Inhibition of Intestinal Proteolytic Activity of Schistocerca piceifrons piceifrons (Walker)¹ and Pterophylla beltrani (Bolívar and Bolívar)² Using Extracts from Chamaedorea radicalis Mart. Fruit
2020
Montelongo-Ruíz, Gerardo | Olazarán-Santibáñez, Fabián Eliseo | Reyes-Zepeda, Francisco | Torres-Castillo, Jorge Ariel | de la Rosa-Manzano, Edilia | Martínez-Ávalos, José Guadalupe | Arellano-Méndez, Leonardo Uriel | Mora-Olivo, Arturo
Inhibition of intestinal proteases by several plant species constitutes a major defense strategy against insects. However, the efficacy of this mechanism depends on the diversity and concentration of enzymatic components in insects and susceptibility of intestinal activity. Protease inhibition capacity by fruit of hardy parlor palms (Chamaedorea radicalis Mart.) and its effect on intestinal proteolytic activity of adult Orthoptera Schistocerca piceifrons piceifrons (Walker) and Pterophylla beltrani (Bolívar and Bolívar) were studied. Proteolytic activity using chromogenic substrate Nα-benzoyl-D, L-arginine-4-nitroanilide hydrochloride was determined by spectrophotometric tests. The intestinal proteolytic activity of both orthopteran species was related to serine and cysteine proteases. Total proteolytic activity was 98,930.56 ± 7,544.46 PAU/g (proteolytic activity units per gram) of intestinal tissue in S. p. piceifrons and 52,847.22 ± 8,509.11 PAU/g in P. beltrani. Inhibition capacity of C. radicalis differed for each Orthoptera species according to the ripening stage of fruit. The orange stage of ripening had greater inhibitory effect on S. p. piceifrons, while the green stage had greater inhibitory effect on P. beltrani. Fruit of hardy parlor palms are a source of protease inhibitors targeting intestinal enzymes of the evaluated Orthoptera and could be considered strong candidates in future studies for identification and characterization of the inhibitors and their potential use in biological control.
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