ABSTRACT In order to provide information on the current knowledge about the native fish Dormitator latifrons and identify the gaps that must be filled to achieve correct resource management, a scientometric study was carried out using different scientific databases. A total of 103 publications were registered between the years 1972 and 2021. Results indicate that the species has been addressed since 2001 with less than one publication per year, with 2008 being the year with the highest number of publications (10). The main topics addressed were ecology, physiology, and parasitology of fish. The available knowledge generated about the species is concentrated in 68 journals, with Mexico as the most productive country, followed by USA and Ecuador, and the most productive research centers about this fish were Mexico’s Instituto Politécnico Nacional and Universidad de Guadalajara. A total of 285 authors were detected contributing knowledge to the species, with Violante-González in the top with ten publications. The co-authorship co-occurrence maps suggest there is no solid collaborative relationship between the scientific community and that the information generated is insufficient for conserving and exploiting this fish. It is essential to increase the study of thematic areas that allow their comprehensive management in the medium term; topics like reproduction in captivity, aquaculture, and nutrition must be addressed in the future to assure a sustainable use of this resource.

ABSTRACT Pacific red snapper (Lutjanus peru) is an important commercial species in Mexico with great aquaculture potential; however, digestive physiology is still unknown. Therefore, the objective of the present work was to characterize the digestive proteases of L. peru juvenile using biochemical and electrophoretic techniques. Results showed a higher acid protease activity than the alkaline proteases, trypsin, chymotrypsin, and leucine aminopeptidase (LAP). The optimum temperature for acid proteases was between 30 to 40°C. Trypsin activity showed two maximum peaks of temperature (30 and 50°C), while alkaline proteases, chymotrypsin, and LAP had optimum temperatures of 50, 50 to 60, and 40°C, respectively. Moreover, the optimum pH of acid proteases was between 2 and 3. Also, alkaline proteases, trypsin, chymotrypsin showed pH optimums at pH 6, 9, and 5, respectively, although LAP showed two optimum pH values at 6 and 9. Acid protease zymogram showed three isoforms, totally inhibited by pepstatin A. Alkaline protease zymogram revealed six bands (125.4, 67.2, 57.9, 48.6, 29.8, and 26.9 kDa), which were inhibited by specific serine-proteases and metalloproteases inhibitors. In conclusion, the main digestion in L. peru depends on stomach proteases, which are characteristic of carnivorous fish, followed by intestinal digestion supported mainly by chymotrypsin.

ABSTRACT Digestive proteases were partially characterized in sheepshead juveniles, using biochemical and electrophoretic techniques. Results showed higher activity level of the stomach proteases (2.39 ± 0.02 U mg protein-1) compared to the intestinal proteases (1.6 ± 0.1 U mg protein-1). The activity of trypsin, chymotrypsin, leucine aminopeptidase and carboxypeptidase A was also recorded. The optimum temperature of the stomach proteases was recorded at 45 °C, while for intestinal proteases was recorded at 55 °C. Stomach proteases showed less stability to temperature changes than intestinal proteases. An optimum pH of 2 was recorded for stomach proteases with high stability under acidic conditions, while an optimum pH of 9 was recorded for intestinal proteases showing high stability under alkaline conditions. Stomach proteases were inhibited around 78% with Pepstatin A, indicating the presence of pepsin as the main protease. The stomach proteases zymogam revealed one active band with Rf of 0.49, this enzyme was completely inhibited by Pepstatin A. The intestinal proteases zymogram revealed four active proteases (51.3, 34.9, 27.8 and 21.2 kDa) that were inhibited by TLCK, which mainly represent a trypsin-like serine proteases. It can be conclude that digestion in sheepshead can be considered as a carnivorous species with an omnivorous tendency.

RESUMEN Se caracterizaron parcialmente las proteasas digestivas de juveniles del sargo, utilizando técnicas bioquímicas y electroforéticas. Los resultados muestran mayores niveles de actividad en las proteasas estomacales (2.39 ± 0.02 U mg proteina-1) comparados con los de las proteasas intestinales (1.6 ± 0.1 U mg protein-1), también se registró la actividad de tripsina, quimotripsina, leucina aminopeptidasa y carboxipeptidasa A. La temperatura óptima de las proteasas estomacales fue de 45 °C, mientras que la de las proteasas intestinales fue de 55 °C. El pH óptimo fue de 2 para las proteasas estomacales con alta estabilidad a condiciones ácidas, mientras que el pH óptimo para las proteasas intestinales fue de 9, mostrando una alta estabilidad en condiciones alcalinas. Las actividades de las proteasas estomacales fue inhibida en un 78% con Pepstatina A, lo que indica la presencia de pepsina, como principal proteasa. El zimograma de proteasas estomacales reveló una sola banda con actividad proteasa, con Rf de 0.49, completamente inhibida por Pepstatina A. El zimograma de proteasas intestinales reveló cuatro bandas (51.3, 34.9, 27.8 y 21.2 kDa). Todas las bandas se inhibieron con TLCK, lo que muestra la presencia principalmente de serina proteasas tipo tripsina. Se concluye que la digestión del sargo puede ser considerada como la de una especie carnívora con tendencia al omnivorismo.