Abstract
Immobilization of α-amylase was carried out by ionic exchange and hydrophobic interactions on gold nanorods (GNRs) synthesized via sequential seed mediated growth method. The optimum temperature of α-amylase increased from 50 to 60°C and its optimum pH was shifted from 6 to 7 upon immobilization. The kinetic parameters, Km and Vmax values were 3mg/ml and 6.4μmmin−1 for free and 3.4mg/ml and 5.91μmmin−1 for immobilized enzymes, respectively. The immobilization process brought significant enhancement of stability to temperature and extreme pH values with respect to free α-amylase. Enzyme shows higher functionality than the free form when incubated for long time (1h) at 80°C and at extreme pH values (3 and 10). In addition to improving thermal stability, the storage stability of α-amylse exhibited a significant increase upon immobilization which makes it a biocatalyst of possible industrial application, specially a potential candidate for production of glucose syrups on industrial scale.
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