{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,11]],"date-time":"2026-01-11T01:00:53Z","timestamp":1768093253614,"version":"3.49.0"},"reference-count":30,"publisher":"Oxford University Press (OUP)","issue":"10","license":[{"start":{"date-parts":[[2015,10,1]],"date-time":"2015-10-01T00:00:00Z","timestamp":1443657600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"},{"start":{"date-parts":[[2015,10,1]],"date-time":"2015-10-01T00:00:00Z","timestamp":1443657600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2015,10,1]],"date-time":"2015-10-01T00:00:00Z","timestamp":1443657600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"name":"Argentina National Research Council","award":["PIP 0662"],"award-info":[{"award-number":["PIP 0662"]}]},{"name":"Argentina National Technological University","award":["UTN, 25\/I060"],"award-info":[{"award-number":["UTN, 25\/I060"]}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["KAKENHI 23580135"],"award-info":[{"award-number":["KAKENHI 23580135"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,10,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>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\u00a0~2.28\u00a0%) was employed as a model substrate. t-Cinnamic acid resulting from deamination of l-Phe was extracted, analyzed at \u03bb\u00a0=\u00a0290\u00a0nm, and used for PAL activity determination. Optimum reaction conditions, optimized using successive Doehlert design, were 35\u00a0mg\u00a0mL\u22121 of CAH and 800\u00a0mU\u00a0mL\u22121 of PAL, while temperature and pH were 42\u00a0\u00b0C 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\u00a0% 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.<\/jats:p>","DOI":"10.1007\/s10295-015-1664-z","type":"journal-article","created":{"date-parts":[[2015,8,4]],"date-time":"2015-08-04T03:38:55Z","timestamp":1438659535000},"page":"1299-1307","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Reduction of<scp>l<\/scp>-phenylalanine in protein hydrolysates using<scp>l<\/scp>-phenylalanine ammonia-lyase from<i>Rhodosporidium toruloides<\/i>"],"prefix":"10.1093","volume":"42","author":[{"given":"Mar\u00eda Teresita","family":"Casta\u00f1eda","sequence":"first","affiliation":[{"name":"grid.9499.d 0000 0001 2097 3940 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"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Osao","family":"Adachi","sequence":"additional","affiliation":[{"name":"grid.268397.1 0000000106607960 Department of Biological Chemistry, Faculty of Agriculture Yamaguchi University 753-8515 Yamaguchi Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Roque Alberto","family":"Hours","sequence":"additional","affiliation":[{"name":"grid.9499.d 0000 0001 2097 3940 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"},{"name":"Department of Chemical Engineering National Technological University-La Plata Regional Faculty (UTN-FRLP) 60 y 124 La Plata Argentina"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2015,10,1]]},"reference":[{"key":"2021033104115396600_CR1","doi-asserted-by":"publisher","first-page":"2839","DOI":"10.1271\/bbb1961.54.2839","article-title":"Crystallization and properties of l-phenylalanine ammonia-lyase from Rhodosporidium toruloides","volume":"54","author":"Adachi","year":"1990","journal-title":"Agric Biol Chem"},{"key":"2021033104115396600_CR2","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/j.ymgme.2015.03.006","article-title":"Practices in prescribing protein substitutes for PKU in Europe: No uniformity of approach","volume":"115","author":"Aguiar","year":"2015","journal-title":"Mol Genet Metab"},{"key":"2021033104115396600_CR3","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/S0022-3565(25)33522-6","article-title":"In vivo safety of hollow fiber enzyme reactors with immobilized phenylalanine ammonia-lyase in a large animal model for phenylketonuria","volume":"224","author":"Ambrus","year":"1983","journal-title":"J Pharmacol Exp Ther"},{"key":"2021033104115396600_CR4","doi-asserted-by":"publisher","first-page":"531","DOI":"10.7326\/0003-4819-106-4-531","article-title":"Extracorporeal enzyme reactors for depletion of phenylalanine in phenylketonuria","volume":"106","author":"Ambrus","year":"1987","journal-title":"Ann Intern Med"},{"key":"2021033104115396600_CR5","first-page":"58","article-title":"Properties of immobilized phenylalanine ammonia lyase and investigation of its use for prediagnosis