Lipase nanogel catalyzed synthesis of vitamin E succinate in non‐aqueous phase

Xia, Jiaojiao; Zou, Bin; Ruoyu, Zhou; Onyinye, Adesanya Idowu

doi:10.1002/jsfa.10947

Cited by 12 publications

(7 citation statements)

References 31 publications

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“…However, for the products analyzed in this research, the 4 products showed transport potential through the first 3 tunnels located in CALB but with a greater possibility of exit through tunnel 2 (Figure 8) which were α-tocopherol acetate with E max −3.7 kcal/mol and E a 2 kcal/mol, α-ferulate tocopherol with E max −4.7 kcal/mol and E a 1.9 kcal/mol, and α-tocopherol nicotinate with E max −4.7 kcal/mol and E a 1.9 kcal/mol and through tunnel 3 was α-tocopherol succinate with E max −4.8 kcal/mol and E a 1.8 kcal/mol. It is important to note that although α-tocopherol acetate is the most commonly used ester in the pharmaceutical and cosmetic industry, α-tocopherol succinate, α-tocopherol nicotinate, and α-tocopherol ferulate are of fundamental importance for biological studies and biotransformation, as they are also addressed in the literature (Xin et al, 2011;Jiaojiao et al, 2021).…”

Section: Product Transportmentioning

confidence: 99%

“…In 2011, Chunhua et al (2011) also synthesized enzymatically, using Candida antarctica lipase B (Novozym 435), to obtain tocopherol succinate, modifying the biocatalyst to improve its catalytic performance using acetic anhydride, propionic anhydride, and succinic anhydride separately, and with the best modifying agent succinic anhydride (1: 5) yielded 94.4%. Jiaojiao et al (2021) used a nanogel-modified Candida rugosa lipase to obtain vitamin E succinate and obtained a yield of approximately 62% with a reaction time of 15 h. Xin et al (2011), on the other hand, verified the ability of lipases to catalyze through the transesterification reaction of α-tocopherol and ethyl ferulate to obtain tocopherol ferulate, and it can be observed that only Candida antarctica lipase B and Candida rugosa lipase catalyzed the transesterification reaction. A yield of 25.2% tocopherol ferulate was obtained using a 5:1 molar ratio of α-tocopherol to solvent-free ethyl ferulate in 72 h of reaction.…”

Section: Introductionmentioning

confidence: 99%

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In Silico Evaluation of Enzymatic Tunnels in the Biotransformation of α-Tocopherol Esters

Azevedo

Silva

Lima

et al. 2022

Front. Bioeng. Biotechnol.

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Motivation: α-Tocopherol is a molecule obtained primarily from plant sources that are important for the pharmaceutical and cosmetics industry. However, this component has some limitations such as sensitivity to oxygen, presence of light, and high temperatures. For this molecule to become more widely used, it is important to carry out a structural modification so that there is better stability and thus it can carry out its activities. To carry out this structural modification, some modifications are carried out, including the application of biotransformation using enzymes as biocatalysts. Thus, the application of a computational tool that helps in understanding the transport mechanisms of molecules in the tunnels present in the enzymatic structures is of fundamental importance because it promotes a computational screening facilitating bench applications.Objective: The aim of this work was to perform a computational analysis of the biotransformation of α-tocopherol into tocopherol esters, observing the tunnels present in the enzymatic structures as well as the energies which correspond to the transport of molecules.Method: To carry out this work, 9 lipases from different organisms were selected; their structures were analyzed by identifying the tunnels (quantity, conformation, and possibility of transport) and later the calculations of substrate transport for the biotransformation reaction in the identified tunnels were carried out. Additionally, the transport of the product obtained in the reaction through the tunnels was also carried out.Results: In this work, the quantity of existing tunnels in the morphological conformational characteristics in the lipases was verified. Thus, the enzymes with fewer tunnels were RML (3 tunnels), LBC and RNL (4 tunnels), PBLL (5 tunnels), CALB (6 tunnels), HLG (7 tunnels), and LCR and LTL (8 tunnels) and followed by the enzyme LPP with the largest number of tunnels (39 tunnels). However, the enzyme that was most likely to transport substrates in terms of α-tocopherol biotransformation (in relation to the Emax and Ea energies of ligands and products) was CALB, as it obtains conformational and transport characteristics of molecules with a particularity. The most conditions of transport analysis were α-tocopherol tunnel 3 (Emax: −4.6 kcal/mol; Ea: 1.1 kcal/mol), vinyl acetate tunnel 1 (Emax: −2.4 kcal/mol; Ea: 0.1 kcal/mol), and tocopherol acetate tunnel 2 (Emax: −3.7 kcal/mol; Ea: 2 kcal/mol).

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Section: Product Transportmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

In Silico Evaluation of Enzymatic Tunnels in the Biotransformation of α-Tocopherol Esters

Azevedo

Silva

Lima

et al. 2022

Front. Bioeng. Biotechnol.

