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Resolution-Based L-Phenylalanine Synthesis

In contrast to the various fermentation and bioconversion approaches that have used enzyme stereoselectivity to syntlresize L-phenylalanine as a single isomer, additional methods have been developed that rely on the same stereoselectivity to resolve racemic mixtures of chemically synthesized amino acids. One such general approach, which has been successfully commercialized for L-phenylalanine production, relies on cleavage of the L-isomer of a D,L-a-amino acid amide mixture by an enantiospecific amidase enzyme. The general procedure operated [Pg.60]

An earlier strategy involving stereoselective enzyme hydrolysis of chemically prepared racemic precursors has been operated successfully for many years by [Pg.61]

Numerous commercial processes have been developed for the large-scale commercial production of L-phenylalanine since the early 1980s, fueled by the enor- [Pg.63]

Sugimoto, S., Kawamura, K. Agric. Biol. Chem. 1988, 52, 2247. [Pg.64]

Katsumata, R. Appl. Microbiol. Biotechnol. 1993, 39. 318. [Pg.64]


See other pages where Resolution-Based L-Phenylalanine Synthesis is mentioned: [Pg.60]   


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