scholarly journals Bisepoxide-activated Hollow Silica Microspheres for Covalent Immobilization of Lipase from Burkholderia cepacia

2019 ◽  
Author(s):  
Flóra Nagy ◽  
Kinga Szabó ◽  
Péter Bugovics ◽  
Gábor Hornyánszky
Keyword(s):  
Burkholderia Cepacia ◽  
Kinetic Resolution ◽  
Immobilized Lipase ◽  
Covalent Immobilization ◽  
Diglycidyl Ether ◽  
Free Form ◽  
Flow Mode ◽  
Silica Microspheres ◽  
Batch Mode ◽  
Hollow Silica

An efficient and easy-to-perform method was developed for covalent immobilization of lipase from Burkholderia cepacia (Lipase PS) on hollow silica microspheres (M540) by bisepoxide activation. For immobilization, various bisepoxides of different length, rigidity and hydrophobicity in their linkers were applied to activate the amino groups on the M540 support. Effect of the individual bisepoxides on the catalytic performance of the immobilized Lipase PS was studied by using lipase-catalyzed kinetic resolution (KR) of racemic 1-phenylethanol (rac-1) with vinyl acetate in batch mode. Catalytic activity, enantiomer selectivity, recyclability and thermal stability of the new immobilized Lipase PS biocatalysts were investigated. The optimal enzyme / support ratio with the support activated by the most efficient bisepoxide, i.e. poly(ethylene glycol) diglycidyl ether (PDE), was 1:5. The most efficient Lipase PS on PDE activated M540 showed an almost five fold higher biocatalytic activity value (rbatch = 42.8 U/g) with enhanced selectivity (ee(R)-2 = 99.1 %) to the free form of Lipase PS (rbatch = 9.0 U/g; ee(R)-2 = 98.9 %). The Lipase PS on PDE-M540 was compared to a commercially available immobilized Lipase PS biocatalyst (Lipobond Lipase PS) and also applied in a packed-bed enzyme reactor operated in continuous-flow mode, where the optimal temperature of M540-PDE-PS reached the 70 °C, while the optimum for Lipobond Lipase PS was 50 °C.

scholarly journals Lipase B from Candida antarctica Immobilized on Epoxy-functionalized Hollow Silica Microspheres: Efficient Biocatalysts for Enantiomer Selective Acylation of Alcohols and Amines

2018 ◽  
Vol 62 (4) ◽  
Author(s):  
Márk Oláh ◽  
Szandra Suba ◽  
Zoltán Boros ◽  
Péter Kovács ◽  
Mathilde Gosselin ◽  
...  
Keyword(s):  
Continuous Flow ◽  
Kinetic Resolution ◽  
Operation Time ◽  
Candida Antarctica ◽  
Effect Of Temperature ◽  
Flow Mode ◽  
Silica Microspheres ◽  
Lipase B ◽  
Hollow Silica ◽  
Racemic Amines

Hollow silica microspheres with promising physical properties (MAT540TM) as support for enzyme immobilization and biocatalyst were investigated in this study. The amine-functionalized MAT540TM was activated by six bisepoxides inclosing different spacers and used as epoxy-functionalized carrier for immobilization of lipase B from Candida antarctica (CaLB). The novel, covalently fixed CaLB biocatalysts were compared in kinetic resolution (KR) of racemic 1-phenyethanol rac-1 and five racemic amines rac-3a-e using shaken flasks and continuous-flow packed-bed microreactors. Mechanic stability, re-usability and the effect of temperature (0–90 °C) on productivity and enantiomer selectivity of the covalently immobilized CaLB were investigated. The best performing CaLB biocatalyst showed good mechanic stability after 24 h operation time in continuous-flow mode at 60 °C and provided in KRs of racemic 1-phenyethanol rac-1 with vinyl acetate and of five racemic amines with isopropyl 2-ethoxyacetate as acylating agent the non-reacted (S)-alcohol [(S)-1] or (S)-amines [(S)-3a-e] and the forming (R)-ester [(R)-2] or (R)-amide [(R)-4a-e] in good yields with high enantiomeric excess (ee > 99 %, for all).

