Immobilization of enantioselective lipase on soluble supports for kinetic resolution of drug intermediates
| Autor: | Sarika Deokar, Surendra Ponrathnam, Asha Chaubey, Rajan C. Raman, Subhash C. Taneja, Rajinder Parshad |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Drug
Polymers and Plastics biology Chemistry Arthrobacter sp media_common.quotation_subject N-Vinylpyrrolidone Enantioselective synthesis Bioengineering Microbial lipase Catalysis Kinetic resolution Biomaterials chemistry.chemical_compound Materials Chemistry biology.protein Organic chemistry Lipase media_common |
| Zdroj: | Journal of Bioactive and Compatible Polymers. 27:499-509 |
| ISSN: | 1530-8030 0883-9115 |
| DOI: | 10.1177/0883911512453638 |
| Popis: | The microbial lipase, Arthrobacter sp. lipase (MTCC 5125), from the Indian Institute of Integrative Medicine repository, is known as an effective catalyst for high enantioselective kinetic resolution of drug intermediates. The ABL was immobilized on water-soluble linear supports by covalently binding it to the epoxy groups on the N-vinyl pyrrolidone/allyl glycidyl ether and N-vinyl pyrrolidone/glycidyl methacrylate copolymers. The immobilized lipase, on different soluble supports, had 90–110 mg/g protein binding and 500–700 U/g hydrolysis activities for tributyrin substrate. These copolymers had soluble/insoluble characteristics in different pH ranges, which is an advantage over insoluble copolymers. A soluble polymer at neutral pH provided better accessibility to the immobilized enzyme, which was recovered by precipitation at pH 2–3 for reuse. Kinetic resolution of racemic acyl derivatives of chiral auxiliaries and drug intermediates, namely, phenyl ethanol, aminoalcohol, and fluoxetine intermediate resulted in a significant enhancement in enantioselectivity (99%). |
| Databáze: | OpenAIRE |
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