Recombinant aspartate aminotransferase-catalyzed synthesis of L-4-fluorophenylalanine

Front. Chem. Sci. Eng. ›› 2008, Vol. 2 ›› Issue (2) : 220 -223.

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Front. Chem. Sci. Eng. ›› 2008, Vol. 2 ›› Issue (2) : 220 -223. DOI: 10.1007/s11705-008-0041-0

Recombinant aspartate aminotransferase-catalyzed synthesis of L-4-fluorophenylalanine

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Abstract

L-4-Fluorophenylalanine (FPhe) was prepared from 4-fluorophenylpyruvate (FPPA) catalyzed by aspartate aminotransferase (Asp-AT) of the recombinant E. coli BL21-pET/aspC. After 12 h enzymatic reaction, the FPPA conversion was over 90% and the yield of FPhe could be above 85% under the following optimal conditions: 37°C, pH value range of 5.0–8.0, 5.5 mass ratio of cell to FPPA, 0.6% (w/v) of Tween 80, 7.08 g/L FPPA, and 1.6 of molar ratio of L-Asp to FPPA.

Keywords

L-4-fluorophenylalanine / 4-fluorophenylpyruvate / aspartate aminotransferase

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null. Recombinant aspartate aminotransferase-catalyzed synthesis of L-4-fluorophenylalanine. Front. Chem. Sci. Eng., 2008, 2(2): 220-223 DOI:10.1007/s11705-008-0041-0

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