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- W4238304489 abstract "An endo-1, 3-β-D-xyIanase (1, 3-β-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 poly aery lamide 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 β-1, 3-xylan solutions and produced xylose and xylooligosaccharides from seaweed β-1, 3-xylan. The enzyme activity was greatly inhibited by Hg2+, SDS, ethylenediamine tetraacetic acid (EDTA), and N-bromosuccinimide (NBS)." @default.
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- W4238304489 date "1990-01-01" @default.
- W4238304489 modified "2023-10-06" @default.
- W4238304489 title "Purification and some properties of endo-1,3-.BETA.-D-xylanase from Pseudomonas sp. PT-5." @default.
- W4238304489 doi "https://doi.org/10.1271/bbb1961.54.921" @default.
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