Abstract
An endo-(1→4)-β-d-xylanase from Neocallimastix frontalis was purified by anion-exchange chromatography. The enzyme had an apparent molecular mass of 30 kDa on SDS-PAGE and exhibited maximum activity at 50°C and at pH values between 6.0 and 6.6. Kinetic studies on the hydrolysis of xylo-oligosaccharides, ranging from xylobiose to xylodecaose, showed that xylohexaose and xyloheptaose were the preferred substrates for the enzyme and that xylobiose, xylotriose and xylotetraose were not hydrolysed. Xylose was not a product of the hydrolysis of any of the xylo-oligosaccharide substrates tested. The enzyme appeared to have a strong preference for the hydrolysis of the internal glycosidic bonds of the oligosaccharides, which is typical of endo-(1→4)-β-d-xylanase activity, but it differed from other fungal endo-(1→4)-β-d-xylanases in that it had uniform action on the various internal linkages in the xylo-oligosaccharides.
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V. Garcia-Campayo, S.I. McCrae and T.M. Wood are with The Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB2 9SB, UK
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Garcia-Campayo, V., McCrae, S.I. & Wood, T.M. Hydrolysis of oligosaccharides of the β-(1→4)-linked d-xylose series by an endo(1→4)-β-d-xylanase from the anaerobic rumen fungus Neocallimastix frontalis . World Journal of Microbiology & Biotechnology 10, 64–68 (1994). https://doi.org/10.1007/BF00357566
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DOI: https://doi.org/10.1007/BF00357566