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 seque
nce of the enzyme, the exlA gene of A. awamori, encoding 1,4-beta-xyla
nase 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 precurso
r, 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 biochemic
al and enzymological properties as the wild-type enzyme.