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.

Bibliographic Details

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
Tags:	Add Tag No Tags, Be the first to tag this record!