Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus

Detalhes bibliográficos
Autor(a) principal: Candiotto,F. B.
Data de Publicação: 2018
Outros Autores: Freitas-Júnior,A. C. V., Neri,R. C. A., Bezerra,R. S., Rodrigues,R. V., Sampaio,L. A., Tesser,M. B.
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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spelling 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
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