Abstract
The immobilization process of the enzyme α-amylase, Termamyl® 2X, in ion exchange resin, Duolite® A-568, was studied. First, a Central Composite Design (CCD) evaluated the influence of pH, immobilization time, and enzyme concentration on the activity of the immobilized enzyme (IA) and recovered activity (RA). A second CCD evaluated the influence of glutaraldehyde concentration and the crosslinking time on the responses IA, RA, and immobilization efficiency (Ef). At pH 4.82, 15 min of immobilization time, and an enzyme concentration of 0.878% v/v, the first CCD revealed a better result for IA (77.70U/g of support) than the one obtained from immobilization by crosslinking (35.66U/g of support). At the same time, RA was very similar for both enzyme immobilization processes. The crosslinked immobilized enzyme showed optimal activity at pH 7 and the addition of glutaraldehyde was not so significant for the immobilized biocatalyst.
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