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| Registros recuperados : 7 | |
| 2. |  | BUARQUE, D. S.; CASTRO, P. F. de; SANTOS, F. M. S.; LEMOS, D.; CARVALHO JUNIOR, L. B.; BEZERRA, R. S. Digestive peptidases and proteinases in the midgut gland of the pink shrimp Farfantepenaeus paulensis (Crustacea, Decapoda, Penaeidae). Aquaculture Research, Oxford, v. 40, n. 7, p. 861-870, 2009.| Biblioteca(s): Embrapa Meio-Norte. |
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| 3. | | CASTRO, P. F.; FREITAS JUNIOR, A. C. V.; SANTANA, W. M.; COSTA, H. M. S.; CARVALHO JUNIOR, L. B.; BEZERRA, R. S. Comparative study of amylases from the midgut gland of three species of penaeid shrimp. Journal of Crustacean Biology, v. 32, n. 4, p. 607-613, 2012.| Biblioteca(s): Embrapa Meio-Norte. |
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| 4. | | SANTOS, J. F.; CASTRO, P. F.; LEAL, A. L. G.; FREITAS JÚNIOR, A. C. V. de; LEMOS, D.; CARVALHO JÚNIOR, L. B.; BEZERRA, R. S. Digestive enzyme activity in juvenile Nile tilapia (Oreochromis niloticus, L) submitted to different dietary levels of shrimp protein hydrolysate. Aquaculture International, v. 21, p. 563-577, 2013.| Biblioteca(s): Embrapa Meio-Norte. |
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| 5. | | SANTOS, J. F.; CASTRO, P. F.; LEAL, A. L. G.; FREITAS JÚNIOR, A. C. V. de; LEMOS, D.; CARVALHO JÚNIOR, L. B.; BEZERRA, R. S. Digestive enzyme activity in juvenile Nile tilapia (Oreochromis niloticus, L) submitted to different dietary levels of shrimp protein hydrolysate. Aquaculture International, v. 21, p. 563-577, 2013.| Biblioteca(s): Embrapa Meio Norte / UEP-Parnaíba. |
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| 6. | | BUARQUE, D. S.; CASTRO, P. F. de; SANTOS, F. M. S.; AMARAL, I. P. G.; OLIVEIRA, S. M.; ALVES, K. B.; CARVALHO JUNIOR, L. B.; BEZERRA, R. S. Digestive proteinases and peptidases in the hepatopancreas of the southern brown shrimp (Farfantepenaeus subtilis) in two sub-adult stages. Aquaculture Nutrition, Oxford, v. 16, n. 4, p. 359-369, 2010.| Biblioteca(s): Embrapa Meio-Norte. |
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| 7. | | ASSIS, C. R. D.; CASTRO, P. F. de; AMARAL, I. P. G.; CARVALHO, E. V. M. M.; CARVALHO JUNIOR, L. B.; BEZERRA, R. S. Characterization of acetylcholinesterase from the brain of the Amazonian tambaqui (Colossoma macropomum) and in vitro effect of organophosphorus and carbamate pesticides. Environmental Toxicology and Chemistry, Elmsford-NY, v. 29, n. 10, p. 2243?2248, 2010.| Biblioteca(s): Embrapa Meio-Norte. |
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| Registros recuperados : 7 | |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Meio-Norte. Para informações adicionais entre em contato com cpamn.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Meio-Norte. |
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Data corrente: |
06/12/2012 |
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Data da última atualização: |
01/06/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
B - 1 |
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Autoria: |
CASTRO, P. F.; FREITAS JUNIOR, A. C. V.; SANTANA, W. M.; COSTA, H. M. S.; CARVALHO JUNIOR, L. B.; BEZERRA, R. S. |
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Afiliação: |
PATRICIA FERNANDES DE CASTRO, CPAMN; AUGUSTO C. V. FREITAS JUNIOR, UFPE; WERLAYNE M. SANTANA, UFPE; HELANE M. S. COSTA, UFPE; LUIZ B. CARVALHO JUNIOR, UFPE; RANILSON S. BEZERRA, UFPE. |
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Título: |
Comparative study of amylases from the midgut gland of three species of penaeid shrimp. |
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Ano de publicação: |
2012 |
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Fonte/Imprenta: |
