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Lipase catalyzed esterification in AOT reverse micelles: A structural study
Affiliation:1. Laboratoire SRSI, URA CNRS 1662, Université P. et M. Curie, 4 Place Jussieu, 75005 Paris, France;2. Service de Chimie Moléculaire, DRECAM, CEA, CE Saclay, 91191 Gif sur Yvette Cedex, France;3. National Hellenic Research Foundation, Athens, Greece;1. Food Chemistry and Food Development, Department of Biochemistry, University of Turku, Finland;2. Department of Nutrition & Food Hygiene, School of Public Health, Peking University Health Science Center, Beijing, China;3. Science Institute, University of Iceland, Iceland;1. National and Local United Engineering Laboratory for New Petrochemical Materials and Fine Utilization of Resources, Key Laboratory of Resource Fine-Processing and Advanced Materials of Hunan Province, College of Chemistry and Chemical Engineering, Hunan Normal University, Changsha 410081, PR China;2. School of Chemical and Environmental Engineering, China University of Mining and Technology (Beijing), Beijing 100083, PR China;3. College of Environmental Science and Engineering, Hunan University, Changsha 410082, PR China
Abstract:AOT reverse micelles are used to cosolubilize hydrophilic and hydrophobic reactants of lipase catalysed esterification. Depending on the nature of the alcohol, a drastic change of the initial rate of the esterification is observed. A structural study of the micellar system with and without reactant is undertaken to explain the change in the activity with the various alcohols.
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