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Isolation and characterization of a 1,4-beta-endoxylanase gene of A. [Aspergillus]. awamori

An enzyme with a particular 1,4-beta-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-beta-xylanase A, has been clo...

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Bibliographic Details
Published in:Current genetics 1994-09, Vol.26 (3), p.228-232
Main Authors: Hessing, J.G.M. (TNO Nutrition and Food Research, Rijswijk (Netherlands)), Rotterdam, C. van, Verbakel, J.M.A, Roza, M, Maat, J, Gorcom, R.F.M. van, Hondel, C.A.M.J.J. van den
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Language:English
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Summary:An enzyme with a particular 1,4-beta-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-beta-xylanase A, has been cloned. Based on the deduced amino-acid sequence, 1,4-beta-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-beta-xylanase A. The overproduced enzyme has the same biochemical and enzymological properties as the wild-type enzyme.
ISSN:0172-8083
1432-0983
DOI:10.1007/BF00309552