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

The precise control of the conditions during support activation with glutaraldehyde has enabled the modification of the amino groups of the matrix with one or two glutaraldehyde molecules. Moreover, the use of aminated supports implies that below each glutaraldehyde molecule, there are amino groups...

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Podrobná bibliografie
Vydáno v:	Enzyme and microbial technology Ročník 39; číslo 4; s. 877 - 882
Hlavní autoři:	Betancor, Lorena, López-Gallego, Fernando, Hidalgo, Aurelio, Alonso-Morales, Noelia, Mateo, Gisela Dellamora-Ortiz Cesar, Fernández-Lafuente, Roberto, Guisán, Jose M.
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Amsterdam Elsevier Inc 01.08.2006 Elsevier Science
Témata:	Biological and medical sciences Biotechnology Covalent immobilization of proteins Fundamental and applied biological sciences. Psychology Glutaraldehyde Hetero-functional supports Physical adsorption of proteins Protein stabilization Physical adsorption of proteins Glutaraldehyde Hetero-functional supports Covalent immobilization of proteins Protein stabilization Support Stabilization Immobilization Activation Glutaral Mechanism Protein Adsorption Covalent bond
ISSN:	0141-0229, 1879-0909
On-line přístup:	Získat plný text
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Popis
Shrnutí:	The precise control of the conditions during support activation with glutaraldehyde has enabled the modification of the amino groups of the matrix with one or two glutaraldehyde molecules. Moreover, the use of aminated supports implies that below each glutaraldehyde molecule, there are amino groups and, therefore, these supports could be considered as heterofunctional matrices; an anion exchanger bearing glutaraldehyde groups for covalent immobilization. Thus, by using several enzymes as models, it has been found that at low ionic strength the protein immobilization on glutaraldehyde activated supports proceeds via a first ionic interchange of the protein on the amino groups of the support, followed by the covalent reaction. Moreover, the dimeric form of glutaraldehyde seems to be much more reactive than its monomeric counterpart, permitting the immobilization of proteins even at very high ionic strength. Although in all cases the immobilization of the enzymes on both monomer and dimeric matrices promoted a significant increment in the enzyme stability, it was found that the stabilization depends on the degree of activation (monomer or dimer), and it is necessary to analyze each individual enzyme before selecting any of the immobilization protocols.
Bibliografie:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23
ISSN:	0141-0229 1879-0909
DOI:	10.1016/j.enzmictec.2006.01.014