Reference

Production of L-phenylalanine from phenylpyruvate using resting cells of Escherichia coli

Production of L-phenylalanine from phenylpyruvate using resting cells of Escherichia coli. Then, J.; Doherty, A.; Neatherway, H.; Marquardt, R.; Deger, H. M.; Voelskow, H.; Woehner, G.; Praeve, P. (Hoechst A.-G., Frankfurt/Main 6230, Fed. Rep. Ger.). Biotechnol. Lett., 9(10), 680-4 (English) 1987. CODEN: BILED3. ISSN: 0141-5492. DOCUMENT TYPE: Journal CA Section: 16 (Fermentation and Bioindustrial Chemistry) L-Phenylalanine was produced from phenylpyruvate using resting cells of a genetically modified strain of E. coli. Fermns. were carried out by continuously raising the feeding rate of D-glucose. A biomass of 10 g/L dry wt. and an aminotransferase activity of 14000 U/L were obtained. The max. phenylalanine concn. achieved was 173 mmol/L with a phenylpyruvate molar conversion yield of 95%.

L-Phenylalanine-benzoic acid (1/1)

L-Phenylalanine-benzoic acid (1/1). Suresh, J.; Krishnakumar, R. V.; Natarajan, S. (Department of Physics, The Madura College, Madurai 625 011, India). Acta Crystallographica, Section E: Structure Reports Online, E61(11), o3625-o3627 (English) 2005 Blackwell Publishing Ltd. URL: http://journals.iucr.org/e/issues/2005/11/00/at6033/index.html. CODEN: ACSEBH. ISSN: 1600-5368. DOCUMENT TYPE: Journal; (online computer file) CA Section: 75 (Crystallography and Liquid Crystals) Section cross-reference(s): 25, 34 In the title compd., C9H11NO2×C7H6O2, the amino acid mol. 876953-88-7 is also in the experiment. exists as a zwitterion and the carboxylic acid mol. is in an unionized state. There is a strong O-H×××O intermol. H bond between the phenylalanine and HOBz mols., and these mol. pairs form H-bonded double layers. Crystallog. data are given. .