Different mechanisms of protein immobilization on glutaraldehyde activated supports: Effect of support activation and immobilization conditions

Betancor, Lorena; López‐Gallego, Fernando; Hidalgo, Aurélio; Alonso-Morales, Noelia; Mateo, Gisela Dellamora-Ortiz Cesar; Fernández‐Lafuente, Roberto; Guisán, José M.

doi:10.1016/j.enzmictec.2006.01.014

Cited by 377 publications

(270 citation statements)

References 20 publications

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“…Furthermore, the support modification with APTS and glutaraldehyde facilitated the rapid binding of the enzyme by covalent interactions between the aldehyde group of glutaraldehyde and the amine groups of the enzyme. A high concentration of aldehyde groups on the support surface may cause many multi-point covalent enzyme-support bonds, so as to obtain rigidity in the structure of the enzyme, favoring a high stability and a high intrinsic activity of the derivative (Betancor, et al, 2006). Hu et al (2009) reported that Serratia marcescens lipase was almost fully immobilized onto aldehydefuncionalized-APTES magnetic nanoparticles within 10 min.…”

Section: Effect Of the Contact Timementioning

confidence: 99%

NANOBIOCATALYTIC SYSTEMS BASED ON LIPASE-Fe3O4 AND CONVENTIONAL SYSTEMS FOR ISONIAZID SYNTHESIS: A COMPARATIVE STUDY

Costa

Souza

Fechine

et al. 2016

Braz. J. Chem. Eng.

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-Superparamagnetic nanomaterials have attracted interest in many areas due to the high saturation magnetization and surface area. For enzyme immobilization, these properties favor the enzyme-support contact during the immobilization reaction and easy separation from the reaction mixture by use of low-cost magnetic processes. Iron oxide magnetic nanoparticles (Fe3O4, MNPs), produced by the co-precipitation method, functionalized with 3-aminopropyltriethoxysilane (APTES) and glutaraldehyde (GLU), were evaluated as a solid support for Candida antarctica lipase B (CALB) immobilization. The nanomagnetic derivative (11nm) obtained after CALB immobilization (MNPs/APTES/GLU/CALB) was evaluated as biocatalyst in isoniazide (INH) synthesis using ethyl isonicotinate (INE) and hydrazine hydrate (HID) as substrates, in 1,4-dioxane. The results showed that MNPs/APTES/CALB had a similar performance when compared to a commercial enzyme Novozym 435, showing significant advantages over other biocatalysts, such as Rhizhomucor miehei lipase (RML) and CALB immobilized on non-conventional, low-cost, chitosan-based supports.

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Section: Effect Of the Contact Timementioning

confidence: 99%

NANOBIOCATALYTIC SYSTEMS BASED ON LIPASE-Fe3O4 AND CONVENTIONAL SYSTEMS FOR ISONIAZID SYNTHESIS: A COMPARATIVE STUDY

Costa

Souza

Fechine

et al. 2016

Braz. J. Chem. Eng.

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“…A dimer GLD form enables fast protein immobilization as compared to its monomer counterpart. 104 In a low ionic medium, immobilization proceeds via ionic exchange with the amino groups on the support followed by the covalent attachment. In a high ionic medium, the biomolecule is directly immobilized by covalent bonding with slower immobilization kinetics.…”

Section: Covalentmentioning

confidence: 99%

Immobilization of Antibodies and Enzymes on 3-Aminopropyltriethoxysilane-Functionalized Bioanalytical Platforms for Biosensors and Diagnostics

et al. 2014

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/npsi/ctrl?lang=en http://nparc.cisti-icist.nrc-cnrc.gc.ca/npsi/ctrl?lang=fr READ THESE TERMS AND CONDITIONS CAREFULLY BEFORE USING THIS WEBSITE.http://nparc.cisti-icist.nrc-cnrc.gc.ca/npsi/jsp/nparc_cp.jsp?lang=en Vous avez des questions? Nous pouvons vous aider. Pour communiquer directement avec un auteur, consultez la première page de la revue dans laquelle son article a été publié afin de trouver ses coordonnées. Si vous n'arrivez pas à les repérer, communiquez avec nous à PublicationsArchive-ArchivesPublications@nrc-cnrc.gc.ca.

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“…Incubation of the immobilized enzymes at pH 7 or 9 after 24 h in 500 mM NaCl/25 mM sodium phosphate produced the full release of the enzyme immobilized on MANAE-agarose [37,38], but all enzyme molecules remained immobilized on the glutaraldehyde preparations, showing the success of getting a covalent immobilization. Finally, we tried to get the direct covalent immobilization of the enzyme on the support [19,22]. In this case, the immobilization will proceed by the most reactive primary amino group, and the main effect of the pH is to control the protein reactivity, which should increase using a higher pH value, but at pH over 8 this effect is detrimental for the glutaraldehyde groups stability [24].…”

Section: Immobilization Of β-Gal On Glutaraldehyde Pre-activated Suppmentioning

confidence: 99%

Exploiting the Versatility of Aminated Supports Activated with Glutaraldehyde to Immobilize β-galactosidase from Aspergillus oryzae

et al. 2017

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Abstract:The enzyme β-galactosidase from Aspergillus oryzae has been immobilized in aminated (MANAE)-agarose beads via glutaraldehyde chemistry using different strategies. The immobilization on MANAE-supports was first assayed at different pH values (this gave different stabilities to the immobilized enzymes) and further modified with glutaraldehyde. Dramatic drops in activity were found, even using 0.1% (v/v) glutaraldehyde. The use of a support with lower activation permitted to get a final activity of 30%, but stability was almost identical to that of the just adsorbed enzyme. Next, the immobilization on pre-activated glutaraldehyde beads was assayed at pH 5, 7 and 9. At pH 7, full, rapid immobilization and a high expressed enzyme activity were accomplished. At pH 9, some decrease in enzyme activity was observed. Direct covalent immobilization of the enzyme was very slow; even reducing the volume of enzyme/support ratio, the yield was not complete after 24 h. The stability of the biocatalyst using pre-activated supports was about 4-6 folds more stable than that of the enzyme immobilized via ion exchange at pH 5, with small differences among them. Thus, the immobilization of the enzyme at pH 7 at low ionic strength on pre-activated glutaraldehyde supports seems to be the most adequate in terms of activity, stability and immobilization rate.

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Different mechanisms of protein immobilization on glutaraldehyde activated supports: Effect of support activation and immobilization conditions

Cited by 377 publications

References 20 publications

NANOBIOCATALYTIC SYSTEMS BASED ON LIPASE-Fe3O4 AND CONVENTIONAL SYSTEMS FOR ISONIAZID SYNTHESIS: A COMPARATIVE STUDY

NANOBIOCATALYTIC SYSTEMS BASED ON LIPASE-Fe3O4 AND CONVENTIONAL SYSTEMS FOR ISONIAZID SYNTHESIS: A COMPARATIVE STUDY

Immobilization of Antibodies and Enzymes on 3-Aminopropyltriethoxysilane-Functionalized Bioanalytical Platforms for Biosensors and Diagnostics

Exploiting the Versatility of Aminated Supports Activated with Glutaraldehyde to Immobilize β-galactosidase from Aspergillus oryzae

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