Cloning of a cDNA encoding cellobiose dehydrogenase, a hemoflavoenzyme from Phanerochaete chrysosporium

Article Abstract:

Screening an expression library of the wood-degrading fungi Phanerochaete chrysosporium OGC101 with a cellobiose dehydrogenase (CDH) specific polyclonal antibody detected a 2.4-kb cDNA that codes for CDH. The cDNA encodes a 755-amino acid protein whose mass is 80,115 Da. The heme domain is at the N-terminus and the flavin domain at the C-terminus. The flavin domain is similar to other FAD-dependent enzymes and binds flavin adenine dinucleotide (FAD). The cellulose binding sequence of the CDH is different from those of the other cellulases.

Dehydrogenases, Oxidoreductases, Amino acid sequence, Amino acid sequencing, Wood-decaying fungi

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Gene cloning and characterization of a novel cellulose-binding beta-glucosidase from Phanerochaete chrysosporium

Article Abstract:

A copyDNA clone and genomic clone of cellulose-binding extracellular beta-glucosidase (CBGL) from the basidiomycete Phanerochaete chrysosporium were synthesized and characterized. Two domains were identified following an analysis of the copyDNA clone of the CBGL gene. Genomic sequencing of the clones also revealed that the CBGL gene is encoded by 30 exons with 29 introns ranging in size from 47 to 68 base pairs. Further characterization of the clones suggested the presence of two alleles of the same gene.

Genetic aspects, Fungi, Identification and classification, Genetic code

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Purification and characterization of a cellulose-binding beta-glucosidase from cellulose-degrading cultures of Phanerochaete chrysosporium

Article Abstract:

Purification of extracellular beta-glucosidase from cellulose-degrading Phanerochaete chrysosporium cultures revealed an enzyme that appears to have separate cellulose-binding and catalytic domains. Papain digestion of the 114,000-molecular-weight enzyme, which was capable of binding microcrystalline cellulose, yielded three bands on SDS- PAGE that appear to be non-cellulose binding and cellulose-binding forms that may correspond to those produced by extracellular proteolysis.

Bacteria, Gel electrophoresis, Liquid chromatography, Microbiological research

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