Abstract
Immobilization of invertase on cross-linked polymers consisting of cellulose and polyethyleneimine (Cell-PEI) and the enzymic activity of immobilized invertase were investigated. Invertase was coupled with Cell-PEI by glutalaldehyde. The amount of invertase coupled was independent of reaction temperature and increased with an increase in invertase concentration. Neutral or weak basic conditions were favorable for the coupling reaction.
The optimum pH of invertase activity was shifted to acidic side by the immobilization. The activity at the optimum pH was 26% of that of native invertase. The optimum temperature of invertase activity was little affected by the immobilization. The immobilized invertase was repeatedly used without the activity loss.
