Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking.

By Isabelle Migneault, C. Dartiguenave, M. Bertrand, K. Waldron. BioTechniques, 2004

1,622 citations recorded by the source corpus.

Glutaraldehyde possesses unique characteristics that render it one of the most effective protein crosslinking reagents. It can be present in at least 13 different forms depending on solution conditions such as pH, concentration, temperature, etc. Substantial literature is found concerning the use of glutaraldehyde for protein immobilization, yet there is no agreement about the main reactive species that participates in the crosslinking process because monomeric and polymeric forms are in equilibrium. Glutaraldehyde may react with proteins by several means such as aldol condensation or Michael-type addition, and we show here 8 different reactions for various aqueous forms of this reagent. As a result of these discrepancies and the unique characteristics of each enzyme, crosslinking procedures using glutaraldehyde are largely developed through empirical observation. The choice of the enzyme-glutaraldehyde ratio, as well as their final concentration, is critical because insolubilization of the enzyme must result in minimal distortion of its structure in order to retain catalytic activity. The purpose of this paper is to give an overview of glutaraldehyde as a crosslinking reagent by describing its structure and chemical properties in aqueous solution in an attempt to explain its high reactivity toward proteins, particularly as applied to the production of insoluble enzymes.

Subfields: Biomaterials, Biotechnology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/0a4181bf70a09c466d291fff56ccecd9da43a92b

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In Biotechnology

R. Fernández-Lafuente

In Molecular Biology

Citations in the corpus

Revisit of reconstituted 30-nm nucleosome arrays reveals an ensemble of dynamic structures (2018, background): “Chemical cross-linking occurs when the C=O groups of glutaraldehyde (O=CH-CH2-CH2CH2-HC=O) react with the primary amine and guanidine groups of the side chains of Lys and Arg residues [33].”
An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes (2015, neutral): “[82] [83] Cross-linked enzyme aggregates (CLEAs) are first prepared by aggregating the enzymes in precipitants such as acetone, ammonium sulphate and ethanol followed by a cross-linker,[57] and the reactions for enzyme immobilization can be executed in three different manners; either by mixing the…”
Improvement of enzyme activity, stability and selectivity via immobilization techniques (2007, methodology): “The glutaraldehyde technique is very versatile and ay be used in very different fashions [37–39].”
Immobilized Enzymes in Biosensor Applications (2019, positive): “Glutaraldehyde has been used for decades in protein cross-linking [165].”