Aminopeptidase activity is related to the amino acids composition of the food in passerine birds

Autores
Garro, Cintia Araceli; Brun, Antonio; Caviedes Vidal, Enrique Juan Raul
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Background. Passerine birds exploit different kinds of feeding habits and they have to face seasonal changes in food availability. Therefore, the composition of the principal nutrient in their food differs from the usual. In consequence the digestive function ? enzyme hydrolysis and absorption ? have to adapt to these nutrients. These changes in digestive physiology could respond to the adaptive modulation hypothesis which postulated that the activities of digestive enzymes should match the levels of their substrates in their diet so energy is not wasted on enzymes that are no need. Thus, we decide to measure intestinal enzymes activities of two species of passerine birds that differ in natural diet. Overall we hypothesized that species with different feeding habits present enzyme activity according to the mainly component of the diet (e.g., carbohydrates, proteins). Our prediction is that the individuals will present enzyme activity proportionally to the primary components of the diets. Methods. We select for study: red ovenbirds (Furnarius rufus), which are strict insectivores and zebra finches (Taeniopygia guttata), which are specialist granivores. We complete the analysis with publish data for house sparrows (Passser domesticus) feed on high starch from the literature. To examine intestinal enzyme activities, we measured the activity of two disaccharidases (sucrase-isomaltase and maltase-glucoamilase) and one dipeptidase (aminopeptidase-N).Results. The average intestinal activity of sucrase shows that the omnivorous P. domesticus presents almost 4 times more activity than the granivorous T. guttata and more than 11 times than the insectivorous F. rufus. This difference is also reflected in the total sucrase hydrolytic capacity where P. domesticus has roughly 10 times more than the other two birds. Surprisingly in F. rufus we found maltase and aminopeptidase activity while sucrase activity was close to zero. In the case of the average activity of maltase for the omnivorous P. domesticus is approximately 40 % more than the granivorous T. guttata and more than 5 times than the insectivorous F. rufus. Although the total maltase hydrolytic capacity of P. domesticus is 5 times more than T. guttata and F. rufus. The average of aminopeptidase-N activity for F. rufus and T. guttata almost doubled the P. domesticus ones. Also F. rufus roughly doubles the other two birds in total aminopeptidase hydrolytic capacity.Discussion. This study has shown that exist a relationship between the levels of amino acids in the diet and the total aminopeptidase capacity, but in the case of carbohydrates this relationship is not evident.
Fil: Garro, Cintia Araceli. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Brun, Antonio. University of Wisconsin; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Caviedes Vidal, Enrique Juan Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Materia
AMINOPEPTIDASE
PASSERINE
BIRDS
AMINO ACIDS
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:11336/67222

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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Aminopeptidase activity is related to the amino acids composition of the food in passerine birdsGarro, Cintia AraceliBrun, AntonioCaviedes Vidal, Enrique Juan RaulAMINOPEPTIDASEPASSERINEBIRDSAMINO ACIDShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Background. Passerine birds exploit different kinds of feeding habits and they have to face seasonal changes in food availability. Therefore, the composition of the principal nutrient in their food differs from the usual. In consequence the digestive function ? enzyme hydrolysis and absorption ? have to adapt to these nutrients. These changes in digestive physiology could respond to the adaptive modulation hypothesis which postulated that the activities of digestive enzymes should match the levels of their substrates in their diet so energy is not wasted on enzymes that are no need. Thus, we decide to measure intestinal enzymes activities of two species of passerine birds that differ in natural diet. Overall we hypothesized that species with different feeding habits present enzyme activity according to the mainly component of the diet (e.g., carbohydrates, proteins). Our prediction is that the individuals will present enzyme activity proportionally to the primary components of the diets. Methods. We select for study: red ovenbirds (Furnarius rufus), which are strict insectivores and zebra finches (Taeniopygia guttata), which are specialist granivores. We complete the analysis with publish data for house sparrows (Passser domesticus) feed on high starch from the literature. To examine intestinal enzyme activities, we measured the activity of two disaccharidases (sucrase-isomaltase and maltase-glucoamilase) and one dipeptidase (aminopeptidase-N).Results. The average intestinal activity of sucrase shows that the omnivorous P. domesticus presents almost 4 times more activity than the granivorous T. guttata and more than 11 times than the insectivorous F. rufus. This difference is also reflected in the total sucrase hydrolytic capacity where P. domesticus has roughly 10 times more than the other two birds. Surprisingly in F. rufus we found maltase and aminopeptidase activity while sucrase activity was close to zero. In the case of the average activity of maltase for the omnivorous P. domesticus is approximately 40 % more than the granivorous T. guttata and more than 5 times than the insectivorous F. rufus. Although the total maltase hydrolytic capacity of P. domesticus is 5 times more than T. guttata and F. rufus. The average of aminopeptidase-N activity for F. rufus and T. guttata almost doubled the P. domesticus ones. Also F. rufus roughly doubles the other two birds in total aminopeptidase hydrolytic capacity.Discussion. This study has shown that exist a relationship between the levels of amino acids in the diet and the total aminopeptidase capacity, but in the case of carbohydrates this relationship is not evident.Fil: Garro, Cintia Araceli. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaFil: Brun, Antonio. University of Wisconsin; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Caviedes Vidal, Enrique Juan Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaPeerJ2017-12info: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/11336/67222Garro, Cintia Araceli; Brun, Antonio; Caviedes Vidal, Enrique Juan Raul; Aminopeptidase activity is related to the amino acids composition of the food in passerine birds; PeerJ; PeerJ Preprints; 5; 12-2017; 1-18; e3443v22167-9843CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.7287/peerj.preprints.3443v2info:eu-repo/semantics/altIdentifier/url/https://peerj.com/preprints/3443/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:58:03Zoai:ri.conicet.gov.ar:11336/67222instacron: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:34982025-09-29 09:58:04.005CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aminopeptidase activity is related to the amino acids composition of the food in passerine birds
title Aminopeptidase activity is related to the amino acids composition of the food in passerine birds
spellingShingle Aminopeptidase activity is related to the amino acids composition of the food in passerine birds
Garro, Cintia Araceli
AMINOPEPTIDASE
PASSERINE
BIRDS
AMINO ACIDS
title_short Aminopeptidase activity is related to the amino acids composition of the food in passerine birds
title_full Aminopeptidase activity is related to the amino acids composition of the food in passerine birds
title_fullStr Aminopeptidase activity is related to the amino acids composition of the food in passerine birds
title_full_unstemmed Aminopeptidase activity is related to the amino acids composition of the food in passerine birds
title_sort Aminopeptidase activity is related to the amino acids composition of the food in passerine birds
dc.creator.none.fl_str_mv Garro, Cintia Araceli
Brun, Antonio
Caviedes Vidal, Enrique Juan Raul
author Garro, Cintia Araceli
author_facet Garro, Cintia Araceli
Brun, Antonio
Caviedes Vidal, Enrique Juan Raul
author_role author
author2 Brun, Antonio
Caviedes Vidal, Enrique Juan Raul
author2_role author
author
dc.subject.none.fl_str_mv AMINOPEPTIDASE
PASSERINE
BIRDS
AMINO ACIDS
topic AMINOPEPTIDASE
PASSERINE
BIRDS
AMINO ACIDS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Background. Passerine birds exploit different kinds of feeding habits and they have to face seasonal changes in food availability. Therefore, the composition of the principal nutrient in their food differs from the usual. In consequence the digestive function ? enzyme hydrolysis and absorption ? have to adapt to these nutrients. These changes in digestive physiology could respond to the adaptive modulation hypothesis which postulated that the activities of digestive enzymes should match the levels of their substrates in their diet so energy is not wasted on enzymes that are no need. Thus, we decide to measure intestinal enzymes activities of two species of passerine birds that differ in natural diet. Overall we hypothesized that species with different feeding habits present enzyme activity according to the mainly component of the diet (e.g., carbohydrates, proteins). Our prediction is that the individuals will present enzyme activity proportionally to the primary components of the diets. Methods. We select for study: red ovenbirds (Furnarius rufus), which are strict insectivores and zebra finches (Taeniopygia guttata), which are specialist granivores. We complete the analysis with publish data for house sparrows (Passser domesticus) feed on high starch from the literature. To examine intestinal enzyme activities, we measured the activity of two disaccharidases (sucrase-isomaltase and maltase-glucoamilase) and one dipeptidase (aminopeptidase-N).Results. The average intestinal activity of sucrase shows that the omnivorous P. domesticus presents almost 4 times more activity than the granivorous T. guttata and more than 11 times than the insectivorous F. rufus. This difference is also reflected in the total sucrase hydrolytic capacity where P. domesticus has roughly 10 times more than the other two birds. Surprisingly in F. rufus we found maltase and aminopeptidase activity while sucrase activity was close to zero. In the case of the average activity of maltase for the omnivorous P. domesticus is approximately 40 % more than the granivorous T. guttata and more than 5 times than the insectivorous F. rufus. Although the total maltase hydrolytic capacity of P. domesticus is 5 times more than T. guttata and F. rufus. The average of aminopeptidase-N activity for F. rufus and T. guttata almost doubled the P. domesticus ones. Also F. rufus roughly doubles the other two birds in total aminopeptidase hydrolytic capacity.Discussion. This study has shown that exist a relationship between the levels of amino acids in the diet and the total aminopeptidase capacity, but in the case of carbohydrates this relationship is not evident.
