Research Commons
      • Browse 
        • Communities & Collections
        • Titles
        • Authors
        • By Issue Date
        • Subjects
        • Types
        • Series
      • Help 
        • About
        • Collection Policy
        • OA Mandate Guidelines
        • Guidelines FAQ
        • Contact Us
      • My Account 
        • Sign In
        • Register
      View Item 
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      JavaScript is disabled for your browser. Some features of this site may not work without it.

      The activity of family 11 xylanases at alkaline pH

      Gibbs, M.D.; Reeves, R.A.; Hardiman, E.M.; Choudhary, P.R.; Daniel, Roy M.; Bergquist, Peter L.
      DOI
       10.1016/j.nbt.2010.06.004
      Find in your library  
      Citation
      Export citation
      Gibbs, 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.
      Permanent Research Commons link: https://hdl.handle.net/10289/4092
      Abstract
      Xylanases 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.
      Date
      2010
      Type
      Journal Article
      Publisher
      Elsevier
      Collections
      • Science and Engineering Papers [3119]
      Show full item record  

      Usage

       
       
       

      Usage Statistics

      For this itemFor all of Research Commons

      The University of Waikato - Te Whare Wānanga o WaikatoFeedback and RequestsCopyright and Legal Statement