| Autor: |
Hessing JG; TNO Nutrition and Food Research, Rijswijk, The Netherlands., van Rotterdam C, Verbakel JM, Roza M, Maat J, van Gorcom RF, van den Hondel CA |
| Jazyk: |
angličtina |
| Zdroj: |
Current genetics [Curr Genet] 1994 Sep; Vol. 26 (3), pp. 228-32. |
| DOI: |
10.1007/BF00309552 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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