of Phanerochaete chrysosporium INA-12 in glycerol as carbon source and non-nitrogen limited. Four lignin peroxidase isozymes (4, 5, 8, 9) were purified and characterized. Although differences in kinetic parameters could be shown, antibody reaction showed homology between isozymes. However, thermal stability studied, peptide mapping results, and N-terminal sequence analyses established a higher degree of homology between isozymes 4/5 and 8/9 types. Protein characterization and kinetic data indicate that lignin peroxidase isozymes 4, 5, 8, and 9 differ from described isozymes in strain BKM. The higher specific activity of lignin peroxidase isozymes in cultures with glycerol than in nitrogen-starved cultures accounts for the higher lignin peroxidase activity obtained in these conditions.

journal_name

Enzyme Microb Technol

authors

Odier E,Delattre M

doi

10.1016/0141-0229(90)90056-v

keywords:

subject

Has Abstract

pub_date

1990-06-01 00:00:00

pages

447-52

issue

6

eissn

0141-0229

issn

1879-0909

pii

0141-0229(90)90056-V

journal_volume

12

pub_type

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