scholarly journals Tailored sol–gel immobilized lipase preparates for the enzymatic kinetic resolution of heteroaromatic alcohols in batch and continuous flow systems

RSC Advances ◽  
2017 ◽  
Vol 7 (83) ◽  
pp. 52977-52987 ◽  
Author(s):  
Mădălina Elena Moisă ◽  
Cristina Georgiana Spelmezan ◽  
Cristina Paul ◽  
Judith Hajnal Bartha-Vári ◽  
László Csaba Bencze ◽  
...  
Keyword(s):  
Continuous Flow ◽  
Kinetic Resolution ◽  
Immobilized Lipase ◽  
Sol Gel ◽  
Flow Mode ◽  
Batch Mode ◽  
Flow Reactors ◽  
Immobilized Lipases ◽  
Enzymatic Kinetic Resolution ◽  
Continuous Flow Reactors

The EKR of some heteroaromatic secondary ethanols with tailored sol–gel immobilized lipases in batch and continuous-flow reactors was studied. The productivity in continuous-flow mode is higher than in batch mode.

scholarly journals Immobilized Whole-Cell Transaminase Biocatalysts for Continuous-Flow Kinetic Resolution of Amines

Catalysts ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 438 ◽  
Author(s):  
Zsófia Molnár ◽  
Emese Farkas ◽  
Ágnes Lakó ◽  
Balázs Erdélyi ◽  
Wolfgang Kroutil ◽  
...  
Keyword(s):  
Continuous Flow ◽  
Kinetic Resolution ◽  
Sol Gel ◽  
Chiral Amines ◽  
Flow Mode ◽  
Immobilized Cell ◽  
Hollow Silica ◽  
E Coli ◽  
Sol Gel Process ◽  
Racemic Amines

Immobilization of transaminases creates promising biocatalysts for production of chiral amines in batch or continuous-flow mode reactions. E. coli cells containing overexpressed transaminases of various selectivities and hollow silica microspheres as supporting agent were immobilized by an improved sol-gel process to produce immobilized transaminase biocatalysts with suitable stability and mechanical properties for continuous-flow applications. The immobilized cell-based transaminase biocatalyst proved to be durable and easy-to-use in kinetic resolution of four racemic amines 1a–d. The batch and continuous-flow mode kinetic resolutions with transaminase biocatalyst of opposite stereopreference provided access to both enantiomers of the corresponding amines. By using the most suitable immobilized transaminase biocatalysts, this study describes the first transaminase-based approach for the production of both pure enantiomers of 1-(3,4-dimethoxyphenyl)ethan-1-amine 1d.

A mixed-function-grafted magnetic mesoporous hollow silica microsphere immobilized lipase strategy for ultrafast transesterification in a solvent-free system

RSC Advances ◽  
2015 ◽  
Vol 5 (54) ◽  
pp. 43074-43080 ◽  
Author(s):  
Mingming Zheng ◽  
Lijing Mao ◽  
Fenghong Huang ◽  
Xia Xiang ◽  
Qianchun Deng ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Immobilized Lipase ◽  
Solvent Free ◽  
Silica Microspheres ◽  
Silica Microsphere ◽  
Free System ◽  
Hollow Silica ◽  
System P ◽  
Solvent Free System

A novel magnetic mesoporous hollow silica microspheres immobilized lipase is described for ultrafast transesterification of phytosterol with fatty acids and triglycerides in a solvent-free system.

scholarly journals Biocatalysis in continuous-flow mode: A case-study in the enzymatic kinetic resolution of secondary alcohols via acylation and deacylation reactions mediated by Novozym 435®

Biocatalysis ◽  
2017 ◽  
Vol 3 (1) ◽  
Author(s):  
Juliana Christina Thomas ◽  
Martha Daniela Burich ◽  
Pamela Taisline Bandeira ◽  
Alfredo Ricardo Marques de Oliveira ◽  
Leandro Piovan
Keyword(s):  
Continuous Flow ◽  
Energy Use ◽  
Kinetic Resolution ◽  
Enantiomeric Excess ◽  
Flow Mode ◽  
Enzymatic Reactions ◽  
Secondary Alcohols ◽  
Batch Mode ◽  
Enzymatic Kinetic Resolution

