caa a22 4500 606212655 CHVBK 20210128101043.0 cr unu---uuuuu 210128e20151001xx s 000 0 eng 10.1007/s10295-015-1664-z doi (NATIONALLICENCE)springer-10.1007/s10295-015-1664-z Reduction of l -phenylalanine in protein hydrolysates using l -phenylalanine ammonia-lyase from Rhodosporidium toruloides [Elektronische Daten] [María Castañeda, Osao Adachi, Roque Hours] l-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from Rhodosporidium toruloides was utilized to remove l-phenylalanine (l-Phe) from different commercial protein hydrolysates. A casein acid hydrolysate (CAH, l-Phe~2.28%) was employed as a model substrate. t-Cinnamic acid resulting from deamination of l-Phe was extracted, analyzed at λ=290nm, and used for PAL activity determination. Optimum reaction conditions, optimized using successive Doehlert design, were 35mgmL−1 of CAH and 800mUmL−1 of PAL, while temperature and pH were 42°C and 8.7, respectively. Reaction kinetics of PAL with CAH was determined under optimized conditions. Then, removal of l-Phe from CAH was tested. Results showed that more than 92% of initial l-Phe was eliminated. Similar results were obtained with other protein hydrolysates. These findings demonstrate that PAL is a useful biocatalyst for l-Phe removal from protein hydrolysates, which can be evaluated as potential ingredients in foodstuffs for PKU patients. Society for Industrial Microbiology and Biotechnology, 2015 Phenylketonuria nationallicence Phenylalanine ammonia-lyase nationallicence Rhodosporidium toruloides nationallicence Casein acid hydrolysate nationallicence l -Phe removal nationallicence Castañeda María Research and Development Center for Industrial Fermentations (CINDEFI; UNLP, CONICET La Plata), School of Science, La Plata National University, 47 y 115, B1900ASH, La Plata, Argentina aut Adachi Osao Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, 753-8515, Yamaguchi, Japan aut Hours Roque Research and Development Center for Industrial Fermentations (CINDEFI; UNLP, CONICET La Plata), School of Science, La Plata National University, 47 y 115, B1900ASH, La Plata, Argentina aut Journal of Industrial Microbiology & Biotechnology Springer Berlin Heidelberg 42/10(2015-10-01), 1299-1307 1367-5435 42:10<1299 2015 42 10295 https://doi.org/10.1007/s10295-015-1664-z text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s10295-015-1664-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Castañeda María Research and Development Center for Industrial Fermentations (CINDEFI; UNLP, CONICET La Plata), School of Science, La Plata National University, 47 y 115, B1900ASH, La Plata, Argentina aut NATIONALLICENCE 700 1- Adachi Osao Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, 753-8515, Yamaguchi, Japan aut NATIONALLICENCE 700 1- Hours Roque Research and Development Center for Industrial Fermentations (CINDEFI; UNLP, CONICET La Plata), School of Science, La Plata National University, 47 y 115, B1900ASH, La Plata, Argentina aut NATIONALLICENCE 773 0- Journal of Industrial Microbiology & Biotechnology Springer Berlin Heidelberg 42/10(2015-10-01), 1299-1307 1367-5435 42:10<1299 2015 42 10295