Journal of Crustacean Biology, v. 32, n. 4, p. 607-613, 2012. |
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Idioma: |
Inglês |
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Conteúdo: |
Amylases from the midgut gland of wild Farfantepenaeus subtilis (Pérez-Farfante, 1967) and Litopenaeus schmitti (Burkenroad, 1936), and farmed Litopenaeus vannamei (Boone, 1931) were characterized through studies on the effect of inhibitor and metallic ions, optimal pH and temperature, thermal stability and zymograms. The substrate zymogram revealed nine, eight, ten and seven amylolytic bands from F. subtilis, L. schmitti, adults and juveniles L. vannamei, respectively. Total amylolytic activity in the farmed shrimp was three times as high as that of the wild specimens. Amylases from all species exhibited residual activity above 85% at alkaline pH (7.0-8.0), with optimal temperature between 40 and 50°C. None of the enzymes from the species were thermally stable at temperatures above 55°C. Alpha-amylase activity in F. subtilis and L. schmitti was totally inhibited by Type I inhibitor at 50 and 100 g.mL-1, while enzymes from adult and juvenile L. vannamei retained 43 5 ± 1 98 and 22 5 ± 0 65% of their activity, respectively, at these same concentrations. Ca2+ increased amylase activity in all species only at a concentration of 1 mM, inhibiting activity at 5 and 10 mM. All other ions employed (Cd2+,Zn2+,Hg2+,Cu2+ and Al 3+) strongly inhibited amylase activity, regardless of the concentration used. |
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Palavras-Chave: |
Caracterização amilase; Glândula do intestino médio. |
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Thesaurus NAL: |
Farfantepenaeus subtilis; Litopenaeus schmitti; Litopenaeus vannamei. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 02068naa a2200241 a 4500
001 1941481
005 2022-06-01
008 2012 bl uuuu u00u1 u #d
100 1 $aCASTRO, P. F.
245 $aComparative study of amylases from the midgut gland of three species of penaeid shrimp.
260 $c2012
520 $aAmylases from the midgut gland of wild Farfantepenaeus subtilis (Pérez-Farfante, 1967) and Litopenaeus schmitti (Burkenroad, 1936), and farmed Litopenaeus vannamei (Boone, 1931) were characterized through studies on the effect of inhibitor and metallic ions, optimal pH and temperature, thermal stability and zymograms. The substrate zymogram revealed nine, eight, ten and seven amylolytic bands from F. subtilis, L. schmitti, adults and juveniles L. vannamei, respectively. Total amylolytic activity in the farmed shrimp was three times as high as that of the wild specimens. Amylases from all species exhibited residual activity above 85% at alkaline pH (7.0-8.0), with optimal temperature between 40 and 50°C. None of the enzymes from the species were thermally stable at temperatures above 55°C. Alpha-amylase activity in F. subtilis and L. schmitti was totally inhibited by Type I inhibitor at 50 and 100 g.mL-1, while enzymes from adult and juvenile L. vannamei retained 43 5 ± 1 98 and 22 5 ± 0 65% of their activity, respectively, at these same concentrations. Ca2+ increased amylase activity in all species only at a concentration of 1 mM, inhibiting activity at 5 and 10 mM. All other ions employed (Cd2+,Zn2+,Hg2+,Cu2+ and Al 3+) strongly inhibited amylase activity, regardless of the concentration used.
650 $aFarfantepenaeus subtilis
650 $aLitopenaeus schmitti
650 $aLitopenaeus vannamei
653 $aCaracterização amilase
653 $aGlândula do intestino médio
700 1 $aFREITAS JUNIOR, A. C. V.
700 1 $aSANTANA, W. M.
700 1 $aCOSTA, H. M. S.
700 1 $aCARVALHO JUNIOR, L. B.
700 1 $aBEZERRA, R. S.
773 $tJournal of Crustacean Biology$gv. 32, n. 4, p. 607-613, 2012.
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