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“…Among the diverse immobilization approaches, in situ polymerization in the presence of enzymes has been developed as a reliable approach, which creates typically enzyme-loaded nanogels with regulated size and properties. , To do so, monomers need to be introduced on the surface of an enzyme via either chemical binding or physical interaction, followed by the copolymerization with a cross-linker . For example, acryloyl groups have been attached covalently to lysine residues of diverse enzymes such as lipase, − horseradish peroxidase, urate oxidase, carbonic anhydrase, catalase, and glucose oxidase . The subsequent polymerization of acrylamide monomers creates a variety of enzyme nanogels.…”

Section: Introductionmentioning

confidence: 99%

Electrostatically Mediated In Situ Polymerization for Enzyme Immobilization and Activation

Wan,

Zhou,

et al. 2024

Biomacromolecules

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Enzyme immobilization in nanoparticles is of interest for boosting their catalytic applications, yet rational approaches to designs achieving both high enzyme loading and activation remain a challenge. Herein, we report an electrostatically mediated in situ polymerization strategy that simultaneously realizes enzyme immobilization and activation. This was achieved by copolymerizing cationic monomers with a cross-linker in the presence of the enzyme lipase (anionic) as the template, which produces enzyme-loaded nanogels. The effects of different control factors such as pH, lipase dosage, and cross-linker fraction on nanogel formation are investigated systematically, and optimal conditions for enzyme loading and activation have been determined. A central finding is that the cationic polymer network of the nanogel creates a favorable environment that not only protects the enzyme but also boosts enzymatic activity nearly 2-fold as compared to free lipase. The nanogels improve the stability of the lipase to tolerate a broader working range of pH (5.5−8.5) and temperature (25−70 °C) and allow recycling such that after six cycles of reaction, 70% of the initial activity is conserved. The established fabrication strategy can be applied generally to different cationic monomers, and most of these nanogels exhibit adequate immobilization and activation of lipase. Our study confirms that in situ polymerization based on electrostatic interaction provides a facile and robust strategy for enzyme immobilization and activation. The wide variety of ionic monomers, therefore, features great potential for developing functional platforms toward satisfying enzyme immobilization and demanding applications.

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“…Furthermore, with the higher requirements for green chemistry processes in recent years, the synthesis of VES by toxic chemical methods such as triethylamine 7 and 4-dimethylaminepyridine 8 was gradually replaced by green and efficient enzymatic synthesis. 9 Because vitamin E and succinic anhydride are prone to acylation, based on what we know about industrial production, we consider that the yield of VES in industrial production is at least more than 95%. Our previous studies suggested that the yield of VES can only reach 46.95% via the catalytic activity of natural lipase.…”

Section: Introductionmentioning

confidence: 99%

Ionic liquid modification reshapes the substrate pockets of lipase to boost its stability and activity in vitamin E succinate synthesis

Ma,

Zhang,

Chen

et al. 2023

J Sci Food Agric

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BACKGROUNDThe relative low stability, reusability and activity of enzymes made the industrial production of vitamin E succinate (VES) can only be performed with complex processes and high cost using chemical methods. To address these issues, in the present study, an ionic liquids (ILs) modification strategy was developed to improve the activity and stability of lipases in VES synthesis.RESULTSThe results showed that the [1‐butyl‐3‐methyl imidazole] [N‐acetyl‐l‐proline] ILs modified Candida rugosa lipase (CRL) has the highest modification degree (48.28%), activity (774 U g−1), thermostability and solvent tolerance in three selected modifiers. Additionally, after reaction condition optimization, the highest yield of VES can be improved to 95.18% at 45 °C for 15 h, which was significantly improved compared to some previous studies.CONCLUSIONIn the present study, a high‐efficiency VES synthesis strategy was successfully developed via modification of lipase. Moreover, the mechanism by which ILs modification can enhance the activity and stability of lipase was investigated via both experimental and computational‐aided methods. Molecular dynamics simulation suggested that ILs modification changed the geometry of Phe344 from flat to upright, which significantly reshaped and enhanced the size of substrate binding pocket of CRL. It is also agreement with our circular dichroism and fluorescence spectroscopy results, which suggested that the modification changed the secondary structure of CRL to a certain extent. The larger pocket also endowed the suitable binding pose of succinate, which made the hydrogen bonds between succinate and active site Ser209 become stronger, and thus improving the yield of VES. © 2023 Society of Chemical Industry.

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Lipase nanogel catalyzed synthesis of vitamin E succinate in non‐aqueous phase

Cited by 12 publications

References 31 publications

In Silico Evaluation of Enzymatic Tunnels in the Biotransformation of α-Tocopherol Esters

In Silico Evaluation of Enzymatic Tunnels in the Biotransformation of α-Tocopherol Esters

Electrostatically Mediated In Situ Polymerization for Enzyme Immobilization and Activation

Ionic liquid modification reshapes the substrate pockets of lipase to boost its stability and activity in vitamin E succinate synthesis

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