of phenylketonuria","volume":"35","author":"Ate\u015f","year":"2010","journal-title":"Turk J Biochem"},{"key":"2021033104115396600_CR6","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.1093\/clinchem\/34.11.2241","article-title":"HPLC measurement of phenylalanine in plasma","volume":"34","author":"Atherton","year":"1988","journal-title":"Clin Chem"},{"key":"2021033104115396600_CR7","first-page":"279","article-title":"Panorama epidemiol\u00f3gico de la fenilcetonuria (PKU) en Latinoam\u00e9rica","volume":"33","author":"Borrajo","year":"2012","journal-title":"Acta Pediatr Mex"},{"key":"2021033104115396600_CR8","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1111\/j.1469-8749.2010.03869.x","article-title":"Neurocognitive function in mild hyperphenylalaninemia","volume":"53","author":"Campistol","year":"2011","journal-title":"Dev Med Child Neurol"},{"key":"2021033104115396600_CR9","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1016\/j.paed.2014.10.006","article-title":"Phenylketonuria","volume":"25","author":"Cleary","year":"2015","journal-title":"Paediatrics and Child Health"},{"key":"2021033104115396600_CR10","doi-asserted-by":"publisher","first-page":"E1249","DOI":"10.1152\/ajpendo.0319.2001","article-title":"Phenylalanine requirement in children with classical PKU determined by indicator amino acid oxidation","volume":"283","author":"Courtney-Martin","year":"2002","journal-title":"Am J Physiol Endocrinol Metab"},{"key":"2021033104115396600_CR11","doi-asserted-by":"publisher","first-page":"231","DOI":"10.2307\/2346327","article-title":"Uniform shell designs","volume":"19","author":"Doehlert","year":"1970","journal-title":"Appl Stat"},{"key":"2021033104115396600_CR12","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/0031-9422(95)00914-0","article-title":"Purification of phenylalanine ammonia lyase from Rhodotorula glutinis","volume":"42","author":"D`Cunha","year":"1996","journal-title":"Phytochemistry"},{"key":"2021033104115396600_CR13","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1542\/peds.2009-3584","article-title":"Challenges and pitfalls in the management of phenylketonuria","volume":"126","author":"Feillet","year":"2010","journal-title":"Pediatrics"},{"key":"2021033104115396600_CR14","doi-asserted-by":"crossref","first-page":"4646","DOI":"10.1016\/S0021-9258(17)33251-9","article-title":"Phenylalanine ammonia-lyase: induction and purification from yeast and clearance in mammals","volume":"251","author":"Fritz","year":"1976","journal-title":"J Biol Chem"},{"key":"2021033104115396600_CR15","doi-asserted-by":"publisher","first-page":"1896","DOI":"10.1021\/bi00845a038","article-title":"l-Phenylalanine ammonia-lyase. I. Purification and molecular size of the enzyme from potato tubers","volume":"7","author":"Havir","year":"1968","journal-title":"Biochemistry"},{"key":"2021033104115396600_CR16","doi-asserted-by":"crossref","first-page":"2977","DOI":"10.1016\/S0021-9258(18)62279-3","article-title":"Yeast phenylalanine ammonia-lyase: purification, properties, and the identification of catalytically essential dehydroalanine","volume":"246","author":"Hodgins","year":"1971","journal-title":"J Biol Chem"},{"key":"2021033104115396600_CR17","doi-asserted-by":"publisher","first-page":"220","DOI":"10.1016\/j.ymthe.2004.05.001","article-title":"Trends in enzyme therapy for phenylketonuria","volume":"10","author":"Kim","year":"2004","journal-title":"Mol Ther"},{"key":"2021033104115396600_CR18","doi-asserted-by":"crossref","first-page":"2692","DOI":"10.1016\/S0021-9258(19)61721-7","article-title":"The metabolism of aromatic compounds in higher plants IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare","volume":"236","author":"Koukol","year":"1961","journal-title":"J Biol Chem"},{"key":"2021033104115396600_CR19","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1016\/S0022-3476(99)70138-1","article-title":"Tetrahydrobiopterin-responsive phenylalanine hydroxilase deficiency","volume":"135","author":"Kure","year":"1999","journal-title":"J Pediatr"},{"key":"2021033104115396600_CR20","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1016\/S0140-6736(13)61841-3","article-title":"Single-dose, subcutaneous recombinant phenylalanine ammonia lyase conjugated with polyethylene glycol in adult patients with phenylketonuria: an open-label, multicentre, phase 1 dose-escalation