Changes of digestive enzymes in totoaba (Totoaba macdonaldi Gilbert, 1890) during early ontogeny

ABSTRACT Totoaba macdonaldi is an endemic species which has been overexploited causing its population to decrease and to be cataloged as endangered. Understanding the larval period is the most critical stage in the development of marine fish farming. Our study aims to determine the changes in digest...

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Autores principales: Córdova-Montejo,Mabelyn, Álvarez-González,Carlos A., López,Lus M., True,Conal D., Frías-Quintana,Carlos A., Galaviz,Mario A.
Lenguaje:English
Publicado: Pontificia Universidad Católica de Valparaíso. Facultad de Recursos Naturales. Escuela de Ciencias del Mar 2019
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Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0718-560X2019000100102
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spelling oai:scielo:S0718-560X20190001001022019-03-27Changes of digestive enzymes in totoaba (Totoaba macdonaldi Gilbert, 1890) during early ontogenyCórdova-Montejo,MabelynÁlvarez-González,Carlos A.López,Lus M.True,Conal D.Frías-Quintana,Carlos A.Galaviz,Mario A. Totoaba macdonaldi ontogeny nutrition proteases amylase lipase zymogram ABSTRACT Totoaba macdonaldi is an endemic species which has been overexploited causing its population to decrease and to be cataloged as endangered. Understanding the larval period is the most critical stage in the development of marine fish farming. Our study aims to determine the changes in digestive enzyme activities during the early ontogeny of totoaba, using biochemical and electrophoretic techniques as SDS-PAGE. The results show that the acid protease had maximum activity between days 28 and 32 days post-hatching (DPH) when the Artemia was replaced by formulated food. Alkaline protease activity was detected at 2 DPH with maximal activity between 20 and 32 DPH; trypsin activity became active from 2 DPH; chymotrypsin activity increased at 6 DPH; leucine aminopeptidase activity was detected at 3 DPH, showing its maximal level at 22 DPH; carboxypeptidase A activity increased at 3 DPH; and lipase and amylase activities were detected at 2 DPH. Acid zymogram showed only one isoform (0.72 rf) from 2 DPH and increased in intensity from 8 DPH. For alkaline proteases, four isoforms were detected from yolk absorption (1 DPH), increasing to six isoforms (77.8, 47.3, 43.5, 21.0, 19.2, and 17.5 kDa) from 8 DPH onwards. Our results demonstrate that larvae of T. macdonaldi present characteristics typical of carnivore marine fish, showing the presence of alkaline digestive enzymes prematurely and the presence of offset pepsin. According to the results obtained in the present study, T. macdonaldi can be a juvenile beginning between 24 and 28 DPH, being the most appropriate day to perform replacement by artificial food.info:eu-repo/semantics/openAccessPontificia Universidad Católica de Valparaíso. Facultad de Recursos Naturales. Escuela de Ciencias del MarLatin american journal of aquatic research v.47 n.1 20192019-03-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0718-560X2019000100102en10.3856/vol47-issue1-fulltext-11
institution Scielo Chile
collection Scielo Chile
language English
topic Totoaba macdonaldi
ontogeny
nutrition
proteases
amylase
lipase
zymogram
spellingShingle Totoaba macdonaldi
ontogeny
nutrition
proteases
amylase
lipase
zymogram
Córdova-Montejo,Mabelyn
Álvarez-González,Carlos A.
López,Lus M.
True,Conal D.
Frías-Quintana,Carlos A.
Galaviz,Mario A.
Changes of digestive enzymes in totoaba (Totoaba macdonaldi Gilbert, 1890) during early ontogeny
description ABSTRACT Totoaba macdonaldi is an endemic species which has been overexploited causing its population to decrease and to be cataloged as endangered. Understanding the larval period is the most critical stage in the development of marine fish farming. Our study aims to determine the changes in digestive enzyme activities during the early ontogeny of totoaba, using biochemical and electrophoretic techniques as SDS-PAGE. The results show that the acid protease had maximum activity between days 28 and 32 days post-hatching (DPH) when the Artemia was replaced by formulated food. Alkaline protease activity was detected at 2 DPH with maximal activity between 20 and 32 DPH; trypsin activity became active from 2 DPH; chymotrypsin activity increased at 6 DPH; leucine aminopeptidase activity was detected at 3 DPH, showing its maximal level at 22 DPH; carboxypeptidase A activity increased at 3 DPH; and lipase and amylase activities were detected at 2 DPH. Acid zymogram showed only one isoform (0.72 rf) from 2 DPH and increased in intensity from 8 DPH. For alkaline proteases, four isoforms were detected from yolk absorption (1 DPH), increasing to six isoforms (77.8, 47.3, 43.5, 21.0, 19.2, and 17.5 kDa) from 8 DPH onwards. Our results demonstrate that larvae of T. macdonaldi present characteristics typical of carnivore marine fish, showing the presence of alkaline digestive enzymes prematurely and the presence of offset pepsin. According to the results obtained in the present study, T. macdonaldi can be a juvenile beginning between 24 and 28 DPH, being the most appropriate day to perform replacement by artificial food.
author Córdova-Montejo,Mabelyn
Álvarez-González,Carlos A.
López,Lus M.
True,Conal D.
Frías-Quintana,Carlos A.
Galaviz,Mario A.
author_facet Córdova-Montejo,Mabelyn
Álvarez-González,Carlos A.
López,Lus M.
True,Conal D.
Frías-Quintana,Carlos A.
Galaviz,Mario A.
author_sort Córdova-Montejo,Mabelyn
title Changes of digestive enzymes in totoaba (Totoaba macdonaldi Gilbert, 1890) during early ontogeny
title_short Changes of digestive enzymes in totoaba (Totoaba macdonaldi Gilbert, 1890) during early ontogeny
title_full Changes of digestive enzymes in totoaba (Totoaba macdonaldi Gilbert, 1890) during early ontogeny
title_fullStr Changes of digestive enzymes in totoaba (Totoaba macdonaldi Gilbert, 1890) during early ontogeny
title_full_unstemmed Changes of digestive enzymes in totoaba (Totoaba macdonaldi Gilbert, 1890) during early ontogeny
title_sort changes of digestive enzymes in totoaba (totoaba macdonaldi gilbert, 1890) during early ontogeny
publisher Pontificia Universidad Católica de Valparaíso. Facultad de Recursos Naturales. Escuela de Ciencias del Mar
publishDate 2019
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0718-560X2019000100102
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