Improved Stability and Catalytic Efficiency of ω-Transaminase in Aqueous Mixture of Deep Eutectic Solvents
The efficient biosynthesis of chiral amines at an industrial scale to meet the high demand from industries that require chiral amines as precursors is challenging due to the poor stability and low catalytic efficiency of ω-transaminases (ω-TAs). Herein, this study adopted a green and efficient solve...
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MDPI AG
2023-05-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/9/3895 |
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| author | Hongpeng Wang Mercy Vimbai Masuku Yachen Tao Jiayao Yang Yi Kuang Changjiang Lyu Jun Huang Shengxiang Yang |
| author_facet | Hongpeng Wang Mercy Vimbai Masuku Yachen Tao Jiayao Yang Yi Kuang Changjiang Lyu Jun Huang Shengxiang Yang |
| author_sort | Hongpeng Wang |
| collection | DOAJ |
| description | The efficient biosynthesis of chiral amines at an industrial scale to meet the high demand from industries that require chiral amines as precursors is challenging due to the poor stability and low catalytic efficiency of ω-transaminases (ω-TAs). Herein, this study adopted a green and efficient solvent engineering method to explore the effects of various aqueous solutions of deep eutectic solvents (DESs) as cosolvents on the catalytic efficiency and stability of ω-TA. Binary- and ternary-based DESs were used as cosolvents in enhancing the catalytic activity and stability of a ω-TA variant from <i>Aspergillus terreus</i> (E133A). The enzyme exhibited a higher catalytic activity in a ternary-based DES that was 2.4-fold higher than in conventional buffer. Moreover, the thermal stability was enhanced by a magnitude of 2.7, with an improvement in storage stability. Molecular docking studies illustrated that the most potent DES established strong hydrogen bond interactions with the enzyme’s amino acid, which enhanced the catalytic efficiency and improved the stability of the ω-TA. Molecular docking is essential in designing DESs for a specific enzyme. |
| first_indexed | 2024-03-11T04:12:33Z |
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| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-11T04:12:33Z |
| publishDate | 2023-05-01 |
| publisher | MDPI AG |
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| series | Molecules |
| spelling | doaj.art-d37097c64e6d4c738c05a2cf733f85df2023-11-17T23:24:55ZengMDPI AGMolecules1420-30492023-05-01289389510.3390/molecules28093895Improved Stability and Catalytic Efficiency of ω-Transaminase in Aqueous Mixture of Deep Eutectic SolventsHongpeng Wang0Mercy Vimbai Masuku1Yachen Tao2Jiayao Yang3Yi Kuang4Changjiang Lyu5Jun Huang6Shengxiang Yang7Zhejiang Provincial Key Lab for Chemical and Biological Processing Technology of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, ChinaZhejiang Provincial Key Lab for Chemical and Biological Processing Technology of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, ChinaZhejiang Provincial Key Lab for Chemical and Biological Processing Technology of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, ChinaZhejiang Provincial Key Lab for Chemical and Biological Processing Technology of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, ChinaZhejiang Provincial Key Laboratory of Chemical Utilization of Forestry Biomass, Zhejiang A&F University, Hangzhou 311300, ChinaZhejiang Provincial Key Lab for Chemical and Biological Processing Technology of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, ChinaZhejiang Provincial Key Lab for Chemical and Biological Processing Technology of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, ChinaZhejiang Provincial Key Laboratory of Chemical Utilization of Forestry Biomass, Zhejiang A&F University, Hangzhou 311300, ChinaThe efficient biosynthesis of chiral amines at an industrial scale to meet the high demand from industries that require chiral amines as precursors is challenging due to the poor stability and low catalytic efficiency of ω-transaminases (ω-TAs). Herein, this study adopted a green and efficient solvent engineering method to explore the effects of various aqueous solutions of deep eutectic solvents (DESs) as cosolvents on the catalytic efficiency and stability of ω-TA. Binary- and ternary-based DESs were used as cosolvents in enhancing the catalytic activity and stability of a ω-TA variant from <i>Aspergillus terreus</i> (E133A). The enzyme exhibited a higher catalytic activity in a ternary-based DES that was 2.4-fold higher than in conventional buffer. Moreover, the thermal stability was enhanced by a magnitude of 2.7, with an improvement in storage stability. Molecular docking studies illustrated that the most potent DES established strong hydrogen bond interactions with the enzyme’s amino acid, which enhanced the catalytic efficiency and improved the stability of the ω-TA. Molecular docking is essential in designing DESs for a specific enzyme.https://www.mdpi.com/1420-3049/28/9/3895catalytic efficiencydeep eutectic solventsthermal stabilitymolecular docking |
| spellingShingle | Hongpeng Wang Mercy Vimbai Masuku Yachen Tao Jiayao Yang Yi Kuang Changjiang Lyu Jun Huang Shengxiang Yang Improved Stability and Catalytic Efficiency of ω-Transaminase in Aqueous Mixture of Deep Eutectic Solvents Molecules catalytic efficiency deep eutectic solvents thermal stability molecular docking |
| title | Improved Stability and Catalytic Efficiency of ω-Transaminase in Aqueous Mixture of Deep Eutectic Solvents |
| title_full | Improved Stability and Catalytic Efficiency of ω-Transaminase in Aqueous Mixture of Deep Eutectic Solvents |
| title_fullStr | Improved Stability and Catalytic Efficiency of ω-Transaminase in Aqueous Mixture of Deep Eutectic Solvents |
| title_full_unstemmed | Improved Stability and Catalytic Efficiency of ω-Transaminase in Aqueous Mixture of Deep Eutectic Solvents |
| title_short | Improved Stability and Catalytic Efficiency of ω-Transaminase in Aqueous Mixture of Deep Eutectic Solvents |
| title_sort | improved stability and catalytic efficiency of ω transaminase in aqueous mixture of deep eutectic solvents |
| topic | catalytic efficiency deep eutectic solvents thermal stability molecular docking |
| url | https://www.mdpi.com/1420-3049/28/9/3895 |
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