Purification and properties of synephrinase from Arthrobacter synephrinum |
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| Authors: | V Manne K R Kutty S R Pillarisetti |
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| Affiliation: | 1. Department of Genetics, University of Georgia, Athens, GA 30602, USA;2. Department of Food Science and Technology, Chung-Ang University, Anseong Gyeonggi 17546, Republic of Korea;3. Oak Ridge National Laboratory, The BioEnergy Science Center and the Center for Bioenergy Innovation, Oak Ridge, TN 37831, USA;1. Department of Chemical Engineering and Biotechnological Engineering, Université de Sherbrooke, 2500 Boulevard de l’Université, Sherbrooke, Québec J1K 2R1, Canada;2. Department of Civil Engineering, Université de Sherbrooke, 2500 Boulevard de l’Université, Sherbrooke, Québec J1K 2R1, Canada;1. State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, PR China;2. University of Chinese Academy of Sciences, Beijing 100049, PR China;1. Key Laboratory of Forestry Genetics & Biotechnology (Nanjing Forestry University), Ministry of Education, Nanjing, 210037, People’s Republic of China;2. Jiangsu Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, College of Chemical Engineering, Nanjing Forestry University, Nanjing, 210037, People’s Republic of China;3. Jiangsu Province Key Laboratory of Green Biomass-based Fuels and Chemicals, Nanjing, 210037, People’s Republic of China;4. Institute of Industrial Biotechnology, GC University, Lahore, 54000, Pakistan |
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| Abstract: | Synephrinase, an enzyme catalyzing the conversion of (-)-synephrine into p-hydroxyphenylacetaldehyde and methylamine, was purified to apparent homogeneity from the cell-free extracts of Arthrobacter synephrinum grown on (+/-)-synephrine as the sole source of carbon and nitrogen. A 40-fold purification was sufficient to produce synephrinase that is apparently homogeneous as judged by native polyacrylamide gel electrophoresis and has a specific activity of 1.8 mumol product formed/min/mg protein. Thus, the enzyme is a relatively abundant enzyme, perhaps comprising as much as 2.5% of the total protein. The enzyme essentially required a sulfhydryl compound for its activity. Metal ions like Mg2+, Ca2+, and Mn2+ stimulated the enzyme activity. Metal chelating agents, thiol reagents, denaturing agents, and metal ions like Zn2+, Hg2+, Ag1+, and Cu2+ inhibited synephrinase activity. Apart from (-)-synephrine, the enzyme acted upon (+/-)-octopamine and beta-methoxysynephrine. Molecular oxygen was not utilized during the course of the reaction. The molecular mass of the enzyme as determined by Sephadex G-200 chromatography, was around 156,000. The enzyme was made up of four identical subunits with a molecular mass of 42,000. |
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