期刊
CHEMCATCHEM
卷 2, 期 5, 页码 534-538出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.201000027
关键词
amino esters; enzyme catalysis; immobilization; kinetic resolution; supported catalysts
资金
- Berzelius Center EXSELENT
- European FP7 network INTENANT (Integrated synthesis and purification of single enantiomers)
- K & A Wallenberg foundation
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 beta-amino ester, ethyl 3-amino-3-phenylpropanoate. The temperature of optimum activity of CALA shifted from 20-30 degrees C to 80-90 degrees C on immobilization in the MCF. An enantiomeric ratio E (E=nu(A)/nu(B); nu(A) and vs are the rate constants for entantiomers A and B) of 69 and a conversion of 43% in 1 h were obtained at 80 degrees C, whereas non-immobilized CALA lost its activity at T >= 50 degrees C. The obtained immobilized CALA showed an E value of greater than 500 at 22 degrees 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.
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