Heterologous Expression of Phanerochaete chrysoporium Glyoxal Oxidase and its Application for the Coupled Reaction with Manganese Peroxidase to Decolorize Malachite Green.
10.5941/MYCO.2012.40.4.258
- Author:
Yu Lim SON
1
;
Hyoun Young KIM
;
Saravanakumar THIYAGARAJAN
;
Jing Jing XU
;
Seung Moon PARK
Author Information
1. Division of Biotechnology, College of Environmental and Bioresource Sciences, Chonbuk National University, Iksan 570-752, Korea. smpark@chonbuk.ac.kr
- Publication Type:Brief Communication
- Keywords:
Dye decolorization;
Glyoxal oxidase;
Manganese peroxidase;
Phanerochaete chrysosporium;
Pichia pastoris
- MeSH:
Alcohol Oxidoreductases;
DNA, Complementary;
Glyoxal;
Manganese;
Organometallic Compounds;
Oxidoreductases;
Peroxidase;
Peroxidases;
Phanerochaete;
Pichia;
Rosaniline Dyes
- From:Mycobiology
2012;40(4):258-262
- CountryRepublic of Korea
- Language:English
-
Abstract:
cDNA of the glx1 gene encoding glyoxal oxidase (GLX) from Phanerochaete chrysosporium was isolated and expressed in Pichia pastoris. The recombinant GLX (rGLX) produces H2O2 over 7.0 nmol/min/mL using methyl glyoxal as a substrate. Use of rGLX as a generator of H2O2 improved the coupled reaction with recombinant manganese peroxidase resulting in decolorization of malachite green up to 150 microM within 90 min.
