Stabilization of enzymes by multipoint covalent immobilization on supports activated with glyoxyl groups

Stabilization of enzymes via immobilization techniques is a valuable approach in order to convert a necessary protocol (immobilization) into a very interesting tool to improve key enzyme properties (stabilization). Multipoint covalent attachment of each immobilized enzyme molecule may promote a very interesting stabilizing effect. The relative distances among all enzyme residues involved in immobilization has to remain unaltered during any conformational change induced by any distorting agent. Amino groups are very interesting nucleophiles placed on protein surfaces. The immobilization of enzyme through the region having the highest amount of amino groups (Lys residues) is key for a successful stabilization. Glyoxyl groups are small aliphatic aldehydes that form very unstable Schiff's bases with amino groups and they do not seem to be useful for enzyme immobilization at neutral pH. However, under alkaline conditions, glyoxyl supports are able to immobilize enzymes via a first multipoint covalent immobilization through the region having the highest amount of Lysine groups. Activation of supports with a high surface density of glyoxyl groups and the performance of very intense enzyme-support multipoint covalent attachments are here described. © Springer Science+Business Media, New York 2013.

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Main Authors: López-Gallego, Fernando, Fernández-Lorente, Gloria, Rocha-Martín, Javier, Bolívar Bolívar, Juan Manuel, Mateo González, César, Guisán, José Manuel
Format: capítulo de libro biblioteca
Published: Humana Press 2013
Subjects:Enzyme stabilization, Over-stabilization of aminated enzymes, Variables that control stabilization,
Online Access:http://hdl.handle.net/10261/100315
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spelling dig-cial-es-10261-1003152020-01-15T09:26:27Z Stabilization of enzymes by multipoint covalent immobilization on supports activated with glyoxyl groups López-Gallego, Fernando Fernández-Lorente, Gloria Rocha-Martín, Javier Bolívar Bolívar, Juan Manuel Mateo González, César Guisán, José Manuel Enzyme stabilization Over-stabilization of aminated enzymes Variables that control stabilization Stabilization of enzymes via immobilization techniques is a valuable approach in order to convert a necessary protocol (immobilization) into a very interesting tool to improve key enzyme properties (stabilization). Multipoint covalent attachment of each immobilized enzyme molecule may promote a very interesting stabilizing effect. The relative distances among all enzyme residues involved in immobilization has to remain unaltered during any conformational change induced by any distorting agent. Amino groups are very interesting nucleophiles placed on protein surfaces. The immobilization of enzyme through the region having the highest amount of amino groups (Lys residues) is key for a successful stabilization. Glyoxyl groups are small aliphatic aldehydes that form very unstable Schiff's bases with amino groups and they do not seem to be useful for enzyme immobilization at neutral pH. However, under alkaline conditions, glyoxyl supports are able to immobilize enzymes via a first multipoint covalent immobilization through the region having the highest amount of Lysine groups. Activation of supports with a high surface density of glyoxyl groups and the performance of very intense enzyme-support multipoint covalent attachments are here described. © Springer Science+Business Media, New York 2013. Peer Reviewed 2014-07-22T07:44:53Z 2014-07-22T07:44:53Z 2013 2014-07-22T07:44:53Z capítulo de libro http://purl.org/coar/resource_type/c_3248 doi: 10.1007/978-1-62703-550-7-5 isbn: 978-1-62703-549-1 Immobilization of Enzymes and Cells (Cap.5): 59-71 (2013) http://hdl.handle.net/10261/100315 10.1007/978-1-62703-550-7-5 Methods in Molecular Biology 1051 none Humana Press
institution CIAL ES
collection DSpace
country España
countrycode ES
component Bibliográfico
access En linea
databasecode dig-cial-es
tag biblioteca
region Europa del Sur
libraryname Biblioteca del CIAL España
topic Enzyme stabilization
Over-stabilization of aminated enzymes
Variables that control stabilization
Enzyme stabilization
Over-stabilization of aminated enzymes
Variables that control stabilization
spellingShingle Enzyme stabilization
Over-stabilization of aminated enzymes
Variables that control stabilization
Enzyme stabilization
Over-stabilization of aminated enzymes
Variables that control stabilization
López-Gallego, Fernando
Fernández-Lorente, Gloria
Rocha-Martín, Javier
Bolívar Bolívar, Juan Manuel
Mateo González, César
Guisán, José Manuel
Stabilization of enzymes by multipoint covalent immobilization on supports activated with glyoxyl groups
description Stabilization of enzymes via immobilization techniques is a valuable approach in order to convert a necessary protocol (immobilization) into a very interesting tool to improve key enzyme properties (stabilization). Multipoint covalent attachment of each immobilized enzyme molecule may promote a very interesting stabilizing effect. The relative distances among all enzyme residues involved in immobilization has to remain unaltered during any conformational change induced by any distorting agent. Amino groups are very interesting nucleophiles placed on protein surfaces. The immobilization of enzyme through the region having the highest amount of amino groups (Lys residues) is key for a successful stabilization. Glyoxyl groups are small aliphatic aldehydes that form very unstable Schiff's bases with amino groups and they do not seem to be useful for enzyme immobilization at neutral pH. However, under alkaline conditions, glyoxyl supports are able to immobilize enzymes via a first multipoint covalent immobilization through the region having the highest amount of Lysine groups. Activation of supports with a high surface density of glyoxyl groups and the performance of very intense enzyme-support multipoint covalent attachments are here described. © Springer Science+Business Media, New York 2013.
format capítulo de libro
topic_facet Enzyme stabilization
Over-stabilization of aminated enzymes
Variables that control stabilization
author López-Gallego, Fernando
Fernández-Lorente, Gloria
Rocha-Martín, Javier
Bolívar Bolívar, Juan Manuel
Mateo González, César
Guisán, José Manuel
author_facet López-Gallego, Fernando
Fernández-Lorente, Gloria
Rocha-Martín, Javier
Bolívar Bolívar, Juan Manuel
Mateo González, César
Guisán, José Manuel
author_sort López-Gallego, Fernando
title Stabilization of enzymes by multipoint covalent immobilization on supports activated with glyoxyl groups
title_short Stabilization of enzymes by multipoint covalent immobilization on supports activated with glyoxyl groups
title_full Stabilization of enzymes by multipoint covalent immobilization on supports activated with glyoxyl groups
title_fullStr Stabilization of enzymes by multipoint covalent immobilization on supports activated with glyoxyl groups
title_full_unstemmed Stabilization of enzymes by multipoint covalent immobilization on supports activated with glyoxyl groups
title_sort stabilization of enzymes by multipoint covalent immobilization on supports activated with glyoxyl groups
publisher Humana Press
publishDate 2013
url http://hdl.handle.net/10261/100315
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