Reduction of l‑phenylalanine in protein hydrolysates using l‑phenylalanine ammonia‑lyase from Rhodosporidium toruloides

cic.lugarDesarrolloCentro de Investigación y Desarrollo en Fermentaciones Industrialeses
cic.lugarDesarrolloUniversidad Nacional de La Plataes
cic.versioninfo:eu-repo/semantics/publishedVersiones
dc.date.accessioned2018-05-18T02:20:48Z
dc.date.available2018-05-18T02:20:48Z
dc.identifier.urihttps://digital.cic.gba.gob.ar/handle/11746/7750
dc.titleReduction of l‑phenylalanine in protein hydrolysates using l‑phenylalanine ammonia‑lyase from Rhodosporidium toruloidesen
dc.typeArtículoes
dcterms.abstractl-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 = 290 nm, and used for PAL activity determination. Optimum reaction conditions, optimized using successive Doehlert design, were 35 mg mL-1 of CAH and 800 mU mL-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.es
dcterms.creator.authorCastañeda, María Teresitaes
dcterms.creator.authorAdachi, Osaoes
dcterms.creator.authorHours, Roque A.es
dcterms.extent9 p.es
dcterms.identifier.otherDOI:10.1007/s10295-015-1664-zes
dcterms.identifier.urlRecurso Completoes
dcterms.isPartOf.issuevol. 42, no.10es
dcterms.isPartOf.seriesJournal of Industrial Microbiology and Biotechnologyes
dcterms.issued2015-08-05
dcterms.languageIngléses
dcterms.licenseAttribution-NonCommercial-NoDerivatives 4.0 International (BY-NC-ND 4.0)es
dcterms.subjectPhenylketonuriaen
dcterms.subjectPhenylalanine ammonialyaseen
dcterms.subjectRhodosporidium toruloidesen
dcterms.subjectCasein acid hydrolysateen
dcterms.subjectl-Phe removalen
dcterms.subject.materiaCiencias Químicases

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