Kinetics and optimization of lipase-catalyzed synthesis of rose fragrance 2-phenylethyl acetate through transesterification |
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| Institution: | 1. College of Tea and Food Science, Wuyi University, 16 Wuyi Avenue, Wuyishan City, Fujian 354300, China;2. Department of Chemical Engineering and Agricultural Biotechnology Center, National Chung Hsing University, 250 Kuo-Kuang Road, Taichung 402, Taiwan;3. Department of Energy and Materials Technology, Hsiuping Institute of Technology, 11 Gongye Road, Taichung 402, Taiwan;4. Biotechnology Center, National Chung Hsing University, 250 Kuo-Kuang Road, Taichung 402, Taiwan;1. Institute of Microbiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, CZ-142 20 Prague, Czech Republic;2. Department of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, Institute of Chemical Technology, Technická 3, CZ-166 28 Prague, Czech Republic;3. Department of Biochemistry, Charles University in Prague, Hlavova 8, CZ-128 40 Prague, Czech Republic;4. Department of Industrial and Information Engineering and Economics, University of l’Aquila, via Giovanni Gronchi n.18 - Nucleo Industriale di Pile, I-67100 L’Aquila, Italy;1. Department of Chemical Engineering, University of Bath, Claverton Down, Bath, BA2 7AY, UK;2. Department of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK;1. Key Laboratory for Molecular Enzymology and Engineering, The Ministry of Education, School of Life Science, Jilin University, Changchun 130012, China;2. Department of Engineering, Aarhus University, Gustav Wieds Vej 10, Aarhus 8000, Denmark;3. College of Pharmacy, Jilin University, Changchun 130021, China;1. Fraunhofer Institute for Process Engineering and Packaging (IVV), Giggenhauserstraße 35, 85354 Freising, Germany;2. Institute for Food Technology and Food Chemistry, Technical University Berlin, Königin-Luise-Straße 22, 14195 Berlin, Germany;1. Catalyst and Advanced Materials Research Laboratory, Chemical Engineering Department, Faculty of Engineering, University of Kashan, Kashan, Iran;2. Institute of Nanoscience and Nanotechnology, University of Kashan, Kashan, Iran;1. Faculty of Pharmaceutical Sciences, Federal University of Amazonas (UFAM), Manaus, AM, Brazil;2. Serviço Nacional de Aprendizagem Industrial - Unidade Portão, Rua Padre Leonardo Nunes, 180, Portão, 80330-320, Curitiba, PR, Brazil;3. Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-0006, Japan;4. Department of Food Science, School of Food Engineering, University of Campinas, Campinas, SP, Brazil;5. Institute of Science and Technology, UFVJM, Diamantina, MG, Brazil |
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| Abstract: | Lipase from Candida rugosa was immobilized on a polyvinylidene fluoride membrane for synthesis of rose flavor ester, 2-phenylethyl acetate. Response surface methodology (RSM) was employed for kinetic modeling of process and prediction the yield. The RSM was used in practice for determining the kinetic models by fitting the initial rate dates based on the equations of ping-pong bi–bi and order bi–bi model. The maximum reaction rate and kinetic constants were matched with the order bi–bi model. The specificity constant of the immobilized lipase was 10-folds higher than the free form indicated the enzyme–substrate affinity, and catalytic ability was enhanced after immobilization. Moreover, the effects of reaction parameters on the yield were evaluated by RSM using a Box–Behnken experimental design. Based on a ridge max analysis, the maximum conversion was 95.33 ± 2.57% at 38.78 h, 35.85 °C, and substrate mole ratio of 3.65:1. Furthermore, the order bi–bi kinetic model was simulated successfully in a batch reaction. A good prediction existed between the RSM results and integrated equation was found. |
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| Keywords: | Transesterification Kinetics Lipase 2-Phenylethyl acetate Response surface methodology |
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