Enantio convergent biotransformation of O,O-dimethyl-4-oxoazetidin-2-ylphosphonate using fungal cells of Penicillium minioluteum and purified enzymes |
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| Affiliation: | 1. Politehnica University of Timişoara, Faculty of Industrial Chemistry and Environmental Engineering, Carol Telbisz 6, 300001 Timisoara, Romania;2. Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar Tudósok körútja 2, H-1117 Budapest, Hungary;3. Research Institute of Chemical and Process Engineering, Faculty of Information Technology, University of Pannonia, Egyetem utca 10, H-8200 Veszprém, Hungary;1. Division of Genetics and Molecular Biology, Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia;2. Centre for Research in Biotechnology for Agriculture, Level 5, Block B, Institute of Postgraduate Studies, University of Malaya, 50603 Kuala Lumpur, Malaysia;3. Zoology Branch, Forest Biodiversity Division, Forest Research Institute Malaysia (FRIM), 52109 Kepong, Selangor, Malaysia;1. Photovoltaic Laboratory Research and Technology Centre of Energy, Borj-Cedria Science and Technology Park, BP 95, 2050 Hammam-Lif, Tunisia;2. University of Applied Medical Sciences of Hafr El Baten, Saudie Arabia;1. State Key Laboratory of Metastable Materials Science and Technology, College of Materials Science and Engineering, Yanshan University, Qinhuangdao 066004, PR China;2. College of Physics and Chemistry, Henan Polytechnic University, Jiaozuo, Henan 454000, PR China;1. College of Power Engineering, Chongqing University, Chongqing 400044, China;2. Key Laboratory of Low-grade Energy Utilization Technologies and Systems, Ministry of Education of PRC, Chongqing 400044, China;1. Institute of Electronics, Silesian University of Technology, 44-100 Gliwice, Poland;2. CNR- SPIN & Department of Physics and Chemical Sciences, University of L’Aquila, 67100, Italy |
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| Abstract: | This report presents the bioconversion of O,O-dimethyl-4-oxoazetidin-2-ylphosphonate 1 performed in two ways: with the enzymatic system of P. minioluteum and with the application of purified enzymes: penicillinase and two proteases of different origin. Recorded NMR spectra allowed confirming the reaction progress and also postulating possible mechanism of conversion. The path of bioconversion was defined as enantio convergent process for both modes of applied biocatalysts. This means that kinetically driven resolution of racemic mixture of the substrate leads to the one enantiomer of the product. The bioconversion started from ester bond hydrolysis (equally in both enantiomers) with the conversion degree from 30% (whole-cell) to 35% (isolated enzymes) and with the production of optically pure monoester (compound 2; 100% of e.e). For whole-cell bioprocess it was the initiative step for the enantioselective amide bond hydrolysis, what resulted in synthesis of desired product 3-amino-3-phosphonopropanoic acid 4. However, the most effective enzymatic hydrolysis of ester bond performed with penicillinase from Enterobacter cloacae led only to the monoester product 2. |
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| Keywords: | Phosphonates Biotransformation Fungus Hydrolases |
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