Hydrolysis of oligosaccharides of the β-(1→4)-linkedd-xylose series by an endo(1→4)-β-d-xylanase from the anaerobic rumen fungusNeocallimastix frontalis
✍ Scribed by V. Garcia-Campayo; S. I. McCrae; T. M. Wood
- Publisher
- Springer
- Year
- 1994
- Tongue
- English
- Weight
- 441 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1573-0972
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✦ Synopsis
An endo-(1 --* 4)-jff-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)-ff-D-xylanase activity, but it differed from other fungal endo-(1 ~ 4)-ff-D-xylanases in that it had uniform action on the various internal linkages in the xylo-oligosaccharides.