Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Biology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842018000200281 |
Resumo: | Abstract Knowledge of specific enzyme activity, along with animal habits and digestive capacity is essential in formulating an appropriate diet for any species. In this study, we evaluated and characterized the activity of digestive enzymes present in the liver, intestine, and stomach of Paralichthys orbignyanus. The effects of pH and temperature on enzyme activity were also evaluated via the use of specific substrates. The use of specific substrates and inhibitors showed strong evidence of the presence of trypsin (BApNA= 0.51 ± 0.2 mU mg-1), chimotrypsin (SApNA= 2.62 ± 1.8 mU mg-1), and aminopeptidases (Leu-p-Nan =0.9709 ± 0.83 mU mg-1) in the intestine. Optimum pH for the activity of trypsin, chemotrypsin, leucino aminopeptidase, amilase, and pepsin were 9.5, 9.0, 8.0, 7.5, and 3.5, respectively, while optimum temperatures were 50, 50, 50, 40, and 45 °C, respectively. These results provide additional information regarding the biology of Brazilian flounder and can be used as a basis for further studies regarding fish feeding physiology. |
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Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanustrypsinproteasedigestive tractAbstract Knowledge of specific enzyme activity, along with animal habits and digestive capacity is essential in formulating an appropriate diet for any species. In this study, we evaluated and characterized the activity of digestive enzymes present in the liver, intestine, and stomach of Paralichthys orbignyanus. The effects of pH and temperature on enzyme activity were also evaluated via the use of specific substrates. The use of specific substrates and inhibitors showed strong evidence of the presence of trypsin (BApNA= 0.51 ± 0.2 mU mg-1), chimotrypsin (SApNA= 2.62 ± 1.8 mU mg-1), and aminopeptidases (Leu-p-Nan =0.9709 ± 0.83 mU mg-1) in the intestine. Optimum pH for the activity of trypsin, chemotrypsin, leucino aminopeptidase, amilase, and pepsin were 9.5, 9.0, 8.0, 7.5, and 3.5, respectively, while optimum temperatures were 50, 50, 50, 40, and 45 °C, respectively. These results provide additional information regarding the biology of Brazilian flounder and can be used as a basis for further studies regarding fish feeding physiology.Instituto Internacional de Ecologia2018-05-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842018000200281Brazilian Journal of Biology v.78 n.2 2018reponame:Brazilian Journal of Biologyinstname:Instituto Internacional de Ecologia (IIE)instacron:IIE10.1590/1519-6984.06616info:eu-repo/semantics/openAccessCandiotto,F. B.Freitas-Júnior,A. C. V.Neri,R. C. A.Bezerra,R. S.Rodrigues,R. V.Sampaio,L. A.Tesser,M. B.eng2018-05-02T00:00:00Zoai:scielo:S1519-69842018000200281Revistahttps://www.scielo.br/j/bjb/https://old.scielo.br/oai/scielo-oai.phpbjb@bjb.com.br||bjb@bjb.com.br1678-43751519-6984opendoar:2018-05-02T00:00Brazilian Journal of Biology - Instituto Internacional de Ecologia (IIE)false |
dc.title.none.fl_str_mv |
Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus |
title |
Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus |
spellingShingle |
Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus Candiotto,F. B. trypsin protease digestive tract |
title_short |
Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus |
title_full |
Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus |
title_fullStr |
Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus |
title_full_unstemmed |
Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus |
title_sort |
Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus |
author |
Candiotto,F. B. |
author_facet |
Candiotto,F. B. Freitas-Júnior,A. C. V. Neri,R. C. A. Bezerra,R. S. Rodrigues,R. V. Sampaio,L. A. Tesser,M. B. |
author_role |
author |
author2 |
Freitas-Júnior,A. C. V. Neri,R. C. A. Bezerra,R. S. Rodrigues,R. V. Sampaio,L. A. Tesser,M. B. |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Candiotto,F. B. Freitas-Júnior,A. C. V. Neri,R. C. A. Bezerra,R. S. Rodrigues,R. V. Sampaio,L. A. Tesser,M. B. |
dc.subject.por.fl_str_mv |
trypsin protease digestive tract |
topic |
trypsin protease digestive tract |
description |
Abstract Knowledge of specific enzyme activity, along with animal habits and digestive capacity is essential in formulating an appropriate diet for any species. In this study, we evaluated and characterized the activity of digestive enzymes present in the liver, intestine, and stomach of Paralichthys orbignyanus. The effects of pH and temperature on enzyme activity were also evaluated via the use of specific substrates. The use of specific substrates and inhibitors showed strong evidence of the presence of trypsin (BApNA= 0.51 ± 0.2 mU mg-1), chimotrypsin (SApNA= 2.62 ± 1.8 mU mg-1), and aminopeptidases (Leu-p-Nan =0.9709 ± 0.83 mU mg-1) in the intestine. Optimum pH for the activity of trypsin, chemotrypsin, leucino aminopeptidase, amilase, and pepsin were 9.5, 9.0, 8.0, 7.5, and 3.5, respectively, while optimum temperatures were 50, 50, 50, 40, and 45 °C, respectively. These results provide additional information regarding the biology of Brazilian flounder and can be used as a basis for further studies regarding fish feeding physiology. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-05-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842018000200281 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1519-69842018000200281 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/1519-6984.06616 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto Internacional de Ecologia |
publisher.none.fl_str_mv |
Instituto Internacional de Ecologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Biology v.78 n.2 2018 reponame:Brazilian Journal of Biology instname:Instituto Internacional de Ecologia (IIE) instacron:IIE |
instname_str |
Instituto Internacional de Ecologia (IIE) |
instacron_str |
IIE |
institution |
IIE |
reponame_str |
Brazilian Journal of Biology |
collection |
Brazilian Journal of Biology |
repository.name.fl_str_mv |
Brazilian Journal of Biology - Instituto Internacional de Ecologia (IIE) |
repository.mail.fl_str_mv |
bjb@bjb.com.br||bjb@bjb.com.br |
_version_ |
1752129884871720960 |