Isolation and characterization of a 1,4-beta-endoxylanase gene of Aspergillus awamori

article






Hessing, J.G.M.

Rotterdam, C. van

Verbakel, J.M.A.

Roza, M.

Maat, J.

Gorcom, R.F.M. van

Hondel, C.A.M.J.J. van den
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 β-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.
Molecular Sequence Numbers: GENBANK: X78115;
Chemicals/CAS: DNA, Fungal; endo-1,4-beta-xylanase, EC 3.2.1.8; Xylosidases, EC 3.2.1.-
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Amino Acid SequenceAspergillusBase SequenceCloning, MolecularDNA, FungalGenes, FungalMolecular Sequence DataTranscription, GeneticXylosidasesAspergillus awamoriTriticum aestivumMulticopy transformantOverexpressionEnzyme (1,4-β-D-xylanohydrolase E.C.3.2.1.8.) purification
TNO Identifier
51883
Repository link
https://resolver.tno.nl/uuid:03ba6fc3-20c3-48fa-97ad-2d690d482742
ISSN
01728083
Source
Current Genetics, 26(3), pp. 228-232.
Pages
228-232
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