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《化学科学与工程前沿(英文)》 >> 2008年 第2卷 第2期 doi: 10.1007/s11705-008-0041-0

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

College of Life Science and Pharmacy, Nanjing University of Technology;

发布日期: 2008-06-05

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摘要

L-4-Fluorophenylalanine (FPhe) was prepared from 4-fluorophenylpyruvate (FPPA) catalyzed by aspartate aminotransferase (Asp-AT) of the recombinant 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.

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