Intensified biocatalytic production of enantiomerically pure halophenylalanines from acrylic acids using ammonium carbamate as the ammonia source

Catal. Sci. Technol., 2016, Advance Article
DOI: 10.1039/C6CY00855K, Communication
Nicholas J. Weise, Syed T. Ahmed, Fabio Parmeggiani, Elina Siirola, Ahir Pushpanath, Ursula Schell, Nicholas J. Turner
An industrial-scale method employing a phenylalanine ammonia lyase enzyme

Intensified biocatalytic production of enantiomerically pure halophenylalanines from acrylic acids using ammonium carbamate as the ammonia source

*Corresponding authors
aManchester Institute of Biotechnology & School of Chemistry, University of Manchester, 131 Princess Street, Manchester, UK
E-mail: nicholas.turner@manchester.ac.uk
bJohnson Matthey Catalysts and Chiral Technologies, 28 Cambridge Science Park, Milton Road, Cambridge, UK
Catal. Sci. Technol., 2016, Advance Article

DOI: 10.1039/C6CY00855K

SEE

An intensified, industrially-relevant strategy for the production of enantiopure halophenylalanines has been developed using the novel combination of a cyanobacterial phenylalanine ammonia lyase (PAL) and ammonium carbamate reaction buffer. The process boasts STYs up to >200 g L−1 d−1, ees ≥ 98% and simplified catalyst/reaction buffer preparation and work up.

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///////Intensified,  biocatalytic production, enantiomerically pure,  halophenylalanines,  acrylic acids,  ammonium carbamate, ammonia source

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