Abstract
The complete gene xylA that encodes endo-1,4-β-xylanase secreted byPenicillium canescens was cloned and sequenced. The coding region of the gene is separated by eight introns. The protein comprises 302 amino acids of the mature protein and 25 amino acids of the signal peptide. The xylanase of P. canescens belongs to the glycosyl hydrolase family 10. Nucleotide sequences for binding catabolite repression protein CREA and transactivator protein were detected in the promoter region. A set of multicopy strains displaying a seven to eightfold increase in xylanase yield was obtained. The fraction of xylanase in most productive strains amounted to 30–50% of the total secreted protein.
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Serebryanyi, V.A., Vavilova, E.A., Chulkin, A.M. et al. Cloning of Penicillium canescens Endo-1,4-β-xylanase Gene and Construction of Multicopy Strains. Applied Biochemistry and Microbiology 38, 420–426 (2002). https://doi.org/10.1023/A:1019908232700
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DOI: https://doi.org/10.1023/A:1019908232700