Enhanced enzyme-catalyzed synthesis of l-methionine with ionic liquid additives |
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| Affiliation: | 1. Faculty of Applied Sciences, Ton Duc Thang University, Ho Chi Minh City, Viet Nam;2. Department of Biological Engineering, Inha University100 Inharo, Nam-gu, Incheon 22212, Republic of Korea;1. Developmental Biology, Washington University School of Medicine, 660 S. Euclid Avenue, Box 8103, St. Louis, MO 63110, USA;2. Department of Medicine, Washington University School of Medicine, 660 S. Euclid Avenue, Box 8103, St. Louis, MO 63110, USA;1. Imam Abdulrahman Bin Faisal University, Dammam, Saudi Arabia;2. Industrial Enzymes & Biofuels (IEBF) Group, I.B. Division, National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Jhang Road, Faisalabad, Pakistan;1. Wageningen University, Biobased Commodity Chemicals, Bornse Weilanden 9, 6708 WG, Wageningen, The Netherlands;2. Delft University, Applied Sciences, Julianalaan 136, 2628 BM, Delft, The Netherlands;1. School of Chemistry & Chemical Engineering, Shaanxi Normal University, Xi’an 710062, PR China;2. College of Chemistry and Chemical Engineering, Xianyang Normal University, Xianyang 712000, PR China;3. Key Laboratory of Macromolecular Science of Shaanxi Province, Shaanxi Normal University, Xi’an 710062, PR China |
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| Abstract: | The low solubility of l-methionine and low activity of enzyme are the major hurdles during l-methionine production by the enzymatic conversion approach. In this study, we investigated various ionic liquids (ILs) as additives for the enzyme-catalyzed production of l-methionine from O-acetyl L-homoserine and methyl mercaptan. Among the ILs evaluated, we found that tetraalkylammonium hydroxide ILs enhanced the solubility of l-methionine as well as the activity of the enzyme. Methionine solubility decreased with increasing alkyl chain length but increased with increasing IL concentration. l-methionine could be dissolved up to 232 g/L in 10% tetramethylammonium hydroxide solution. The enzyme O-acetylhomoserine aminocarboxypropyltransferase reached its maximum activity when the IL concentration was 2.5% (3 times higher than that without ILs) and significantly decreased with increasing IL concentration. The stability of the enzyme also decreased rapidly after 2 h of incubation regardless of the presence or absence of ILs. Nevertheless, 74 g/L of l-methionine could be produced in a reaction media containing 2.5% tetraethylammonium hydroxide compared to 35 g/L of l-methionine obtained in a reaction system without ILs. |
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| Keywords: | Ionic liquids Enzyme |
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