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The purpose of the work was to study the meat productivity of broiler chickens of the cross Ross PM3 when feeding the enzyme drug VP-1. The work was carried out on the basis of the poultry farm of JSC “Lindovskaya poultry farm-breeding plant”. The control group of broiler chickens were fed with complete compound feed without additives. The poultry of the 1st experimental group received an enzyme additive in the amount of 0,4 kg/t of feed, the 2nd group received it 0,5 kg/t of feed, the 3rd group received it in the amount of 0,6 kg/t of feed. The enzyme additive was incorporated by stepwise mixing. The broiler chickens of the control group were characterized by a fairly high growth rate, which by the age of 38 days had a live weight of 2082,29 g. At the same time, the broiler chickens of the 1st experimental group had slightly better indicators. So, by the age of 38 days their average live weight was 232,42 g higher than their herdmates from the control group (P ≥ 0,999). The broiler chickens of the 2nd experimental group had the average live weight of 2271,72 g, which was by 189,43 g or 9,10 % (P ≥ 0,999) higher than in the control group. The maximum live weight for 38 days of rearing was gained by broiler chickens of the 3rd experimental group 2352,92 g, which exceeded broiler chickens of the 1st experimental group by 38,21 g or 1,65 %, as well as the live weight of chickens of the 2nd experimental group by 81,20 g or 3,57 %. The maximum positive dynamics of live weight was shown by broiler chickens of the 3rd experimental group, and the minimum was shown by chickens of the control group. Chickens of the 1st experimental group and the 2nd experimental group showed the dynamics of live weight gain significantly exceeding the growth rate of live weight of broilers of the control group.

The interaction of AIMP1/р43 recombinant protein, which is a component of aminoacyl-tRNA synthetase complex in higher eukaryotes, in the complex with tRNA was studied. It was shown that temperature stability of AIMP1/p43 is significantly increased in the complex. Local conformational transition of residue Trp271 of AIMP1/p43, which is associated with intramolecular protein stability, is observed at 430C, but in a complex with tRNA it is observed at 490C. Based on the data of spectrofluorimetric titration the value of the dissociation constant and the stoichiometry of the complex of AIMP1/p43 with tRNA were determined. The model of the complex of AIMP1/p43 with tRNA was obtained by the molecular docking method.

Stability of the recombinant AIMP1/p43 protein – component of aminoacyl-tRNA synthetase complex of higher eukaryotic – in nanocomposite complex with β-cyclodextrin was investigated. A significant increase in thermal stability AIMP1/p43 in the composition of nanocomposite complex was shown. The local conformational transition associated with the exposure of Trp271 residue on the AIMP1/p43 surface was observed at 43 0 C, but in the nanocomposite complex it was observed at 52 0 C. Stabilization of AIMP1/p43 protein in nanocomposite complex provides opportunities for further structural and functional studies and its use as a new biotechnology product in biomedicine.