Hydrophobic deep eutectic solvents-lipase synergistically catalyze the synthesis of Vitamin E succinate via hydrogen bonds

Ma, Guangzheng; Zhang, Zihan; Lu, Zeping; Qi, Yuan; Nian, Binbin; Hu, Yi

doi:10.1016/j.molliq.2023.123711

Cited by 9 publications

(1 citation statement)

References 55 publications

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“…Coincidentally, Hollenbach et al [ 84 ] found that the ester exchange activity of lipases in urea-based DESs was significantly higher than that of glucose-based DESs due to similar reasons. Through circular dichroism, Ma et al [ 85 ] found that when DESs were used as a reactive medium, the proportion of β-turn in the structure of Candida rugosa lipase (CRL) was significantly increased, which in turn stabilized the secondary structure of CRL. Analysis of molecular dynamics (MD) simulations demonstrated that stabilizing hydrogen bonds were formed between DESs and CRL, which could significantly increase the affinity between CRL and its substrates and enhance the catalytic activity of CRL.…”

Section: Effect Of Different Solvents On Stability and Activity Of Li...mentioning

confidence: 99%

Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art

Chen,

Jin,

Nian

et al. 2024

Molecules

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Lipases, crucial catalysts in biochemical synthesis, find extensive applications across industries such as food, medicine, and cosmetics. The efficiency of lipase-catalyzed reactions is significantly influenced by the choice of solvents. Polar organic solvents often result in a decrease, or even loss, of lipase activity. Conversely, nonpolar organic solvents induce excessive rigidity in lipases, thereby affecting their activity. While the advent of new solvents like ionic liquids and deep eutectic solvents has somewhat improved the activity and stability of lipases, it fails to address the fundamental issue of lipases’ poor solvent tolerance. Hence, the rational design of lipases for enhanced solvent tolerance can significantly boost their industrial performance. This review provides a comprehensive summary of the structural characteristics and properties of lipases in various solvent systems and emphasizes various strategies of protein engineering for non-aqueous media to improve lipases’ solvent tolerance. This study provides a theoretical foundation for further enhancing the solvent tolerance and industrial properties of lipases.

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Section: Effect Of Different Solvents On Stability and Activity Of Li...mentioning

confidence: 99%

Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art

Chen,

Jin,

Nian

et al. 2024

Molecules

Self Cite

View full text Add to dashboard Cite

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Efficient enzymatic synthesis of vitamin E succinate using an organic solvent‐stable immobilized lipase

Li,

Lin,

Lan

et al. 2024

J Americ Oil Chem Soc

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Vitamin E succinate has gained substantial attention as a potential therapeutic agent for cancer treatment due to its biomedical activities. One of the prominent methods of synthesizing vitamin E succinate is through enzymatic processes, which, although advantageous, presents inherent challenges related to optimization, scalability, and particularly, the poor stability of lipases in organic solvents. Our study addresses these challenges by conducting a comprehensive comparative analysis between Lipase UM1 and three other immobilized commercial lipases, demonstrating Lipase UM1's enhanced resistance to organic solvents and its superior efficiency in vitamin E succinate production. Further optimization experiments with Lipase UM1 led to an unprecedented conversion of 99%. Additionally, we scaled the reaction to a proof‐of‐concept industrial level. The synthesized product was verified using Fourier transform infrared spectroscopy and nuclear magnetic resonance analysis, ensuring its quality and consistency. This study validates Lipase UM1 as an efficient catalyst for vitamin E succinate synthesis, offering a promising avenue for industrial production with potential applications in cancer therapy and beyond.

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Effect of CHAPS on the selective synthesis of (S)-n-octyl ibuprofen ester in AOT reverse micelle catalyzed by lipase

Chen,

Huang

2024

Journal of Molecular Liquids

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Hydrophobic deep eutectic solvents-lipase synergistically catalyze the synthesis of Vitamin E succinate via hydrogen bonds

Cited by 9 publications

References 55 publications

Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art

Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art

Efficient enzymatic synthesis of vitamin E succinate using an organic solvent‐stable immobilized lipase

Effect of CHAPS on the selective synthesis of (S)-n-octyl ibuprofen ester in AOT reverse micelle catalyzed by lipase

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