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 characterisation of a thermostable endo-β-1,4-mannanase cloned from “Caldocellum saccharolyticum”

      Bicho, Paul A.; Clark, Tom A.; Mackie, Keith; Morgan, Hugh W.; Daniel, Roy M.
      DOI
       10.1007/BF00208153
      Link
       www.springerlink.com
      Find in your library  
      Citation
      Export citation
      Bicho, P.A., Clark, T.A., Mackie, K., Morgan, H.W. & Daniel, R.M. (1991). The characterisation of a thermostable endo-β-1,4-mannanase cloned from “Caldocellum saccharolyticum”. Applied Microbiology and Biotechnology, 36(3), 337-343.
      Permanent Research Commons link: https://hdl.handle.net/10289/4493
      Abstract
      An endo-gb-1,4-mannanase cloned from caldocellum saccharolyticum and expressed in Escherichia coli was partially purified. The purification involved heat treatment, anion exchange and gel filtration. The mannanase was only active against mannan, glucomannans and galactoglucomannans and obeyed Michaelis-Menten kinetics on these substrates. The rate and extent of hydrolysis was dependent on the type of substrate. Galactomannans were not as readily depolymerized as the mannan and glucomannans investigated. The glucose content of the glucomannans did not affect the rate of hydrolysis and only slightly affected the extent. The molecular mass of the mannanase was estimated at 39 kDa. The pH and temperature optima were 6.5 and 80° C respectively. The mannanase was very thermostable with a half life of 48 min at 85° C and no loss in activity after 24 h at 70° C.
      Date
      1991
      Type
      Journal Article
      Publisher
      Springer
      Collections
      • Science and Engineering Papers [3071]
      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