Purification and properties of manganese peroxidase from Trametes versicolor

Two manganese peroxidase (MnP) active fractions D1 and D2 were got from the extracellular culture of Trametes versicolor by using ammonium sulfate precipitation, DEAE-cellulose DE52 chromatography. MnP1 was purified to electrophoretic homogeneity from the D2 by Phenyl Sepharose 6 Fast Flow chromatography and MnP2 was purified to electrophoretic homogeneity from the D1 by Sephacryl S-200HR chromatography and Phenyl Sepharose 6 Fast Flow chromatography. The specific activities of two MnP isozymes are 579.1U/mg and 425.0U/mg; purification folds are 17.51 and 12.85 and the yields are 6.17% and 2.47%, respectively. MnP1 and MnP2 have approximate molecular masses of 46.3kD and 43.0kD respectively, as determined by SDS-PAGE. The isoenzymes differed in optimum temperature (60degreesC and 65degreesC) and optimum pH(5.8 and 6.2) for oxidation of DMP (2,6-dimethoxyphenol). MnP1 and MnP2 are stable below 45degreesC and ranging from pH4.0 to pH7.0. DMP is the best substrate, the Km values of MnP1 and MnP2 for DMP are 13.43micromol/L and 12.45micromol/L respectively. Catalysis doesn't occur in the complete absence of Mn. EDTA inhibites the activities of MnP1 and MnP2 at the higher concentration and DTT inhibites the enzyme activities completely.

Medienart:

Artikel

Erscheinungsjahr:

2005

Erschienen:

2005

Enthalten in:

Zur Gesamtaufnahme - volume:45

Enthalten in:

Wei sheng wu xue bao = Acta microbiologica Sinica - 45(2005), 5 vom: 01. Okt., Seite 711-5

Sprache:

Chinesisch

Beteiligte Personen:

Zhang, Lian-hui [VerfasserIn]
Yang, Xiu-qing [VerfasserIn]
Ge, Ke-shan [VerfasserIn]
Qian, Shi-jun [VerfasserIn]

Themen:

EC 1.11.1.-
EC 1.11.1.13
English Abstract
Journal Article
Manganese peroxidase
Peroxidases
Research Support, Non-U.S. Gov't

Anmerkungen:

Date Completed 23.04.2009

Date Revised 13.12.2005

published: Print

Citation Status MEDLINE

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM15944912X