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.

      Properties of a thermostable β-glucosidase immobilized using tris(hydroxymethyl)phosphine as a highly effective coupling agent

      Oswald, Paul R.; Evans, Rachel A.; Henderson, William; Daniel, Roy M.; Fee, Conan J.
      DOI
       10.1016/S0141-0229(98)00005-2
      Find in your library  
      Citation
      Export citation
      Oswald, P.R., Evans, R.A., Henderson, W., Daniel, R.M. & Fee, C.J. (1998). Properties of a thermostable β-glucosidase immobilized using tris(hydroxymethyl)phosphine as a highly effective coupling agent. Enzyme and Microbial Technology, 23(1-2), 14-19.
      Permanent Research Commons link: https://hdl.handle.net/10289/4465
      Abstract
      A very stable b-glucosidase (EC 3.2.1.21) was immobilized to polyacrylamide-magnetite beads, aminopropyl silica, and chitosan using tris(hydroxymethyl)phosphine (THP) or glutaraldehyde as the coupling reagent. The use of THP on chitosan resulted in greater than 90% yields with respect to free enzyme activity compared with only 60% observed when using the more conventional glutaraldehyde coupling reagent. THP-immobilized enzyme also lost activity more slowly than both glutaraldehyde-immobilized and the free enzyme when incubated at 90°C. Repetitive assays of THP and glutaraldehyde-immobilized enzyme also showed that THP was more able to retain active enzyme on the silica-based support. The pH optimum and Km app were unchanged with respect to free enzyme.
      Date
      1998
      Type
      Journal Article
      Publisher
      Elsevier
      Collections
      • Science and Engineering Papers [3211]
      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