Research Article

Body-surface protease inhibitors in cage and hive Apis mellifera L.

Aneta Strachecka, Jerzy Paleolog, Grzegorz Borsuk, Krzysztof Olszewski, Krzysztof Grzywnowicz, Magdalena Gryzińska

Abstract. The aim of the work was to determine the activity of protease inhibitors sampled from the body surface of bee workers kept in a natural hive environment and in a cage. The samples were collected for five weeks. 40 cage samples and 50 hive samples were gathered, each containing 10 bees. Hydrophilic (water-treated) and hydrophobic (Triton-rinsed) proteins were isolated from the insects. The samples containing washed-out proteins were tested as follows: the activity of aspartic and serine protease inhibitors by the Lee and Lin method; electrophoretic analysis of proteins in a polyacrylamide gel for protease inhibitor detection by means of the modified Felicioli method; and in vivo tests of antifungal and antibacterial activity using the double application method. The cage environment had a destabilizing effect on the natural protease inhibitor system causing radical variation in its activity, which was not the case with the hive environment. The samples were not found to be active in relation to M. luteus and E. coli. The cage bees were less resistant to microorganisms. The results of the in vivo microorganismal test confirmed the fact of weaker protease inhibitor activity in the washed-out body-surface samples of the cage bees that was also observed in in vitro biochemical analyses. The results of cage-based analyses of non-specific apian resistance should be treated with caution when used in reference to hive bees.

Keywords: Apis mellifera, beehive, body surface, cage, protease inhibitors

 

This Article

Published online: 4 May 2017

Accesses: 185

How to cite

Strachecka, A., Paleolog, J., Borsuk, G., Olszewski, K., Grzywnowicz, K., Gryzińska, M., (2011). Body-surface protease inhibitors in cage and hive Apis mellifera L.. Acta Sci. Pol. Zootechnica, 10(4), 125–132.