Fil: Garro, Cintia Araceli. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Brun, Antonio. University of Wisconsin; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Caviedes Vidal, Enrique Juan Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
description Background. Passerine birds exploit different kinds of feeding habits and they have to face seasonal changes in food availability. Therefore, the composition of the principal nutrient in their food differs from the usual. In consequence the digestive function ? enzyme hydrolysis and absorption ? have to adapt to these nutrients. These changes in digestive physiology could respond to the adaptive modulation hypothesis which postulated that the activities of digestive enzymes should match the levels of their substrates in their diet so energy is not wasted on enzymes that are no need. Thus, we decide to measure intestinal enzymes activities of two species of passerine birds that differ in natural diet. Overall we hypothesized that species with different feeding habits present enzyme activity according to the mainly component of the diet (e.g., carbohydrates, proteins). Our prediction is that the individuals will present enzyme activity proportionally to the primary components of the diets. Methods. We select for study: red ovenbirds (Furnarius rufus), which are strict insectivores and zebra finches (Taeniopygia guttata), which are specialist granivores. We complete the analysis with publish data for house sparrows (Passser domesticus) feed on high starch from the literature. To examine intestinal enzyme activities, we measured the activity of two disaccharidases (sucrase-isomaltase and maltase-glucoamilase) and one dipeptidase (aminopeptidase-N).Results. The average intestinal activity of sucrase shows that the omnivorous P. domesticus presents almost 4 times more activity than the granivorous T. guttata and more than 11 times than the insectivorous F. rufus. This difference is also reflected in the total sucrase hydrolytic capacity where P. domesticus has roughly 10 times more than the other two birds. Surprisingly in F. rufus we found maltase and aminopeptidase activity while sucrase activity was close to zero. In the case of the average activity of maltase for the omnivorous P. domesticus is approximately 40 % more than the granivorous T. guttata and more than 5 times than the insectivorous F. rufus. Although the total maltase hydrolytic capacity of P. domesticus is 5 times more than T. guttata and F. rufus. The average of aminopeptidase-N activity for F. rufus and T. guttata almost doubled the P. domesticus ones. Also F. rufus roughly doubles the other two birds in total aminopeptidase hydrolytic capacity.Discussion. This study has shown that exist a relationship between the levels of amino acids in the diet and the total aminopeptidase capacity, but in the case of carbohydrates this relationship is not evident.
publishDate 2017
dc.date.none.fl_str_mv 2017-12
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/11336/67222
Garro, Cintia Araceli; Brun, Antonio; Caviedes Vidal, Enrique Juan Raul; Aminopeptidase activity is related to the amino acids composition of the food in passerine birds; PeerJ; PeerJ Preprints; 5; 12-2017; 1-18; e3443v2
2167-9843
CONICET Digital
CONICET
url http://hdl.handle.net/11336/67222
identifier_str_mv Garro, Cintia Araceli; Brun, Antonio; Caviedes Vidal, Enrique Juan Raul; Aminopeptidase activity is related to the amino acids composition of the food in passerine birds; PeerJ; PeerJ Preprints; 5; 12-2017; 1-18; e3443v2
2167-9843
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/url/https://peerj.com/preprints/3443/
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https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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reponame_str CONICET Digital (CONICET)
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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
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