TY - JOUR
T1 - Partial characterisation of digestive proteases of the Mayan cichlid Cichlasoma urophthalmus
AU - Cuenca-Soria, C. A.
AU - Álvarez-González, C. A.
AU - Ortiz-Galindo, J. L.
AU - Nolasco-Soria, H.
AU - Tovar-Ramírez, D.
AU - Guerrero-Zárate, R.
AU - Castillo-Domínguez, A.
AU - Perera-García, M. A.
AU - Hernández-Gómez, R.
AU - Gisbert, E.
N1 - Funding Information:
Acknowledgments Authors thank the Consejo Nacional de Ciencia y Tecnología from Mexico for providing grant for postgraduate studies, Carlos Alfonso Frías Quintana (Labor-atorio de Acuicultura Tropical, DACBIOL-UJAT, Tabasco, Mexico) for providing advice, as well as the project ‘‘Iden-tificación de ingredientes en alimentos balanceados y su digest-ibilidad en el cultivo experimental de peces nativos en Tabasco’’ financed by the Fondos Mixtos CONACyT, Mexico, for supporting the development of the study. The result of the study that is published was funded with PIFI 2012 resources. To the National Polytechnical Institute (IPN) of Mexico, to allow me to continue with my academic trajectory.
PY - 2014/6
Y1 - 2014/6
N2 - The characterisation of digestive proteases in native freshwater fish such as the Mayan cichlid Cichlasoma urophthalmus provides scientific elements that may be used to design balanced feed that matches with the digestive capacity of the fish. The purpose of this study was to characterise the digestive proteases, including the effect of the pH and the temperature on enzyme activity and stability, as well as the effect of inhibitors using multienzymatic extracts of the stomach and intestine of C. urophthalmus juveniles. Results showed that the optimum activities of the acid and alkaline proteases occurred at pH values of 3 and 9, respectively, whereas their optimum temperatures were 55 and 65 °C, respectively. The acid proteases were most stable at pH values of 2-3 and at temperatures of 35-45 °C, whereas the alkaline proteases were most stable at pH values of 6-9 and at 25-55 °C. The inhibition assays recorded a residual activity of 4 % with pepstatin A for the acid proteases. The inhibition of the alkaline proteases was greater than 80 % with TPCK, TLCK, EDTA and ovalbumin, and of 60 and 43.8 % with PMSF and SBT1, respectively. The results obtained in this study make it possible to state that C. urophthalmus has a sufficiently complete digestive enzyme machinery to degrade food items characteristic of an omnivorous fish species, although specimens showed a tendency to carnivory.
AB - The characterisation of digestive proteases in native freshwater fish such as the Mayan cichlid Cichlasoma urophthalmus provides scientific elements that may be used to design balanced feed that matches with the digestive capacity of the fish. The purpose of this study was to characterise the digestive proteases, including the effect of the pH and the temperature on enzyme activity and stability, as well as the effect of inhibitors using multienzymatic extracts of the stomach and intestine of C. urophthalmus juveniles. Results showed that the optimum activities of the acid and alkaline proteases occurred at pH values of 3 and 9, respectively, whereas their optimum temperatures were 55 and 65 °C, respectively. The acid proteases were most stable at pH values of 2-3 and at temperatures of 35-45 °C, whereas the alkaline proteases were most stable at pH values of 6-9 and at 25-55 °C. The inhibition assays recorded a residual activity of 4 % with pepstatin A for the acid proteases. The inhibition of the alkaline proteases was greater than 80 % with TPCK, TLCK, EDTA and ovalbumin, and of 60 and 43.8 % with PMSF and SBT1, respectively. The results obtained in this study make it possible to state that C. urophthalmus has a sufficiently complete digestive enzyme machinery to degrade food items characteristic of an omnivorous fish species, although specimens showed a tendency to carnivory.
KW - Characterisation
KW - Cichlasoma urophthalmus
KW - Digestive proteases
KW - Inhibitors
KW - Temperature
KW - pH
UR - http://www.scopus.com/inward/record.url?scp=84899931215&partnerID=8YFLogxK
U2 - 10.1007/s10695-013-9876-5
DO - 10.1007/s10695-013-9876-5
M3 - Artículo
SN - 0920-1742
VL - 40
SP - 689
EP - 699
JO - Fish Physiology and Biochemistry
JF - Fish Physiology and Biochemistry
IS - 3
ER -