A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives DOI Open Access
Joanna Siódmiak, Jacek Dulęba, Natalia Kocot

et al.

International Journal of Molecular Sciences, Journal Year: 2024, Volume and Issue: 25(10), P. 5084 - 5084

Published: May 7, 2024

The use of lipase immobilized on an octyl-agarose support to obtain the optically pure enantiomers chiral drugs in reactions carried out organic solvents is a great challenge for chemical and pharmaceutical sciences. Therefore, it extremely important develop optimal procedures achieve high enantioselectivity biocatalysts medium. Our paper describes new approach biocatalysis performed solvent with CALB-octyl-agarose including application polypropylene reactor, appropriate buffer immobilization (Tris base-pH 9, 100 mM), drying step, then storage lipases climatic chamber or refrigerator. An B from Candida antarctica (CALB) was used kinetic resolution (R,S)-flurbiprofen by enantioselective esterification methanol, reaching enantiomeric excess (eep = 89.6 ± 2.0%). As part optimization, influence different buffers investigated. effect reactor material reaction medium activity also studied. Moreover, stability lipases: rugosa (CRL) CALB during various temperature humidity conditions (climatic refrigerator) tested. allowed receiving over 9-fold higher conversion values compared results achieved when conducting glass as well approximately 30-fold comparison free lipase. good demonstrated. After 7 days refrigerator (with protection humidity) 60% were obtained observed form that had not been stored. involving indicates significant role polymer being achieving catalytic activity.

Language: Английский

Enzyme loading in the support and medium composition during immobilization alter activity, specificity and stability of octyl agarose-immobilized Eversa Transform DOI Creative Commons
Guilherme J. Sabi,

Leonardo de Souza,

Pedro Abellanas-Pérez

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: 295, P. 139667 - 139667

Published: Jan. 9, 2025

Language: Английский

Citations

1
Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization DOI Creative Commons
Pedro Abellanas-Pérez, Diandra de Andrades, Andrés R. Alcántara

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: 310, P. 143305 - 143305

Published: April 17, 2025

Language: Английский

Citations

0
Support Enzyme Loading Influences the Effect of Aldehyde Dextran Modification on the Specificity of Immobilized Ficin for Large Proteins DOI Creative Commons

El Hocine Siar,

Pedro Abellanas-Pérez, Javier Rocha‐Martín

et al.

Molecules, Journal Year: 2024, Volume and Issue: 29(15), P. 3674 - 3674

Published: Aug. 2, 2024

It has been reported that the modification of immobilized glyoxyl-ficin with aldehyde dextran can promote steric hindrances greatly reduce activity protease against hemoglobin, while still maintained a reasonable level casein. In this paper, we studied if effect may be different depending on amount ficin loaded support. For purpose, both moderately and overloaded biocatalysts were prepared modified dextran. While biocatalyst had significantly reduced activity, mainly was almost maintained. This suggests able to modify areas enzyme not available when overloaded. promoted significant increase in stability for biocatalysts, but higher (perhaps due combination inter- intramolecular crosslinking).

Language: Английский

Citations

1
Silica‐Mediated Incorporation of Lipase Into The Bulk of a Deep Eutectic Solvent: An Efficient Biocatalytic Phase for Esters Synthesis DOI Open Access
Anna Wolny,

Agata Babiuch,

Piotr Latos

et al.

ChemCatChem, Journal Year: 2024, Volume and Issue: unknown

Published: Oct. 17, 2024

Abstract Aiming at sustainable solutions suitable for industrial‐scale catalysis catalytic phase containing lipase and deep eutectic solvent (DES) was designed. To achieve this, both physical chemical immobilizations of lipases were performed on the surface silica carbon materials. The activity developed biosystem tested in biotransformation α‐angelica lactone into butyl levulinate 60 °C. best results achieved Candida antarctica B adsorbed fumed suspended choline chloride: glycerol (1:2) with addition 20 wt% water. Under these conditions 99.9% conversion 100% selectivity to obtained after 45 min. biocatalytic system maintained its up five consecutive reaction cycles full ester. heterogenization enzyme allowed biocatalyst be integrated bulk DES, which includes essential This combination resulted formation a stable easy‐to‐operate where reagents formed second organic phase. integration cost‐effective process efficiency provides greener alternative significant potential industrial use.

Language: Английский

Citations

1
A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives DOI Open Access
Joanna Siódmiak, Jacek Dulęba, Natalia Kocot

et al.

International Journal of Molecular Sciences, Journal Year: 2024, Volume and Issue: 25(10), P. 5084 - 5084

Published: May 7, 2024

The use of lipase immobilized on an octyl-agarose support to obtain the optically pure enantiomers chiral drugs in reactions carried out organic solvents is a great challenge for chemical and pharmaceutical sciences. Therefore, it extremely important develop optimal procedures achieve high enantioselectivity biocatalysts medium. Our paper describes new approach biocatalysis performed solvent with CALB-octyl-agarose including application polypropylene reactor, appropriate buffer immobilization (Tris base-pH 9, 100 mM), drying step, then storage lipases climatic chamber or refrigerator. An B from Candida antarctica (CALB) was used kinetic resolution (R,S)-flurbiprofen by enantioselective esterification methanol, reaching enantiomeric excess (eep = 89.6 ± 2.0%). As part optimization, influence different buffers investigated. effect reactor material reaction medium activity also studied. Moreover, stability lipases: rugosa (CRL) CALB during various temperature humidity conditions (climatic refrigerator) tested. allowed receiving over 9-fold higher conversion values compared results achieved when conducting glass as well approximately 30-fold comparison free lipase. good demonstrated. After 7 days refrigerator (with protection humidity) 60% were obtained observed form that had not been stored. involving indicates significant role polymer being achieving catalytic activity.

Language: Английский

Citations

0