AbstractEnzymatic kinetic resolution reactions are a well-established way to achieve optically active compounds. When enzymatic reactions are combined to continuous-flow methodologies, other benefits are added, including reproducibility, optimized energy use, minimized waste generation, among others. In this context, we herein report a case study involving lipase-mediated transesterification by acylation and deacylation reactions of secondary alcohols/esters in batch and continuous-flow modes. Acylation reactions were performed with high values of enantiomeric excess (72 up to >99%) and enantioselectivity (E > 200) for both batch and continuous-flow modes. On the other hand, for deacylation reactions using n-butanol as nucleophile, enatiomeric excess ranged between 38 to >99% and E from 6 to >200 were observed for batch mode. For deacylation reactions in continuous-flow mode, results were disappointing, as in some cases, very low or no conversion was observed. Enantiomeric excess ranged from 16 to >99% and enantioselectivity from 5 to >200 were observed. In terms of productivity, continuous-flow mode reactions were superior in both strategies (acylation: r from 1.1 up to 18.1-fold higher, deacylation: 2.8 up to 7.4- fold higher in continuous-flow than in batch mode).

scholarly journals Covalent immobilization of lipases on activated hollow silica microspheres

2019 ◽  
Vol 64 (2 T1) ◽  
pp. 69-78 ◽  
Author(s):  
Bianka Szokol ◽  
◽  
Gábor Hornyánszky ◽  
József Nagy ◽  
◽  
...  
Keyword(s):  
Covalent Immobilization ◽  
Silica Microspheres ◽  
Hollow Silica

scholarly journals Covalent Immobilization of Lipase in Residual Yerba Mate Stick (Ilex paraguariensis A. St.-Hil.)

2021 ◽  
Vol 11 (6) ◽  
pp. 14564-14579
Keyword(s):  
Thermal Inactivation ◽  
Immobilized Enzyme ◽  
Immobilized Lipase ◽  
Enzyme Characterization ◽  
Covalent Immobilization ◽  
Operational Stability ◽  
Free Form ◽  
Ilex Paraguariensis ◽  
Yerba Mate ◽  
Sodium Metaperiodate

The objective of this study was to immobilize Eversa® Transform 2.0 lipase on residual yerba mate stick. The stick went through an alkaline pre-treatment and different activation treatments (APTS/glutaraldehyde and sodium metaperiodate). Immobilization was performed using hexane solvent and ammonium nitrate buffer. Support characterization, esterification activity, immobilized enzyme characterization, and operational stability were performed. Characterization by SEM demonstrated that the activation treatments were efficient. The immobilization of lipase on APTS/glutaraldehyde activated support showed a yield of 225.52 % and metaperiodate 162.76 %, using hexane as solvent. Good operational stability of the immobilized lipase was observed both in support activated with APTS / glutaraldehyde (8 recycles) and in support activated with metaperiodate (5 recycles), maintaining the activity of 65.62% and 52.00% in concern to the activity initial, respectively. The optimal reaction temperature was 40 ºC for the free and immobilized enzyme. Km and Vmáx values were 16.55 μmol.g-1 and 5555.56 μmol.g-1.min-1 for free enzyme; 33.52 μmol.g-1 and 4761.9 μmol.g-1.min-1 for immobilized enzyme, respectively. The parameters of thermal inactivation confirmed a better thermostability of the lipase in free form.

Investigation of radiofrequency induced release kinetics from magnetic hollow silica microspheres

2012 ◽  
Vol 159 ◽  
pp. 119-125 ◽  
Author(s):  
Pavel Kovačík ◽  
Zuzana Kremláčková ◽  
František Štěpánek
Keyword(s):  
Release Kinetics ◽  
Silica Microspheres ◽  
Hollow Silica
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