Highly enantioselective resolution of β-amino esters by Candida antarctica lipase A immobilized in mesocellular foam: application to dynamic kinetic resolution
2010 (English)In: ChemCatChem, ISSN 1867-3899, Vol. 2, no 5, 534-538 p.Article in journal (Refereed) Published
Candida antarctica lipase A (CALA) immobilized in functionalized mesocellular foam in the presence of sucrose, followed by lyophilization, led to a dramatic increase in the enantioselectivity as well as an improved thermostability of the enzyme. The immobilized lipase was used for kinetic resolution (KR) and dynamic kinetic resolution (DKR) of the β-amino ester, ethyl 3-amino-3-phenylpropanoate. The temperature of optimum activity of CALA shifted from 20–30 °C to 80–90 °C on immobilization in the MCF. An “enantiomeric ratio” E (E=νA/νB; νA and νB are the rate constants for entantiomers A and B) of 69 and a conversion of 43 % in 1 h were obtained at 80 °C, whereas non-immobilized CALA lost its activity at T≥50 °C. The obtained immobilized CALA showed an E value of greater than 500 at 22 °C. Combination of the immobilized CALA with a ruthenium complex, acting as a racemization catalyst, allowed for a successful DKR of ethyl 3-amino-3-phenylpropanoate resulting in 85 % conversion and 89 % ee.
Place, publisher, year, edition, pages
2010. Vol. 2, no 5, 534-538 p.
amino esters, enzyme catalysis, immobilization, kinetic resolution, supported catalysts
IdentifiersURN: urn:nbn:se:su:diva-47405DOI: 10.1002/cctc.201000027OAI: oai:DiVA.org:su-47405DiVA: diva2:373953
FunderEU, FP7, Seventh Framework ProgrammeKnut and Alice Wallenberg Foundation