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

PROCESS, spectroscopy, SYNTHESIS

Jun 012016

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

Nicholas J. Weise,^a Syed T. Ahmed,^a Fabio Parmeggiani,^a Elina Siirola,^b Ahir Pushpanath,^b Ursula Schell^b and Nicholas J. Turner*^a

*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

http://pubs.rsc.org/en/Content/ArticleLanding/2016/CY/C6CY00855K?utm_source=feedburner&utm_medium=feed&utm_campaign=Feed%3A+rss%2Fcy+%28RSC+-+Catalysis+Science+%26+Technology+latest+articles%29#!divAbstract

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.