Abstract
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 SAS13F. subtilis.
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