Screening α-glucosidase inhibitor from natural products by capillary electrophoresis with immobilised enzyme onto polymer monolith modified by gold nanoparticles.

A novel strategy for screening ot-glucosidase inhibitors (AGIs) from natural products by capillary electrophoresis (CE) with an immobilised enzyme microreactor was developed. In this approach, gold nanopartides (AuNPs) was first covalently attached to surface of the pores of the porous polymer capillary monolith via the formation of an Au-S bond, and alpha-glucosidase was then simply and stably immobilised onto AuNPs through the strong affinity of gold for amino groups of the enzyme. In order to profiling the activity of the immobilised alpha-glucosidase, the natural substrate was hydrolyzed by it and the yield of product was determined by CE. The amount of covalently attached alpha-glucosidase to the monolith was calculated to be about 30.0 mu g/mg. The immobilised enzyme exhibited 80% activity after 25 runs, and only lost 7.6% of activity after 6 runs within 31 days. Screening of AGIs present in extracts of natural products by the proposed method was demonstrated. (C) 2013 Elsevier Ltd. All rights reserved.