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Covalent binding of enzymes to synthetic membranes containing acrylamide units, using formaldehyde
Author(s) -
Krysteva MA,
Shopova BI,
Yotova LY,
Karasavova MI
Publication year - 1991
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1991.tb00145.x
Subject(s) - membrane , chemistry , acrylamide , invertase , immobilized enzyme , covalent bond , enzyme , trypsin , formaldehyde , reagent , chromatography , biochemistry , organic chemistry , polymer , copolymer
Synthetic membranes containing 10% acrylamide units were subjected to activation with formaldehyde at pH 7.5 and 45 degrees C. Trypsin, invertase, and urease were bound to this activated membrane and the kinetic properties of immobilized enzymes were studied. The permeability of the membrane for distilled water manifests certain differences depending on the enzyme bound. The membranes with immobilized enzymes stored at 4 degrees C in a moist state showed no change in their activity for 6 months. The membrane with immobilized invertase has preserved its activity even after 20 operations with 2% sucrose solution at 25 degrees C. The proposed method of binding enzymes to synthetic membranes containing acrylamide groups, through the introduction of N‐hydroxymethyl groups, possesses several advantages with respect to the activation of the membrane in a one‐step reaction with cheap and accessible reagent, high operative stability of the immobilized enzymes, no danger of bacterial rotting, and long shelf life of the membrane.