trial","volume":"384","author":"Longo","year":"2014","journal-title":"Lancet"},{"issue":"1","key":"2021033104115396600_CR21","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1007\/s10545-008-0952-4","article-title":"Nutritional management of PKU with glycomacropeptide from cheese whey","volume":"32","author":"Ney","year":"2009","journal-title":"J Inherit Metab Dis"},{"key":"2021033104115396600_CR22","doi-asserted-by":"publisher","first-page":"311","DOI":"10.1271\/bbb1961.30.311","article-title":"Microbial formation of cinnamic acid from phenylalanine","volume":"30","author":"Ogata","year":"1966","journal-title":"Agric Biol Chem"},{"key":"2021033104115396600_CR23","doi-asserted-by":"publisher","first-page":"200","DOI":"10.1271\/bbb1961.31.200","article-title":"Metabolism of aromatic amino acid in microorganisms: part I. Formation of cinnamic acid from phenylalanine","volume":"31","author":"Ogata","year":"1967","journal-title":"Agric Biol Chem"},{"key":"2021033104115396600_CR24","doi-asserted-by":"publisher","first-page":"20894","DOI":"10.1073\/pnas.0808421105","article-title":"Preclinical evaluation of multiple species of PEGylated recombinant phenylalanine ammonia lyase for the treatment of phenylketonuria","volume":"105","author":"Sarkissian","year":"2008","journal-title":"PNAS"},{"key":"2021033104115396600_CR25","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1111\/1541-4337.12057","article-title":"Strategies used in production of phenylalanine-free foods for PKU management","volume":"13","author":"Soltanizadeh","year":"2014","journal-title":"Compr Rev Food Sci F"},{"key":"2021033104115396600_CR26","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1007\/s10545-010-9216-1","article-title":"Large neutral amino acids in the treatment of PKU: from theory to practice","volume":"33","author":"van Spronsen","year":"2010","journal-title":"J Inherit Metab Dis"},{"key":"2021033104115396600_CR27","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1038\/gim.2013.157","article-title":"Phenylalanine hydroxylase deficiency: diagnosis and management guideline","volume":"16","author":"Vockley","year":"2014","journal-title":"Genet Med"},{"key":"2021033104115396600_CR28","doi-asserted-by":"publisher","first-page":"380","DOI":"10.1104\/pp.98.1.380","article-title":"Phenylalanine ammonia-lyase from loblolly pine: purification of the enzyme and isolation of complementary DNA clones","volume":"98","author":"Whetten","year":"1991","journal-title":"Plant Physiol"},{"key":"2021033104115396600_CR29","first-page":"31","article-title":"Phenylketonuria: an inborn error of phenylalanine metabolism","volume":"29","author":"Williams","year":"2008","journal-title":"Clin Biochem Rev"},{"key":"2021033104115396600_CR30","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1128\/AEM.42.5.773-778.1981","article-title":"Production of l-phenylalanine from trans-cinnamic acid with Rhodotorula glutinis containing l-phenylalanine ammonia-lyase activity","volume":"42","author":"Yamada","year":"1981","journal-title":"Appl Environ Microbiol"}],"container-title":["Journal of Industrial Microbiology and Biotechnology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s10295-015-1664-z.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s10295-015-1664-z\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/academic.oup.com\/jimb\/article-pdf\/42\/10\/1299\/36813001\/jimb1299.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/academic.oup.com\/jimb\/article-pdf\/42\/10\/1299\/36813001\/jimb1299.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s10295-015-1664-z.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,5,29]],"date-time":"2025-05-29T21:29:48Z","timestamp":1748554188000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jimb\/article\/42\/10\/1299\/5995355"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,10,1]]},"references-count":30,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2015,10,1]]}},"URL":"https:\/\/doi.org\/10.1007\/s10295-015-1664-z","relation":{},"ISSN":["1476-5535","1367-5435"],"issn-type":[{"value":"1476-5535","type":"electronic"},{"value":"1367-5435","type":"print"}],"subject":[],"published-other":{"date-parts":[[2015,10,1]]},"published":{"date-parts":[[2015,10,1]]},"assertion":[{"value":"16 February 2015","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"24 July 2015","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 August 2015","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}]}}