| Autor: |
BUARQUE, D. S., CASTRO, P. F., SANTOS, F. M. S., AMARAL, I. P. G., OLIVEIRA, S. M., ALVES, K. B., CARVALHO JR, L. B., BEZERRA, R. S. |
| Předmět: |
|
| Zdroj: |
Aquaculture Nutrition; Aug2010, Vol. 16 Issue 4, p359-369, 11p, 2 Charts, 7 Graphs |
| Abstrakt: |
The aim of this study was to examine proteinases and peptidases from the hepatopancreas of two sub-adult stages of Farfantepenaeus subtilis: SAS6 (5.93 ± 0.69 g wet weight) and SAS13 (13.26 ± 0.60 g wet weight). Trypsin and chymotrypsin activity was higher in the extract from the SAS6 individuals ( P < 0.05). The highest activity among aminoacyl-β-naphthylamide substrates was found using alanine-, arginine-, leucine- and lysine-β-naphthylamide. There was a positive correlation between the recommended concentration of essential amino acids in penaeid shrimp feed and aminopeptidase activity in both sub-adult stages. Proteolytic activity of F. subtilis was strongly inhibited by specific trypsin inhibitors. The optimal temperature for trypsin, chymotrypsin and leucine aminopeptidase activity was between 45 and 55 °C. Six and seven bands were found in caseinolytic zymograms for SAS6 and SAS13 respectively. All bands were inhibited by phenylmethylsulfonyl fluoride in both sub-adult stages. The use of tosyl-lysine-chloromethyl-ketone and benzamidine caused strong inhibition of the proteolytic bands. Trypsin and chymotrypsin activity was the main difference observed between the protease pattern of SAS6 and SAS13 F. subtilis. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
