Reduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from <i>Rhodosporidium toruloides</i>

L-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 resultin...

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Autores principales: Castañeda, María Teresita, Adachi, Osao, Hours, Roque Alberto
Formato: Articulo
Lenguaje:Inglés
Publicado: 2015
Materias:
Ciencias Exactas
Phenylketonuria
Phenylalanine ammonialyase
Rhodosporidium toruloides
Casein acid hydrolysate
L-Phe removal
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/136963
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-136963
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Phenylketonuria
Phenylalanine ammonialyase
Rhodosporidium toruloides
Casein acid hydrolysate
L-Phe removal
spellingShingle Ciencias Exactas
Phenylketonuria
Phenylalanine ammonialyase
Rhodosporidium toruloides
Casein acid hydrolysate
L-Phe removal
Castañeda, María Teresita
Adachi, Osao
Hours, Roque Alberto
Reduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from <i>Rhodosporidium toruloides</i>
topic_facet Ciencias Exactas
Phenylketonuria
Phenylalanine ammonialyase
Rhodosporidium toruloides
Casein acid hydrolysate
L-Phe removal
description L-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.
format Articulo
Articulo
author Castañeda, María Teresita
Adachi, Osao
Hours, Roque Alberto
author_facet Castañeda, María Teresita
Adachi, Osao
Hours, Roque Alberto
author_sort Castañeda, María Teresita
title Reduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from <i>Rhodosporidium toruloides</i>
title_short Reduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from <i>Rhodosporidium toruloides</i>
title_full Reduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from <i>Rhodosporidium toruloides</i>
title_fullStr Reduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from <i>Rhodosporidium toruloides</i>
title_full_unstemmed Reduction of L-phenylalanine in protein hydrolysates using L-phenylalanine ammonia-lyase from <i>Rhodosporidium toruloides</i>
title_sort reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from <i>rhodosporidium toruloides</i>
publishDate 2015
url http://sedici.unlp.edu.ar/handle/10915/136963
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