Purification and some properties of endo-1,3-beta-D-xylanase from Pseudomonas sp. PT-5.
An endo-1,3-beta-D-xylanase (1,3-beta-D-xylan xylanohydrolase, EC 3.2.1.32) was purified from the culture fluid of Pseudomonas sp. PT-5 by ammonium sulfate fractionation, DEAE-Sepharose CL-6B, Toyopearl HW-50S, and Butyl-Toyopearl 650 M column chromatography. The purified enzyme gave a single band on polyacrylamide gel disc electrophoresis and its molecular weight was 35,000 by SDS-polyacrylamide gel electrophoresis. The enzyme was stable from pH 5.5 to 8.0 and had its maximum activity at pH 7.5. The enzyme rapidly reduced the viscosity of glycol beta-1,3-xylan solutions and produced xylose and xylooligosaccharides from seaweed beta-1,3-xylan. The enzyme activity was greatly inhibited by Hg2+, SDS, ethylenediamine tetraacetic acid (EDTA), and N-bromosuccinimide (NBS).
Department of Applied Microbial Technology, Kumamoto Institute of Technology, Japan.
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Yamaura
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Matsumoto
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Funatsu
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Mukai
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002854:Chromatography, Paper; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D043325:Xylan Endo-1,3-beta-Xylosidase; D014990:Xylans / Q000378:metabolism
D000596:Amino Acids; D014990:Xylans; C065917:1,3-xylan; D006026:Glycoside Hydrolases; D043325:Xylan Endo-1,3-beta-Xylosidase