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.
Subject(s)
Alcohol Oxidoreductases , DNA, Complementary , Glyoxal , Manganese , Organometallic Compounds , Oxidoreductases , Peroxidase , Peroxidases , Phanerochaete , Pichia , Rosaniline DyesABSTRACT
The cDNA of endo-1,4-beta-xylanaseA, isolated from Phaenerocheate chrysosporium was expressed in Pichia pastoris. Using either the intrinsic leader peptide of XynA or the alpha-factor signal peptide of Saccharomyces cerevisiae, xylanaseA is efficiently secreted into the medium at maximum concentrations of 1,946 U/L and 2,496 U/L, respectively.