Purification and characterization of beta-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214.
beta-1,3-Xylanase was purified to gel electrophoretic homogeneity and 83-fold from a cell-free culture fluid of Vibrio sp. XY-214 by ammonium sulfate precipitation and successive chromatographies. The enzyme had a pl of 3.6 and a molecular mass of 52 kDa. The enzyme had the highest level of activity at pH 7.0 and 37 degrees C. The enzyme activity was completely inhibited by Cu2+, Hg2+, and N-bromosuccinimide. The enzyme hydrolyzed beta-1,3-xylan to produce mainly xylotriose and xylobiose but did not act on xylobiose, p-nitrophenyl-beta-D-xyloside, beta-1,4-xylan, beta-1,3-glucan, or carboxymethyl cellulose.
Araki
T
T
Faculty of Bioresources, Mie University, Japan. araki@bio.mie-u.ac.jp
Tani
S
S
Maeda
K
K
Hashikawa
S
S
Nakagawa
H
H
Morishita
T
T
D000595:Amino Acid Sequence; D001974:Bromosuccinimide / Q000494:pharmacology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003300:Copper / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008628:Mercury / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D012623:Seawater / Q000382:microbiology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014733:Vibrio / Q000201:enzymology*; D043325:Xylan Endo-1,3-beta-Xylosidase; D014995:Xylosidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D010446:Peptide Fragments; D003300:Copper; D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase; D008628:Mercury; D001974:Bromosuccinimide