Journal of Apicultural Science

The activity of nineteen hydrolases in extracts from Varroa destructor and in hemolymph of Apis mellifera carnica worker bees

Journal of Apicultural Science. Volume 53, Issue 1, Pages 43-51, ISSN (Print) 1643-4439
The activity of 19 hydrolases in extracts of Varroa destructor mite and hemolymph of Apis mellifera carnica honey bee (a host) were studied. Within parasite's esterases high activity of alkaline and acid phosphatase, low esterase (C4) and esterase (C8), and no activity of lipase (C14) was noticed. Among its peptidases the activity of leucine arylamidase was high, and a low activity of valine, cysteine arylamidase and trypsin was detected. However, no activity of chymotrypsin was observed. Except for á-galactosidase, á-mannosidase, a high activity was observed in the rest of the á- and ß-glycosidases. The activity for all 19 enzymes was found in the hemolymph of worker bees. It should be noticed that the relative activity of most of the enzymes was on almost the same level in the host as in the parasite. However, the activities of glycosidases; á-fucosidase, ß-glucuronidase and á-galactosidase were higher in the parasite than in the honey bee hemolymph.
Apis mellifera carnica, Varroa destructor, enzyme, hydrolase
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