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.

      Esterase catalysis of substrate vapour: enzyme activity occurs at very low hydration

      Lind, Penelope A.; Daniel, Roy M.; Monk, Colin R.; Dunn, Rachel V.
      DOI
       10.1016/j.bbapap.2004.08.005
      Find in your library  
      Citation
      Export citation
      Lind, P.A., Daniel, R.M., Monk, C. & Dunn, R.V. (2004). Esterase catalysis of substrate vapour: enzyme activity occurs at very low hydration. Biochimica et Biophysica Acta (BBA) – Proteins & Proteomics, 1702(1), 103-110.
      Permanent Research Commons link: https://hdl.handle.net/10289/4444
      Abstract
      It has been generally accepted that enzyme activity requires a minimal hydration of about 0.2 g H2O g⁻¹ protein. This fits well with evidence that hydration above this level is associated with the onset of intramolecular motions. The influence of enzyme hydration on the hydrolysis of substrate by Candida rugosa Lipase B and pig liver esterase was investigated. Each enzyme was studied as a powder at various hydration levels, using vapour phase ethyl butyrate as substrate. This procedure allows the separation of those effects that are due to hydration from those arising from diffusional constraints. We found hydrolytic activity in both enzymes at all hydration levels above zero (between 0.054–0.47 and 0.029–0.60 g H2O g⁻¹ protein, respectively) that were investigated. The lowest hydration level investigated, <0.03 g H2O g⁻¹ enzyme, corresponded to a water/enzyme mole ratio of 100 and a coverage of about 10% of the enzyme surface by water molecules. The hydrolytic activity of both enzymes was dependent on protein hydration. However, since the hydrolysis of ethyl butyrate requires water as a second substrate, the absence of activity at zero hydration does not rule out the possibility of enzyme activity in the absence of water. These results suggest that the properties conferred on proteins by water, at least above 10% surface coverage (in this case corresponding to a hydration level of 0.03 g H2O g⁻¹ protein), are not a requirement for enzyme catalysis.
      Date
      2004-10
      Type
      Journal Article
      Publisher
      Elsevier
      Collections
      • Science and Engineering Papers [3122]
      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