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dc.contributor.author
Toledo Solís, Francisco Javier
dc.contributor.author
Hilerio Ruiz, Andrea Guadalupe
dc.contributor.author
Delgadin, Tomás Horacio
dc.contributor.author
Pérez Sirkin, Daniela Irina
dc.contributor.author
Di Yorio, María Paula
dc.contributor.author
Vissio, Paula Gabriela
dc.contributor.author
Peña Marín, Emyr Saul
dc.contributor.author
Martínez García, Rafael
dc.contributor.author
Maytorena Verdugo, Claudia Ivette
dc.contributor.author
Alvarez González, Carlos Alfonso
dc.contributor.author
de Rodrigáñez, Miguel Ángel Sáenz
dc.date.available
2022-12-16T16:57:24Z
dc.date.issued
2021-08
dc.identifier.citation
Toledo Solís, Francisco Javier; Hilerio Ruiz, Andrea Guadalupe; Delgadin, Tomás Horacio; Pérez Sirkin, Daniela Irina; Di Yorio, María Paula; et al.; Changes in digestive enzyme activities during the early ontogeny of the South American cichlid (Cichlasoma dimerus); Springer; Fish Physiology and Biochemistry; 47; 4; 8-2021; 1211-1227
dc.identifier.issn
0920-1742
dc.identifier.uri
http://hdl.handle.net/11336/181572
dc.description.abstract
Cichlasoma dimerus is a neotropical cichlid that has been used as a biological model for neuroendocrinology studies. However, its culture is problematic in terms of larval feeding to allow having enough fry quantity and quality. Larviculture requires full knowledge about the digestive system and nutrition; therefore, this study was intended to assess the digestive enzymes' changes at different ages during the early ontogeny. Acid protease activity was detectable from the first day after hatching (dah), increasing to its maximum peaks on 9 dah. In contrast, alkaline proteases had low activity in the first days of life but reached their maximum activity on 17 dah. Chymotrypsin, L-aminopeptidase, and carboxypeptidase A activities increased at 6 dah, while trypsin activity was first detected on 13 dah and reached its maximum activity on 17 dah. Lipase and α-amylase activity were detectable at low levels in the first days of life, but the activity fluctuated and reaching its maximum activity at 21 dah. Alkaline phosphatase continued to oscillate and had two maximum activity peaks, the first at 6 dah and the second at 19 dah. Zymograms of alkaline proteases on day 6 dah six revealed four activity bands with molecular weights from 16.1 to 77.7 kDa. On 13 dah, two more activity bands of 24.4 and 121.9 kDa were detected, having a total of six proteases. The enzymatic activity analyzes indicate the digestive system shows the low activity of some enzymes in the first days after hatching, registering significant increases on 6 dah and the maximum peaks of activities around at 17 dah. Therefore, we recommend replacing live food with dry feed and only providing dry feed after day 17 dah.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CICHLASOMA DIMERUS
dc.subject
LIPASE
dc.subject
PROTEASES
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ZYMOGRAMS
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Α-AMYLASE
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Otros Tópicos Biológicos
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Changes in digestive enzyme activities during the early ontogeny of the South American cichlid (Cichlasoma dimerus)
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-09-19T16:00:43Z
dc.journal.volume
47
dc.journal.number
4
dc.journal.pagination
1211-1227
dc.journal.pais
Alemania
dc.journal.ciudad
Berlin
dc.description.fil
Fil: Toledo Solís, Francisco Javier. Universidad de Almería; España. Consejo Nacional de Ciencia y Tecnología; México
dc.description.fil
Fil: Hilerio Ruiz, Andrea Guadalupe. Universidad Juárez Autónoma de Tabasco; México
dc.description.fil
Fil: Delgadin, Tomás Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
dc.description.fil
Fil: Pérez Sirkin, Daniela Irina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
dc.description.fil
Fil: Di Yorio, María Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
dc.description.fil
Fil: Vissio, Paula Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Biodiversidad y Biología Experimental y Aplicada. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Biodiversidad y Biología Experimental y Aplicada; Argentina
dc.description.fil
Fil: Peña Marín, Emyr Saul. Universidad Juárez Autónoma de Tabasco; México
dc.description.fil
Fil: Martínez García, Rafael. Universidad Juárez Autónoma de Tabasco; México
dc.description.fil
Fil: Maytorena Verdugo, Claudia Ivette. Universidad Juárez Autónoma de Tabasco; México
dc.description.fil
Fil: Alvarez González, Carlos Alfonso. Universidad Juárez Autónoma de Tabasco; México
dc.description.fil
Fil: de Rodrigáñez, Miguel Ángel Sáenz. Universidad de Granada; España
dc.journal.title
Fish Physiology and Biochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/10.1007/s10695-021-00976-z
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s10695-021-00976-z
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