Isolation and characterization of a 1,4-beta-endoxylanase gene of A. 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 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.
TNO Nutrition and Food Research, Rijswijk, The Netherlands.
J G
JG
Hessing
C
C
van Rotterdam
J M
JM
Verbakel
M
M
Roza
J
J
Maat
R F
RF
van Gorcom
C A
CA
van den Hondel
D000595:Amino Acid Sequence; D001230:Aspergillus / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D004271:DNA, Fungal; D043364:Endo-1,4-beta Xylanases; D005800:Genes, Fungal; D008969:Molecular Sequence Data; D014158:Transcription, Genetic; D014995:Xylosidases / Q000235:genetics*
D004271:DNA, Fungal; D014995:Xylosidases; D043364:Endo-1,4-beta Xylanases