An extracellular endo-1,4-beta-xylanase from Aspergillus japonicus: Purification, properties, and characterization of the encoding gene.
An extracellular endo-1,4-beta-xylanase with specific activity of 566 U/mg was purified from the culture filtrate of a filamentous fungus, Aspergillus japonicus strain MU-2, grown on oat spelt xylan. The purified enzyme showed a single band on SDS-PAGE with an apparent M(r) of 25.1 kDa. Xylanase activity was optimal at pH 5.0 and 60 degrees C. The xylanase gene (xynA) encoded a 42 residue prepropeptide and a 191 residue mature protein. The XynA protein showed the highest sequence identity of 69% to Aspergillus niger XynB (DQ174549), which belongs to the glycoside hydrolase family 11.
Wakiyama
Motoki
M
Department of Biochemistry and Applied Biosciences, Faculty of Agriculture, University of Miyazaki, 1-1 Gakuen Kibanadai Nishi, Miyazaki 889-2192, Japan.
Yoshihara
Koji
K
Hayashi
Sachio
S
Ohta
Kazuyoshi
K
D000595:Amino Acid Sequence; D001230:Aspergillus / Q000201:enzymology*; D001483:Base Sequence; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D004789:Enzyme Activation; D004795:Enzyme Stability; D008969:Molecular Sequence Data
D043364:Endo-1,4-beta Xylanases