Factors influencing covalent coupling of enzymes on derivatized polyacrylamide gel beads: A survey

B. Szajáni, L. Boross

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Several enzymes (aldolase, aminoacylase, arginase, carboxypeptidase B, cholinesterase, cyclodextrin glycosyltransferase and glucoamylase) were immobilized by covalent coupling on polyacrylamide bead polymers possessing carboxylic functional groups activated by water-soluble carbodiimides. The factors influencing the immobilization process were studied. The catalytic activities of the immobilized enzymes were influenced advantageously by the structure of carbodiimide used as coupling agent. Immobilized enzymes of highest catalytic activity could be obtained if the carbodiimide was introduced into the reaction mixture in a stoichiometric quantity relative to the carboxylic functional groups located on the support and the support/protein ratio was from 1:0.25 to 1:1. It was found that the hydrogen ion concentration of the coupling reaction mixture has a profound effect on the immobilization of enzymes. In the function of the ionic strength of coupling reaction mixture, the catalytic activity of immobilized enzyme produced showed an apparent optimum. The increasing porosity of support was favourable for the immobilization of enzymes. The insertion of a spacer in the support appeared to be disadvantageous for the enzyme immobilization.

Original languageEnglish
Pages (from-to)125-130
Number of pages6
JournalHungarian Journal of Industrial Chemistry
Volume27
Issue number2
Publication statusPublished - Jan 1 1999

ASJC Scopus subject areas

  • Chemistry (miscellaneous)
  • Chemistry(all)
  • Chemical Engineering(all)

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