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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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.
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| skos:exactMatch | |
| uniprot:name |
Curr. Genet.
|
| uniprot:author |
Hessing J.G.M.,
Maat J.,
Roza M.,
Verbakel J.M.A.,
van Gorcom R.F.M.,
van Rotterdam C.O.,
van den Hondel C.A.M.J.J.
|
| uniprot:date |
1994
|
| uniprot:pages |
228-232
|
| uniprot:title |
Isolation and characterization of a 1,4-beta-endoxylanase gene of A. awamori.
|
| uniprot:volume |
26
|
| dc-term:identifier |
doi:10.1007/BF00309552
|