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Characterization Of \Beta-Xylosidase And\Alpha-L-Arabinofuranosidase Activities Fromthermomonospora Fusca Bd25, Müni̇r Tuncer
Characterization Of \Beta-Xylosidase And\Alpha-L-Arabinofuranosidase Activities Fromthermomonospora Fusca Bd25, Müni̇r Tuncer
Turkish Journal of Biology
Thermomonospora fuscaBD25 produces relatively high levels of activity of \beta-xylosidase and \alpha-L-arabinofuranosidase. The aim of the work described in this study was to characterize some properties of \beta-xylosidase and \alpha-L-arabinofuranosidase produced by T. fusca BD25 when growing on oat spelt xylan as the main carbon and energy sources. The substrates p-NPX and p-NPA reacted with \beta-xylosidase and \alpha-L-arabinofuranosidase with specific activities of 4.01 U mg -1 protein and 0.35 U mg -1 protein, respectively. The \beta-xylosidase remained stable at up to 65 °C, but \alpha-L-arabinofuranosidase lost 10 % of its maximum activity at 55 °C. \beta-xylosidase and \alpha-L-arabinofuranosidase activities remained …
Characterization Of Endoxylanase Activity Fromthermomonospora Fusca Bd25, Müni̇r Tuncer
Characterization Of Endoxylanase Activity Fromthermomonospora Fusca Bd25, Müni̇r Tuncer
Turkish Journal of Biology
Thermomonospora fuscaBD25 produces relatively high levels of activity of endoxylanases. Only oat spelt xylan, RBB-xylan and birchwood xylan reacted with endoxylanases with the maximum specific activity of 47.65 U mg -1 protein on birchwood xylan. The endoxylanase remained stable up to 70 °C. At 60 °C endoxylanase activity showed stability (92 %) for 16 h, however it showed a half-life of 8 h at 70 °C and 30 min at 80 °C in the absence of substrate at pH 8.0. The relative endoxylanase activity in the pH ranges of 6.5 to 9.5 remained between 68 % and 72 % of …