Optimization of lipase-catalyzed synthesis of acetylated EGCG by response surface methodology |
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| Institution: | 1. State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, PR China;2. School of Food Science and Technology, Jiangnan University, Wuxi 214122, PR China;1. Beijing Bioprocess Key Laboratory, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, PR China;2. Amoy-BUCT Industrial of Bio-technovation Institute, Amoy 361026, PR China;3. State Key Laboratory of Chemical Resource Engineering, Institute of Materia Medica, College of Science, Beijing University of Chemical Technology, Beijing 100029, PR China;1. Department of Chemical Engineering, Monash University, Clayton 3800, VIC, Australia;2. Institute of Thermodynamics, Helmut-Schmidt-University/University of Federal Armed Forces Hamburg, Holstenhofweg 85, Hamburg D-22043, Germany;1. Centre National de la Recherche Scientifique UMR 5221, Laboratoire Charles Coulomb, Université de Montpellier, Montpellier, France;2. Centre National de la Recherche Scientifique UMR 5149, Institut de Mathématiques et de Modélisation de Montpellier, Université de Montpellier, Montpellier, France;3. Faculté de Médecine, Laboratoire d’Hématologie, Hôpital Saint Eloi, The Cardiovascular Health Research Unit de Montpellier, Montpellier, France;4. Centre National de la Recherche Scientifique UMR 5048-UM–Institut National de la Santé et de la Recherche Médicale UMR 1054, Centre de Biochimie Structurale, Montpellier, France;1. Heterogeneous biocatalysis group, CIC Biomagune, Parque tecnológico de San Sebastián, Edificio Empresarial “C”, Paseo Miramón 182, 20009 Donostia-San Sebastián Guipúzcoa, Spain;2. Departamento de Biotecnología Universidad Autónoma Metropolitana Iztapalapa, Av. San Rafael Atlixco #186, Col. Vicentina 09340, Distrito Federal, Mexico;3. Departamento de Biocatálisis, Instituto de Catálisis (CSIC), Campus UAM Cantoblanco, 28049, Madrid, Spain;4. Mass spectrometry. CIC Biomagune, Parque tecnológico de San Sebastián, Edificio Empresarial “C”, Paseo Miramón 182, 20009 Donostia-San Sebastián Guipúzcoa, Spain;5. Centro de Biología Molecular Severo Ochoa, CSIC-UAM, Departamento de Biología Molecular, Campus UAM, Cantoblanco, 28049 Madrid, Spain;6. IKERBASQUE, Basque Foundation for Science, Bilbao, Spain;1. Key Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People’s Republic of China;2. National Key Laboratory of Agro-Microbiology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People’s Republic of China;3. College of Food Science and Technology, Huazhong Agricultural University, Wuhan, 430070, People’s Republic of China |
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| Abstract: | (−)-Epigallocatechin-3-O-gallate (EGCG) acetylated derivatives, which can be widely used as a natural antioxidant in both lipid containing food and cosmetic applications, were prepared by lipase catalyzed acylation of EGCG with vinyl acetate. Response surface methodology (RSM) and 5-level-4-factor central composite rotatable design (CCRD) were employed to evaluate the effects of synthesis parameters, such as reaction time (6–10 h), temperature (30–50 °C), enzyme amount (1.5–2.5% (w/w) of substrate), and substrate molar ratio of EGCG to vinyl acetate (0.5–1.5) on conversion of EGCG. By using multiple regression analysis, the experimental data were fitted to a second order polynomial model. The most suitable combination of variables was 40 °C, 2.12%, 10 h and 1.13 for the reaction temperature, the enzyme amount, the reaction time, and EGCG/vinyl acetate mole ratio, respectively. At these optimal conditions, the conversion yield reached 87.37%. The presence of mono-, di- and tri-acetylated derivatives in acetylated EGCG was confirmed by LC–MS-MS and identified as 5″-O-acetyl-EGCG, 3″, 5″-2-O-acetyl-EGCG and 5′, 3″, 5″-3-O-acetyl-EGCG by NMR. |
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| Keywords: | EGCG Acetylation Lipase Optimization Response surface methodology |
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