CLONING AND EXPRESSION OF PYRANOSE OXIDASE CDNA FROM CORIOLUS-VERSICOLOR IN ESCHERICHIA-COLI

Complementary DNA encoding pyranose oxidase (PROD) was cloned and sequ enced for the first time from Coriolus veisicolor. The nucleotide sequ ence 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 fro m the N-terminus of the protein appeared to be eliminated during prote in maturation. The cDNA was successfully expressed under the control o f lacUV5 promoter in Escherichia coli at 25 degrees C, which will be b eneficial in industrial production. Copyright (C) 1996 Elsevier Scienc e B.V.