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摘要
This study aimed to evaluate beta-galactosidase immobilization. For this purpose, the ionic strength of the buffer, reaction time, amount of the immobilization support, and pH were evaluated by a central composite design. Assay 8, which consisted of 1.5 mol L-1 phosphate buffer (pH 7.5) and a reaction time of 2 h, produced the maximum yield. Eupergit (R) C (400 mg) was subsequently used as an immobilization support. Immobilization kinetics wereinvestigated, and a significant increase in the yield was obtained after immobilization compared with that obtained from assay 8 (22.0 U mL(-1) vs. 15.6 U mL(-1)). The enzyme efficiency of actuation was evaluated using o-nitrophenyl-beta-D-galactopyranoside and lactose, with lactose providing better results. The reuse of beta-galactosidase was evaluated, and more than 50% of the initial enzyme activity was maintained after five cycles of use. Enzyme characterization revealed that immobilization improved some aspects of the thermostability of beta-galactosidase.
- 出版日期2014
