Tuning the catalytic properties of lipases immobilized on divinylsulfone activated agarose by altering its nanoenvironment

Santos, José Cleiton Sousa dos; Rueda, Nazzoly; Gonçalves, Luciana Rocha Barros; Fernández‐Lafuente, Roberto

doi:10.1016/j.enzmictec.2015.05.001

Cited by 79 publications

(48 citation statements)

References 68 publications

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“…2). Similar results were found using this lipase and supports activated with divinylsulfone, even although an intense multipoint covalent attachment could be expected using this support [67], [68].…”

Section: Resultssupporting

confidence: 85%

Immobilization of CALB on activated chitosan: Application to enzymatic synthesis in supercritical and near-critical carbon dioxide

Santos

Bonazza

Matos

et al. 2017

Biotechnology Reports

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Section: Resultssupporting

confidence: 85%

Immobilization of CALB on activated chitosan: Application to enzymatic synthesis in supercritical and near-critical carbon dioxide

Santos

Bonazza

Matos

et al. 2017

Biotechnology Reports

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“…Blocking the support after immobilization is convenient to prevent any undesired enzyme‐support reaction. The change in the blocking reagent has been reported to affect enzyme activity and stability . In our case, the change of glycine for EDA did not change the enzyme activity.…”

Section: Resultscontrasting

confidence: 41%

“…The change in the blocking reagent has been reported to affect enzyme activity and stability. 28,[48][49][50] In our case, the change of glycine for EDA did not change the enzyme activity. Thus, the derivative blocked with glycine was also tested for glucose inhibition and thermal stability.…”

Section: β-Glucosidases Immobilizationcontrasting

confidence: 40%

Preparation of immobilized/stabilized biocatalysts of β‐glucosidases from different sources: Importance of the support active groups and the immobilization protocol

Andrades

Graebin

Ayub

et al. 2019

Biotechnology Progress

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β‐Glucosidases from two different commercial preparations, Pectinex Ultra SP‐L and Celluclast® 1.5L, were immobilized on divinylsulfone (DVS) supports at pH 5.0, 7.0, 9.0, and 10. In addition, the biocatalysts were also immobilized in agarose beads activated by glyoxyl, and epoxide as reagent groups. The best immobilization results were observed using higher pH values on DVS‐agarose, and for Celluclast® 1.5L, good results were also obtained using the glyoxil‐agarose immobilization. The biocatalyst obtained using Pectinex Ultra SP‐L showed the highest thermal stability, at 65°C, and an operational stability of 67% of activity after 10 reuses cycles when immobilized on DVS‐agarose immobilized at pH 10 and blocked with ethylenediamine. The β‐glucosidase from Celluclast® 1.5L produced best results when immobilized on DVS‐agarose immobilized at pH 9 and blocked with glycine, reaching 7.76‐fold higher thermal stability compared to its free form and maintaining 76% of its activity after 10 successive cycles. The new biocatalysts obtained by these protocols showed reduction of glucose inhibition of enzymes, demonstrating the influence of immobilization protocols, pH, and blocking agent.

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“…However, detergents may have many effects when working with lipases. They can prevent the formation of lipase‐lipase dimers, have a direct effect on the open‐close equilibrium of the lipase lid, and may induce conformational changes in the structure 3D of the lipase …”

Section: Resultsmentioning

confidence: 99%

Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350

Pinheiro

Rios

Fonseca

et al. 2018

Biotechnology Progress

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Novozyme 435, which is a commercial immobilized lipase B from Candida antarctica (CALB), has been proven to be inadequate for the kinetic resolution of rac-indanyl acetate. As it has been previously described that different immobilization protocols may greatly alter lipase features, in this work, CALB was covalently immobilized on epoxy Immobead-350 (IB-350) and on glyoxyl-agarose to ascertain if better kinetic resolution would result. Afterwards, all CALB biocatalysts were utilized in the hydrolytic resolution of rac-indanyl acetate and rac-(chloromethyl)-2-(o-methoxyphenoxy) ethyl acetate. After optimization of the immobilization protocol on IB-350, its loading capacity was 150 mg protein/g dried support. Furthermore, the CALB-IB-350 thermal and solvent stabilities were higher than that of the soluble enzyme (e.g., by a 14-fold factor at pH 5-70°C and by a 11-fold factor in dioxane 30%-65°C) and that of the glyoxyl-agarose-CALB (e.g., by a 12-fold factor at pH 10-50°C and by a 21-fold factor in dioxane 30%-65°C). The CALB-IB-350 preparation (with 98% immobilization yield and activity versus p-nitrophenyl butyrate of 6.26 ± 0.2 U/g) was used in the hydrolysis of rac-indanyl acetate using a biocatalyst/substrate ratio of 2:1 and a pH value of 7.0 at 30°C for 24 h. The conversion obtained was 48% and the enantiomeric excess of the product (e.e. ) was 97%. These values were much higher than the ones obtained with Novozyme 435, 13% and 26% of conversion and e.e.p, respectively. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 34:878-889, 2018.

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Tuning the catalytic properties of lipases immobilized on divinylsulfone activated agarose by altering its nanoenvironment

Cited by 79 publications

References 68 publications

Immobilization of CALB on activated chitosan: Application to enzymatic synthesis in supercritical and near-critical carbon dioxide

Immobilization of CALB on activated chitosan: Application to enzymatic synthesis in supercritical and near-critical carbon dioxide

Preparation of immobilized/stabilized biocatalysts of β‐glucosidases from different sources: Importance of the support active groups and the immobilization protocol

Kinetic resolution of drug intermediates catalyzed by lipase B from Candida antarctica immobilized on immobead‐350

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