Diversidad enzimática de la fracción soluble de un aislado venezolano de adultos Paragonimus sp

paragonimus sp. is a trematode that causes chronic inflammation of the lung in carnivorous mammals and humans, which constitute a public health problem in asian and latin american countries. trematodes have enzymes that facilitate their penetration and migration through different host organs to ensure their life cycle. to evaluate the enzymatic diversity of the soluble fraction (fspa, 100,000 g) of a venezuelan isolate of paragonimus sp. adult worms, several enzyme determinations were conducted at different ph. the activities of enzymes releasing p-nitrophenol or p-nitroanilina from the corresponding dye-related synthetic peptides were assessed by interpolating absorbance (a 405 nm) values in the corresponding calibration curve (a 405 nm vs. nmol); on the other hand, absorbances of 2-naphtylamine and 2-naphtols released from another series of synthetic substrates were read at different wavelengths between 450 nm and 620 nm to assess for the activity of the corresponding hydrolases. phosphohydrolase, glycosidase and peptidase activities were detected in fspa, β-n-acetyl-β-d-glucosaminidase (0.55 μmol/h/mg, ph 5.5) and cystein protease (0.4 μmol/h/mg, ph 5.5) being higher than all the other detected activities. these activities are probably related to the adult worm habitat and its need for glycan and peptide degradation of lung secretions. these results represent the first enzymatic study done with a venezuelan isolate of adult paragonimus sp. worms collected from the common reservoir didelphis marsupialis.