Partial characterization of digestive proteases in adults of bigclaw river shrimp Macrobrachium carcinus

• Manríquez-Santos, Teresa de Jesús ^[1] ; Álvarez-González, Carlos Alfonso ^[1] ; Peña, Emyr ^[1] ; Camarillo-Coop, Susana ^[1] ; Martínez-García, Rafael ^[1] ; Vega-Villasante, Fernando ^[2]
  1. [1] Universidad Juárez Autónoma de Tabasco

     Universidad Juárez Autónoma de Tabasco

     México

     
  2. [2] Universidad de Guadalajara

     Universidad de Guadalajara

     México

     
• Localización: Latin American Journal of Aquatic Research, ISSN-e 0718-560X, ISSN 0716-1069, Vol. 46, Nº. 3, 2018, págs. 525-533
• Idioma: inglés
• Enlaces
  • Texto completo
• Resumen

  • The present research was focused to characterize the digestive proteases in Macrobrachium carcinus adults using biochemical and electrophoretic techniques. Our results showed that the alkaline proteolytic activity from males and females did not show significant differences (P > 0.05) between them, the optimum pH for digestive proteases is 8, and is very stable to changes in alkaline pH (8 and 10). The optimum temperature for alkaline proteases is 45ºC and is stable from 25 to 45ºC. The activity was totally inhibited with phenylmethylsulfonyl fluoride (PMSF), additionally the inhibition with trypsin soybean inhibitor 1 (SBT1) and tosyl-lysine-methyl ketone (TLCK) indicate high effect over serine proteases. Eight active bands were found using sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE) zymogram (range 17.8-94.0 kDa), which were partially inhibited with ovalbumin (Ovo), SBT1, phenanthroline (Phen), tosyl-phenylalanine-methyl ketone (TPCK), TLCK and ethylenediaminetetraacetic acid (EDTA), indicating an omnivorous digestive capacity, which remarks that the mainly alkaline protease in M. carcinus hepatopancreas are trypsin like enzymes.