Nishimura I, Okada K, Koyama Y.
Research and Development Division, Kikkoman Corporation, Chiba Pref., Japan.
Complementary DNA encoding pyranose oxidase (PROD) was cloned and sequenced for the first time from Coriolus versicolor. The nucleotide sequence revealed an open reading frame encoding a polypeptide composed of 623 amino acid residues. Compared with the experimentally determined N-terminal sequence of the PROD from C. versicolor. 38 amino acids from the N-terminus of the protein appeared to be eliminated during protein maturation. The cDNA was successfully expressed under the control of lacUV5 promoter in Escherichia coli at 25 degrees C, which will be beneficial in industrial production.
PMID: 9025322 [PubMed – indexed for MEDLINE]
Kajita S, Sugawara S, Miyazaki Y, Nakamura M, Katayama Y, Shishido K, Iimura Y.
Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo, 184-8588, Japan.
One of the major extracellular enzymes of the white-rot fungus Coriolus versicolor is laccase, which is involved in the degradation of lignin. We constructed a homologous system for the expression of a gene for laccase III (cvl3) in C. versicolor, using a chimeric laccase gene driven by the promoter of a gene for glyceraldehyde-3-phosphate dehydrogenase (gpd) from this fungus. We transformed C. versicolor successfully by introducing both a gene for hygromycin B phosphotransferase (hph) and the chimeric laccase gene. In three independent experiments, we recovered 47 hygromycin-resistant transformants at a transformation frequency of 13 transformants microg(-1) of plasmid DNA. We confirmed the introduction of the chimeric laccase gene into the mycelia of transformants by a polymerase chain reaction in nine randomly selected transformants. Overproduction of extracellular laccase by the transformants was revealed by a colorimetric assay for laccase activity. We examined the transformant (T2) that had the highest laccase activity and found that its activity was significantly higher than that of the wild type, particularly in the presence of copper (II). Our transformation system should contribute to the efficient production of the extracellular proteins of C. versicolor for the accelerated degradation of lignin and aromatic pollutants.
PMID: 15480638 [PubMed – indexed for MEDLINE]
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