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

Autores
Castañeda, María Teresita; Adachi, Osao; Hours, Roque Alberto
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 = 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.
Fil: Castañeda, María Teresita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
Fil: Adachi, Osao. Yamaguchi University; Japón
Fil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina. Universidad Tecnológica Nacional; Argentina
Materia
Casein Acid Hydrolysate
L-Phe Removal
Phenylalanine Ammonia-Lyase
Phenylketonuria
Rhodosporidium Toruloides
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/49508
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/49508
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloidesCastañeda, María TeresitaAdachi, OsaoHours, Roque AlbertoCasein Acid HydrolysateL-Phe RemovalPhenylalanine Ammonia-LyasePhenylketonuriaRhodosporidium Toruloideshttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2l-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.Fil: Castañeda, María Teresita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; ArgentinaFil: Adachi, Osao. Yamaguchi University; JapónFil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina. Universidad Tecnológica Nacional; ArgentinaSpringer Heidelberg2015-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/49508Castañeda, María Teresita; Adachi, Osao; Hours, Roque Alberto; Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides; Springer Heidelberg; Journal of Industrial Microbiology & Biotechnology; 42; 10; 10-2015; 1299-13071367-5435CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s10295-015-1664-zinfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10295-015-1664-zinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:11:24Zoai:ri.conicet.gov.ar:11336/49508instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:11:24.777CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides
title Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides
spellingShingle Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides
Castañeda, María Teresita
Casein Acid Hydrolysate
L-Phe Removal
Phenylalanine Ammonia-Lyase
Phenylketonuria
Rhodosporidium Toruloides
title_short Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides
title_full Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides
title_fullStr Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides
title_full_unstemmed Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides
title_sort Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides
dc.creator.none.fl_str_mv Castañeda, María Teresita
Adachi, Osao
Hours, Roque Alberto
author Castañeda, María Teresita
author_facet Castañeda, María Teresita
Adachi, Osao
Hours, Roque Alberto
author_role author
author2 Adachi, Osao
Hours, Roque Alberto
author2_role author
author
dc.subject.none.fl_str_mv Casein Acid Hydrolysate
L-Phe Removal
Phenylalanine Ammonia-Lyase
Phenylketonuria
Rhodosporidium Toruloides
topic Casein Acid Hydrolysate
L-Phe Removal
Phenylalanine Ammonia-Lyase
Phenylketonuria
Rhodosporidium Toruloides
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv 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 = 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.
Fil: Castañeda, María Teresita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
Fil: Adachi, Osao. Yamaguchi University; Japón
Fil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina. Universidad Tecnológica Nacional; Argentina
description 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 = 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.
publishDate 2015
dc.date.none.fl_str_mv 2015-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/49508
Castañeda, María Teresita; Adachi, Osao; Hours, Roque Alberto; Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides; Springer Heidelberg; Journal of Industrial Microbiology & Biotechnology; 42; 10; 10-2015; 1299-1307
1367-5435
CONICET Digital
CONICET
url http://hdl.handle.net/11336/49508
identifier_str_mv Castañeda, María Teresita; Adachi, Osao; Hours, Roque Alberto; Reduction of l-phenylalanine in protein hydrolysates using l-phenylalanine ammonia-lyase from Rhodosporidium toruloides; Springer Heidelberg; Journal of Industrial Microbiology & Biotechnology; 42; 10; 10-2015; 1299-1307
1367-5435
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s10295-015-1664-z
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10295-015-1664-z
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer Heidelberg
publisher.none.fl_str_mv Springer Heidelberg
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842270156800131072
score 13.13397

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