Data/hora: 11/06/2024 08:58:37

Provedor de dados: | Institutional Archive of Ifreme (ArchiMer)
País: | France
Título: | Partial characterization of hepatopancreatic and extracellular digestive proteinases of wild and cultivated Octopus maya
Autores: | Martinez, Romain; Santos, R.; Alvarez, A.; Cuzon, Gerard; Arena, L.; Mascaro, M.; Pascual, C.; Rosas, C.
Data: | 2011-06
Ano: | 2011
Palavras-chave: | Cephalopods; Digestive proteinases; Hepatopancreas; Gastric juice; Octopus maya.
Resumo: | Proteinases from hepatopancreas (HP) and gastric juice (GJ) from wild and cultured red octopus (Octopus maya) were characterized. Hepatopancreas assays revealed optimal activity at pH 4, 9-10 and 10 for wild and pH 3, 8, and 9, for cultured octopuses, for total proteinases, trypsin and chymotrypsin, respectively. In the gastric juice, maximum activity was recorded at pH 6, 8, and 7 for total proteinases, trypsin, and chymotrypsin, respectively for both wild and cultured octopus. A reduction on enzyme activity of 70 and 20% was observed in HP and GJ extracts, respectively when protease inhibitor Pepstatin A was used. That result suggests that the main proteases in the HP were aspartic acid proteinases type (possibly Cathepsin D) and some of them were present in the GJ. Dissociating discontinuous polyacrylamide gel electrophoresis showed activity bands between 20 and 28, 30 and 34, 35 and 45, 60 and 70 kDa, and a last one between 75 and 100 kDa. We concluded that extracellular digestion of O. maya takes place in an acid environment, around pH 6. In contrast, intracellular digestion in the HP is developed at pHs between 3 and 4, where cathepsin D could be the most important enzyme for O. maya.
Tipo: | Text
Idioma: | Inglês

Identificador:

http://archimer.ifremer.fr/doc/00036/14683/17998.pdf

DOI:10.1007/s10499-010-9360-5

Editor: | Springer
Relação: | http://archimer.ifremer.fr/doc/00036/14683/
Formato: | application/pdf
Fonte: | Aquaculture International (0967-6120) (Springer), 2011-06 , Vol. 19 , N. 3 , P. 445-457
Fonte: | Springer Science+Business Media B.V. 2010