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Turkish Journal of Biology

MÜNİR TUNCER

DOI

-

Abstract

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 the activity at pH 8.0. The apparent K m value for the crude endoxylanase was 6.66 mg of oat spelt xylan ml -1 , while the V max value was 2.5 mmol reducing sugar min -1 ml -1 . Endoxylanase activity was affected by the addition of xylobiose (1 mM) to the reaction mixture of endoxylanase preparation and resulted in approximately 25 % reduction in activity. Also, the addition of supernatant fluids from cultures grown on xylan (reducing sugar concentration of 1 mg ml -1 xylose equivalent) to the reaction mixture resulted in approximately 30 % reduction in activity.

Keywords

Endo-1, 4-\beta-xylanase, lignocellulose degradation, Thermomonospora fusca, xylan, actinomycete.

First Page

737

Last Page

752

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