Purification of major lignin peroxidase isoenzymes from Phanerochaete chrysosporium by chromatofocusing.

Abstract:

:The basidiomycete Phanerochaete chrysosporium produces several isoforms of lignin peroxidase, which catalyzes the oxidative depolymerization of lignin To date, ion-exchange chromatography and preparative isoelectric focusing (IEF) have been commonly used for isolation of lignin peroxidase isoenzymes. In this work we have purified major lignin peroxidases to high purity by a one-step chromatographic method, chromatofocusing. The purified isoenzymes were identified by analytical IEF using isoenzymes purified by preparative IEF as standards. The specific activities and spectral properties of the isoenzymes were comparable with the previously published data. The predominant isoenzyme under the growth conditions used was LiP 4.65. Almost 50% of the lignin peroxidase activity applied into the column was recovered in the LiP 4.65 fraction. The total recovery of the lignin peroxidase activity was over 80%.

journal_name

Protein Expr Purif

authors

Ollikka P,Leppänen VM,Anttila T,Suominen I

doi

10.1006/prep.1995.1044

subject

Has Abstract

pub_date

1995-06-01 00:00:00

pages

337-42

issue

3

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(85)71044-3

journal_volume

6

pub_type

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