Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system.

Abstract:

:The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was recombined into a baculovirus and heterologously expressed in Sf9 cells. The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H2O2.

authors

Pease EA,Aust SD,Tien M

doi

10.1016/0006-291x(91)91903-p

subject

Has Abstract

pub_date

1991-09-16 00:00:00

pages

897-903

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)91903-P

journal_volume

179

pub_type

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