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An efficient enzymatic synthesis of 5-aminovaleric acid
Affiliation:1. Laboratory of Organic Chemistry, Wageningen University, Dreijenplein 8, 6703 HB, Wageningen, The Netherlands;2. Agrotechnology and Food Sciences Group, Wageningen UR, Wageningen, The Netherlands;3. Valorisation of Plant Production Chains, Wageningen University, Wageningen, The Netherlands;4. University “A. Vlaicu”, Arad, Romania;1. Department of Biological Engineering, College of Engineering, Konkuk University, Seoul, Republic of Korea;2. Deparment of Biotechnology, The Catholic University of Korea, Bucheon, Republic of Korea;3. Department of Environmental and Safety Engineering, College of Engineering, Ajou University, Gyeonggi-do, Republic of Korea;4. Department of Energy Systems Research, Ajou University, Gyeonggi-do, Republic of Korea;5. Department of Biological and Chemical Engineering, Hongik University, Sejong, Republic of Korea;1. Key Laboratory of Industrial Biocatalysis (Ministry of Education), Department of Chemical Engineering, Tsinghua University, Beijing, 100084, China;2. Tsinghua Innovation Center in Dongguan, Dongguan, 523808, China;3. Center for Synthetic and Systems Biology, Tsinghua University, Beijing, 100084, China;4. School of Physiology, Pharmacology & Neuroscience, Faculty of Life Sciences, University of Bristol, Bristol, BS8 1TD, United Kingdom;1. State Key Laboratory of Bioreactor Engineering, School of Biotechnology, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, China;2. State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, 800 Dong Chuan Road, Shanghai, 200240, China;3. Shanghai Collaborative Innovation Center for Biomanufacturing Technology (SCICBT), East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, China
Abstract:The title compound was prepared enzymatically from l-lysine in an excellent yield and under buffer-free conditions. l-Lysine was oxidized by the action of l-lysine α-oxidase from Trichoderma viride followed by spontaneous oxidative decarboxylation of the intermediate 6-amino-2-oxocaproic acid in the reaction medium. l-Lysine α-oxidase was immobilized on an epoxy-activated solid support (Sepabeads EC-EP) and the activity of both solution-based and immobilized enzyme in this reaction was determined.
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