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- W2027589222 abstract "1. An α-l-arabinofuranoside was purified from the culture fluid of corticium rolfsii IFO 4878. The process was as follows: salting out by (NH4)2SO4, gel filtration on Sephadex G-100 and G-200, heat treatment, chromatography on DEAE-Sephadex A-50, SE-Sephadex C-50 and QAE-Sephadex A-50. 2. The highly purified enzyme was demonstrated to be homogeneous by ultra-centrifugal analysis and disc electrophoresis, respectively. 3. The activity of the purified enzyme towards phenyl α-l-arabinofuranoside and beet arabinan was found to be maximum at pH 2.5. The enzyme was also found to be stable over a wide pH range, pH 1.5 to 10, and to be unusually acid stable; even after storage at pH 2.0 and 5° for 72 h, 83% of enzymic activity remained. 4. Km values were determined to be 2.86 · 10−3 M for phenyl α-l-arabinofuranoside, 8.47 g/l for arabinan and 28.6 g/l for 1.5-arabinan. The values of vmax were also determined to be 124.0 μmoles for phenyl α-l-arabinofuranoside, 53.0 μmoles for arabinan and 16.7 μmoles for 1,5-arabinan per min per mg of protein, respectively." @default.
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- W2027589222 date "1971-11-01" @default.
- W2027589222 modified "2023-09-23" @default.
- W2027589222 title "Properties of purified α-l-arabinofuranosidase from Corticium rolfsh" @default.
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- W2027589222 doi "https://doi.org/10.1016/0005-2744(71)90193-8" @default.
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