Abstract
The β-cyclodextrin glycosyltransferase (β-CGTase) from Bacillus circulans STB01 was immobilized on gelatin with an immobilization yield of 100 % and an activity recovery of 23.1 %. Compared with the free β-CGTase, the immobilized exhibited a broader pH optimum with two peaks (pH 5.5 and pH 8.5) as well as significantly enhanced thermostability and pH stability. Immobilized β-CGTase retained 85.5 % of its activity after storage for 50 days at 4 ℃ and 91.9 % of its activity after 20 cycles of enzyme activity assay. β-Cyclodextrin inhibition experiments showed that immobilized β-CGTase was less susceptible to product inhibition than free β-CGTase. As a result, immobilized β-CGTase delivered a 9.7 % increase of product yield in a single use and the total yield after 10 times of use was 9.2-fold of the yield using free enzyme. According to the results, immobilization can greatly improve the utility of β-CGTase as a catalyst for the industrial production of β-cyclodextrin.
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