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Similar patterns of hydrolases were observed in three species representing two genera of entomopathogenic nematodes: Steinernema affinis, S. feltiae, and Heterorhabditis zealandica. The same enzymes were present in the studied nematodes but they differed in the level of activity of individual sub-classes of enzymes. A higher activity of esterases and proteolytic enzymes could be observed for H. zealandica than for S. affinis and S. feltiae. On the other hand, the activity of glycosidases in steinernematids was generally much higher than in H. Zealandica.
The content of glycogen, glucose and trehalose was measured in larvae and adults of Cystidicola farionis, the parasite isolated from the swim bladder of Osmerus eperlanus from Vistula Lagoon. Activity of glycogen phosphorylase, α-amylase, glucoamylase. maltase, trehalase. And trehalose phosphorylase were measured. The highest activity was recorded for α-amylase 10,07 ± 0,97 mu/mg and 7,47 ± 0,24 mu/mg, next maltase 1,34 ± 0,63 μmol /mg and 2,06 ± 1,65 μmol/mg respectively for larvae and adults. The activity of glucoamylase was nearly the same for adults and larvae (about 0,20 μmol/mg). The trehalase activity was higher at adults (0,49 ± 0,42 μmol/mg) than at larvae (0,18 ± 0,12 μmol/mg). The activity of glycogen phosphorylase was much higher at larvae (3,58 ± 1,49 μmol/mg) than at adults parasite (0,10 ± 0,02 μmol/mg). The trehalose phosphorylase was present in both stages of parasite, but its activity was low. The content of glycogen and glucose was two-limes higher in the adults' body than in larvae.
The experimental studies were conducted on caterpillars of wax moth Galleria mellonella infected with Steinernema affinis larvae. The concentration of trehalose and the activity of trehal ase were measured during the invasion lasting 48h. The level of trehalose and activity of enzyme were slightly lower in infected insects in comparison to the control animals.
α-Amylase is present in the third (L3) and in the fourth-stage (L4) of larvae from Anisakis simplex. The enzymes from both sources differ in same of their properties. Α-Amylase from L3 showed a maximum at pH 7,8, enzyme from L4 stage at pH 6,5. The α-amylase from L3 was mainly lysosomal enzyme. The enzyme from L4 was located in the microsomal fraction. The L3 α-amylase showed the inhibition by EDT A and by -SH reagent iodoacetic acid. These agents did not change the activity of L4 enzyme. Bath izoenzymes were unaffected by calcium and magnesium ions. Generally the α-amylase from L4 stage had higher activity (3,71 u/mg) than L3 one (2,29 u/mg).
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