Lipase immobilized in ordered mesoporous silica: A powerful biocatalyst for ultrafast kinetic resolution of racemic secondary alcohols |
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| Institution: | 1. Oil Crops Research Institute, Chinese Academy of Agricultural Sciences, Hubei Key Laboratory of Lipid Chemistry and Nutrition, Key laboratory of Biology and Genetic Improvement of Oil Crops, Ministry of Agriculture, Wuhan 430062, China;2. Functional Oil Laboratory Associated by Oil Crops Research Institute, Chinese Academy of Agricultural Sciences and Infinite (China) Co. LTD, Guangzhou 51000, China;1. Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, M?egyetem rkp. 3, H-1111 Budapest, Hungary;2. Fermentia Ltd., Berlini út. 47-49, H-1049, Budapest, Hungary;3. SynBiocat Ltd., Löv?ház u 19/1, H-1024 Budapest, Hungary;4. Department of Physical Chemistry and Materials Science, Budapest University of Technology and Economics, Budafoki út 8, H-1111 Budapest, Hungary;5. Agricultural Institute, Centre of Agricultural Research, Hungarian Academy of Sciences, Brunszvik u. 2, H-2462 Martonvásár, Hungary;6. Department of Inorganic and Analytical Chemistry, Budapest University of Technology and Economics, Szt. Gellért tér 4, H-1111 Budapest, Hungary;1. BRD School of Biosciences, Satellite Campus, Vadtal Road, P.O. Box # 39, Sardar Patel University, Vallabh Vidhyanagar, Anand 388 120, Gujarat, India;2. Department of Materials Science, Sardar Patel University, Vallabh Vidhyanagar, Anand 388 120, Gujarat, India;1. Laboratory of Applied Organic Chemistry, Sciences Faculty, Chemistry Department, University of Badji Mokhtar, P.O. Box 12, 23000 Annaba, Algeria;2. Istituto di Chimica del Riconoscimento Molecolare, CNR, via Mario Bianco 9, 20131 Milan, Italy |
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| Abstract: | Although Burkholderia cepacia lipase (BCL) has been proved to be a potential catalyst for chiral resolution, it is rarely applied in industry because of the low catalysis activity and poor stability of the free form. In this article, BCL was immobilized on the phenyl-modified ordered mesoporous silica (Ph-OMMs) to obtain a novel immobilized lipase. Benefits from the bottle-neck mesoporous structure, high loading of BCL could be completed within only 15 min. When BCL@Ph-OMMs was used as a catalyst for the resolution of 1-phenylethanol, up to 50% conversion with more than 99% ees was obtained within only 25 min, which is about 65-folds faster than that of the free lipase. Stabilized BCL@Ph-OMMs was successfully used for the ultrafast resolution of six secondary alcohols by selectivity transesterification, which reached high conversion (50%) and high enantioselectivity (≥99%) within 20–180 min. The activity of BCL@Ph-OMMs was kept relatively constant in 50 consecutive cycles, which is the best result among the reported immobilized lipases. The study suggests that BCL@Ph-OMMs is an attractive catalyst in industrial applications. |
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| Keywords: | Lipase Ordered mesoporous silica Biocatalyst Kinetic resolution Secondary alcohols |
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