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Isolation and characterization of a 1,4-β-endoxylanase gene of A. awamori

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Abstract

An enzyme with a particular 1,4-β-xylanase activity was identified and purified from wheat-bran culture medium of an Aspergillus awamori strain. With oligonucleotides based on the N-terminal amino-acid sequence of the enzyme, the exlA gene of A. awamori, encoding 1,4-β-xylanase A, has been cloned. Based on the deduced amino-acid sequence, 1,4-β-xylanase A is produced as a 211 amino-acid-residue-long precursor, which is converted post-translationally into a 184-aa-residue-long mature protein. Transformation of the original A. awamori strain with multiple copies of the exlA gene resulted in a 40-fold overproduction of 1,4-β-xylanase A. The overproduced enzyme has the same biochemical and enzymological properties as the wild-type enzyme.

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Hessing, J.G.M., van Rotterdam, C., Verbakel, J.M.A. et al. Isolation and characterization of a 1,4-β-endoxylanase gene of A. awamori . Curr Genet 26, 228–232 (1994). https://doi.org/10.1007/BF00309552

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  • DOI: https://doi.org/10.1007/BF00309552

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