Abstract
Tannase from Aspergillus niger van Teighem was immobilized on concanavalin A–Sepharose via bioaffinity interaction. The immobilized enzyme showed a pH optimum similar to that of the free enzyme. Km values for free and immobilized enzyme were 0.3 and 0.6 mM respectively. Vmax changed from 0.013 to 0.02 μmol·min−1 upon immobilization. The immobilized preparation was quite stable to reuse, there was no loss of enzyme activity after three cycles and it retained 81% activity even after the sixth cycle. Ester hydrolysis using the immobilized enzyme led to a 40% conversion into gallic acid as compared with 30% obtained with the free enzyme.
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