Journal ArticleDOI
Optimization of glutaraldehyde activation of a support for enzyme immobilization
TLDR
In this article, the activation of an amine porous silica with glutaraldehyde has been studied and compared with the capacity of the activated silica to bind trypsin, based on a reaction mechanism with a polymeric form resulting from aldol condensation.About:
This article is published in Journal of Molecular Catalysis.The article was published on 1978-02-01. It has received 177 citations till now. The article focuses on the topics: Glutaraldehyde & Immobilized enzyme.read more
Citations
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Journal ArticleDOI
Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization
Oveimar Barbosa,Claudia Ortiz,Ángel Berenguer-Murcia,Rodrigo Torres,Rafael C. Rodrigues,Roberto Fernandez-Lafuente +5 more
TL;DR: Glutaraldehyde, an apparently old fashioned reactive, remains the most widely used and with broadest application possibilities among the compounds used for the design of biocatalyst.
Journal ArticleDOI
Some studies of crosslinking chitosan-glutaraldehyde interaction in a homogeneous system.
TL;DR: In this article, a chitosan:glutaraldehyde molar proportion of 1:20 was established for a CHITOSAN:GLUTARaldehyde mixture.
Journal ArticleDOI
Importance of the Support Properties for Immobilization or Purification of Enzymes
José C. S. dos Santos,José C. S. dos Santos,Oveimar Barbosa,Claudia Ortiz,Ángel Berenguer-Murcia,Rafael C. Rodrigues,Roberto Fernandez-Lafuente +6 more
TL;DR: This review will focus its attention on the requirements of a support surface to produce the desired objectives, the ideal physical properties of the matrix, the properties ofThe introduced reactive groups, the best surface activation degree to reach the desired objective, and the Properties of the reactive groups will be discussed.
Journal ArticleDOI
Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties.
Oveimar Barbosa,Rodrigo Torres,Claudia Ortiz,Ángel Berenguer-Murcia,Rafael C. Rodrigues,Roberto Fernandez-Lafuente +5 more
TL;DR: This Review will discuss the suitable properties of the groups able to give the covalent attachment, and the groups unable to produce the first enzyme adsorption on the support, as well as the likely pathways for the evolution.
Journal ArticleDOI
Different mechanisms of protein immobilization on glutaraldehyde activated supports: Effect of support activation and immobilization conditions
Lorena Betancor,Fernando López-Gallego,Aurelio Hidalgo,Noelia Alonso-Morales,Gisela Dellamora-Ortiz Cesar Mateo,Roberto Fernandez-Lafuente,Jose M. Guisan +6 more
TL;DR: The immobilization of the enzymes on both monomer and dimeric matrices promoted a significant increment in the enzyme stability, but 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.
References
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Journal ArticleDOI
Étude du mécanisme d'établissement des liaisons glutaraldéhyde-protéines
TL;DR: In this article, the effect of pH on the reaction of glutaraldehyde with amino acids and on the stability of the products under acid conditions, shows the importance of the structure modification of the dialdehyde which occurs when pH increases, and even leads to precipitation in highly alkaline solutions.
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Glutaraldehyde: nature of the reagent.
TL;DR: Three unstable products can be partially isolated from acid hydrolyzates of glutaraldehyde-treated proteins or from the reaction mixtures of glutARaldehyde and model compounds; two of these products have strong ultraviolet absorption near 265 nm.
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Simultaneously immobilized glucose oxidase and catalase in controlled‐pore titania
TL;DR: The immobilization of glucose oxidase and catalase by adsorption within the pores of controlled‐pore titania has yielded a remarkably stable enzyme system.