dc.creatorCastañeda, María Teresita
dc.creatorAdachi, Osao
dc.creatorHours, Roque Alberto
dc.date2015-10
dc.date2022-05-27T18:36:36Z
dc.date.accessioned2023-07-15T05:10:53Z
dc.date.available2023-07-15T05:10:53Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/136963
dc.identifierissn:1476-5535
dc.identifierissn:1367-5435
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7472388
dc.descriptionL-Phenylalanine ammonia-lyase (PAL, EC 4.3.1.25) from <i>Rhodosporidium toruloides</i> 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.
dc.descriptionCentro de Investigación y Desarrollo en Fermentaciones Industriales
dc.formatapplication/pdf
dc.format1299-1307
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.rightsCreative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.subjectCiencias Exactas
dc.subjectPhenylketonuria
dc.subjectPhenylalanine ammonialyase
dc.subjectRhodosporidium toruloides
dc.subjectCasein acid hydrolysate
dc.subjectL-Phe removal
dc.titleReduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from <i>Rhodosporidium toruloides</i>
dc.typeArticulo
dc.typeArticulo


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