Homologous expression of recombinant lignin peroxidase in Phanerochaete chrysosporium

Article Abstract:

The homologous expression of the gene encoding lignin peroxidase isozyme H8, lip2, has been investigated in primary metabolic cultures of Phanerochaete chrysosporium. The expression of lip2 was driven using the glyceraldehyde-3-phosphate dehydrogenase promoter while the expression vector pUGL was employed to transform a Phanerochaete chrysosporium Ura11 auxotroph to prototrophy. Results show that both the steady-state and transient-state kinetic characteristics of the oxidation of veratryl alcohol between wild-type LiPh8 and rLiPh8 were similar, as were the molecular mass, optical absorption spectrum and pI.

Plant genetics, Gene expression, Bacteria, Phytopathogenic, Phytopathogenic bacteria, Recombinant proteins, Peroxidase, Lignin

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Purification and characterization of a 1,4-Benzoquinone reductase from the basidiomycete Phanerochaete chrysosporium

Article Abstract:

A 1,4-benzoquinone reductase was purified from Phanerochaetechrysosporium and characterized, revealing a Km for 2- methoxy-1,4-benzoquinone of2.4 micromolar and a kcat of 440,000 per second. The intracellular, soluble reductasewas expressed in nitrogen- sufficient to nitrogen-limiting cultures containing between 12and 1.2 mM ammonium tartrate. Catalysis of two-electron reduction of quinones by theenzyme is accomplished using either NADH or NADPH electrondonors.

Analysis, Usage, Enzymes, Bacteria, Gel electrophoresis, Catalysis

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