Enantioselectivity modulation through immobilization of Arthrobacter sp. lipase: Kinetic resolution of fluoxetine intermediate

摘要: Abstract Arthrobacter sp. lipase (ABL, MTCC no. 5125) has been identified for its excellent performance in kinetic resolution of a number drug intermediates. ABL free enzyme provided product II and V (ee  I IV ) compared to cell biomass naturally immobilized state R isomer ee 99%), was modulated by immobilization using various methods vis-a-vis substrate modification (Scheme 2). Immobilized obtained hydrophobic binding 6710–7720 U/g, covalent 200 U/g, sol–gel entrapment 65–110 U/g activity. Substantial improvement enantioselectivity acylates ethyl 3-hydroxy-3-phenylpropanoate fluoxetine intermediate ( from 93 99% E 43 127–473) at 29–45% conversion fixed time period 21 h, indicating thereby some change conformation enzyme. The demonstrated reasonable superiority over the as well all rate hydrolysis. enzymes prepared have shown operational stability used 10 cycles without loss activity technique can be upscaled process development.