Analysis of Aspergillus sp. lipase immobilization for the application in organic synthesis

Gricajeva, Alisa; Kazlauskas, Simas; Kalėdienė, Lilija; Bendikienė, Vida

doi:10.1016/j.ijbiomac.2017.11.010

Cited by 23 publications

(14 citation statements)

References 66 publications

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“…Organic solvents can reduce the viscosity of the medium in the lipase‐catalyzed reaction to improve the stability of the lipase and the mass transfer of the substrate. And the addition of cosolvents can make up for an absence of sufficient water in maintaining the lipase's active enzyme structure and enhance the activity and enantioselectivity of the lipase 29,30 . The results in Figure 9 demonstrate that compared with the control group that lacked a cosolvent, the addition of 5% (v/v) cosolvent DMSO accelerated the reaction rate to promote the reaction, while other cosolvents barely promoted enzymatic resolution.…”

Section: Resultsmentioning

confidence: 98%

“…And the addition of cosolvents can make up for an absence of sufficient water in maintaining the lipase's active enzyme structure and enhance the activity and enantioselectivity of the lipase. 29,30 The results in Figure 9 demonstrate that compared with the control group that lacked a cosolvent, the addition of 5% (v/v) cosolvent DMSO accelerated the reaction rate to promote the reaction, while other cosolvents barely promoted enzymatic resolution. Thus, cosolvent DMSO was chosen for the succeeding experiments.…”

Section: Effects Of Cosolvent On Enzymatic Resolutionmentioning

confidence: 99%

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A novel lipase from Aspergillus oryzae WZ007 catalyzed synthesis of brivaracetam intermediate and its enzymatic characterization

Zhang

et al. 2020

Chirality

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Brivaracetam is a structural derivative of the chiral drug levetiracetam and has been approved for the adjuvant treatment of partial epilepsy. As a new antiepileptic drug, it is widely used in a variety of epilepsy models. In this study, a novel lipase M16 derived from Aspergillus oryzae WZ007 was cloned, expressed, and used for chiral resolution. Lipase M16 has a high enantioselectivity to the racemic substrate (R,S)-methyl 2-propylsuccinate 4-tert-butyl ester, and the intermediate (R)-2-propylsuccinic acid 4-tert-butyl ester of brivaracetam was obtained efficiently. Under optimal conditions, the enantiomeric excess of substrate was up to 99.26%, and the e.e. p was 96.23%. The conversion and apparent E value were 50.63% and 342.48, respectively. This study suggests a new biocatalytic resolution via lipase M16 for preparing the brivaracetam chiral intermediate and its potential application in the pharmaceutical industry.

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Section: Resultsmentioning

confidence: 98%

Section: Effects Of Cosolvent On Enzymatic Resolutionmentioning

confidence: 99%

A novel lipase from Aspergillus oryzae WZ007 catalyzed synthesis of brivaracetam intermediate and its enzymatic characterization

Zhang

et al. 2020

Chirality

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“…Immobilized lipase from Aspergillus sp. (Resinase A 2X) may also contribute to the synthesis of perfume; it uses a harmless solvent and the product recovery is simple ( Gricajeva et al, 2018 ). A lipase purified immobilized lipase isolated from R. miehei (immobilized on anionic exchange support) have been used as pentyl nonanoate in enhancing fruit aroma ( Muniandy et al, 2019 ).…”

Section: Heterologous Expression and Molecular Modification Of Microbial Lipasesmentioning

confidence: 99%

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Yao

Liu

et al. 2021

Front. Microbiol.

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As a powerful factory, microbial cells produce a variety of enzymes, such as lipase. Lipase has a wide range of actions and participates in multiple reactions, and they can catalyze the hydrolysis of triacylglycerol into its component free fatty acids and glycerol backbone. Lipase exists widely in nature, most prominently in plants, animals and microorganisms, among which microorganisms are the most important source of lipase. Microbial lipases have been adapted for numerous industrial applications due to their substrate specificity, heterogeneous patterns of expression and versatility (i.e., capacity to catalyze reactions at the extremes of pH and temperature as well as in the presence of metal ions and organic solvents). Now they have been introduced into applications involving the production and processing of food, pharmaceutics, paper making, detergents, biodiesel fuels, and so on. In this mini-review, we will focus on the most up-to-date research on microbial lipases and their commercial and industrial applications. We will also discuss and predict future applications of these important technologies.

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“…Hyperactivation after immobilization, especially with lipases, may be associated to enzyme open conformation (more active). 6,29 Besides hydrolysis reaction in aqueous medium, immobilized lipase was employed in ethyl oleate synthesis in nheptane. Primarily, a 2 3 factorial design was used to analyze the effects of temperature, enzyme amount (in total units), and molar ratio (MR) acid:alcohol effect on ester yield (%) in 24 h (Table 1).…”

Section: Lipase Immobilization and Organic Reactionmentioning

confidence: 99%

“…Enzyme recovery allows its reuse as long as its stability lasts, increasing processes' cost effectiveness and taking less time on biocatalysts synthesis. [4][5][6] Different materials have been studied and produced in order to be used as supports to immobilize enzymes. Benucci et al 7 produced supports for stem bromelain immobilization (proteolytic enzyme) based on chitosan and nanoclays films produced by solvent casting.…”

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confidence: 99%

Lipase immobilization on biodegradable film with sericin

Castro

Garcia

Andrade

et al. 2021

Biotech and App Biochem

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An ecofriendly and low‐cost film composed by cassava starch, polyvinyl alcohol, and sericin blend (CS–PVA–SS) was synthesized, characterized, and applied as a novel support for Botryosphaeria ribis EC‐01 lipase immobilization by enzyme–film–enzyme adsorption. Film revealed thickness between 230 and 309 μm and higher flexibility and malleability in comparison with film without SS. Based on p‐nitrophenyl palmitate hydrolysis reaction, the activity retention of immobilized lipase was 987%. For optimal conditions, the yield in ethyl oleate was 95% for immobilized enzyme. Maximum yield was obtained at 49°C, molar ratio oleic acid:ethanol of 1:3, 1.25 g lipase film or 50 U (1.03 ± 0.03 mg protein) and 30 h. Even after seven cycles of use, immobilized lipase showed 52% reduction in ester yield. Biodegradable and biorenewable film is a promising material as a support to immobilize lipases and application in biocatalysis.

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Analysis of Aspergillus sp. lipase immobilization for the application in organic synthesis

Cited by 23 publications

References 66 publications

A novel lipase from Aspergillus oryzae WZ007 catalyzed synthesis of brivaracetam intermediate and its enzymatic characterization

A novel lipase from Aspergillus oryzae WZ007 catalyzed synthesis of brivaracetam intermediate and its enzymatic characterization

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Lipase immobilization on biodegradable film with sericin

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