Potential Application of Native Lipases in the Resolution of (RS)-Phenylethylamine

Author(s)

Pilissao, Cristiane ^[1] ; Carvalho, Patricia de O. ^[2] ; Nascimento, Maria da G. ^[1]

Affiliation

^[1] Univ Fed Santa Catarina, Dept Quim, BR-88040900 Florianopolis, SC - Brazil

^[2] Univ Sao Francisco, Curso Farm, BR-12916900 Braganca Paulista, SP - Brazil

• Document type: Journal article
• Source: Journal of the Brazilian Chemical Society; v. 21, n. 6, p. 973-977, 2010.
• Web of Science Citations: 10

Abstract

The performance of two native lipases (lipase from Aspergillus niger and Rhizoupus oligosporus) in the resolution of (RS)-phenylethylamine (1), varying the temperature, acyl donor type (ethyl acetate, vinyl acetate, iso-propenyl acetate and acetic anhydride) and organic medium, was studied. The effect of the nature of the anion using native A. niger lipase in n-heptane with a series of imidazolium-based ILs {[}BMIm]{[}X], where X = BF(4), PF(6), SCN and Cl, was also evaluated. Using the lipase from A. niger, the R-2b amide was obtained with conversions from 6 to > 99% and E-values from 2 to > 200, with n-heptane or n-hexane. This lipase showed better E-values in a two-phase system using n-heptane and {[}BMIm]{[}PF6] or {[}BMIm]{[}BF4] 9: 1 (v/v), obtaining values of 9 and 7, respectively, when vinyl acetate was used as the acyl donor, compared to the use of pure n-heptane (E = 2). The series for the anions in terms of decreasing performance was as follows: PF(6)(-)>BF(4)(-)>SCN->Cl(-). (AU)