Aldehydic derivatives of bead cellulose--relationships between matrix structure and function in immobilization of enzymes catalyzing hydrolysis of high molecular substrates.
Benzaldehyde derivatives of bead cellulose (BAC) were prepared and used, in parallel with bead cellulose oxidized by periodate (OC), for trypsin immobilization by reductive alkylation. Influence of pH (range 5-9) on formation and reduction of Schiff base as well as the importance of the reducing agent type-cyanoborohydride or borohydride-were tested. Borohydride reduction was more advantageous at pH 7 and pH 9 for BAC and OC, respectively. Residual activity of trypsin immobilized in this way was evaluated with substrates in the range 435 <or= M(r) <or= 15.4 x 10(4). Results were treated using two equations; one was interpreted via the exclusion principle of gel chromatography. High statistical significance of this treatment made possible an elaboration of criteria for suitability (a) of the matrix for immobilization of enzymes catalyzing hydrolysis of high molecular substrates and (b) of the covalent immobilization method for the given type of enzyme.
Institute of Chemistry, Slovak Academy of Sciences, 842 38 Bratislava, Czechoslovakia.
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