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

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          Abstract

          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.

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          Author and article information

          Journal
          Biotechniques
          BioTechniques
          Future Science Ltd
          0736-6205
          0736-6205
          Nov 2004
          : 37
          : 5
          Affiliations
          [1 ] Université de Montréal, Montréal, Canada.
          Article
          10.2144/04375RV01
          15560135
          d7abec5f-e626-4773-8384-9a765d85621b
          History

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