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dc.contributor.authorGibbs, M.D.
dc.contributor.authorReeves, R.A.
dc.contributor.authorHardiman, E.M.
dc.contributor.authorChoudhary, P.R.
dc.contributor.authorDaniel, Roy M.
dc.contributor.authorBergquist, Peter L.
dc.identifier.citationGibbs, M.D., Reeves, R.A., Hardiman, E.M., Choudhary, P.R., Daniel, R.M. & Bergquist, P.L. (2010). The activity of family 11 xylanases at alkaline pH. New Biotechnology, 27(6), 795-802.en_NZ
dc.description.abstractXylanases have several industrial uses, particularly in baking, modification of animal feed and in pulp bleaching in the paper industry. Process conditions in kraft pulp bleaching generally favour an enzyme that is active at high pH values. The activities of several glycosyl hydrolase family 11 xylanases reported to be active under alkaline conditions were determined under optimal conditions and found to have optima in the pH 5–6 range. Only one enzyme tested, BadX, was shown to have an alkaline pH optimum. Significant activity at pH values higher than 8 appears often to be the result of excess enzyme added to the reaction mixtures so that substrate is limiting. The different nature of laboratory and industrial substrates needs to be taken into consideration in designing assay conditions. In some cases, significant differences were observed in pH profiles generated using a small-molecule substrate when compared to those generated using xylan. We conclude that small-molecule substrates are not a suitable proxy for determining the pH profiles of family 11 xylanases.en_NZ
dc.titleThe activity of family 11 xylanases at alkaline pHen_NZ
dc.typeJournal Articleen_NZ
dc.relation.isPartOfNew Biotechnologyen_NZ

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