Abstract

The interaction of chitosan (ChS) and the Bombyx mori protein on different pH ranges was studied, and the fundamental possibility of obtaining complexes of ChS with the Bombyx mori protein was revealed. The for-mation of a polymolecular complex of protein with ChS in aqueous solutions was confirmed by the results of physico-chemical methods. It is shown that the ChS structure is characterized by a certain rigidity and ionogenicity. The results indicate the complexation of the pupae protein with ChS in 2% acetic acid in the range of pH = 4.8–6.7. The detected changes and shifts of the absorption bands in the IR spectra confirm the occurrence of the complex formation reaction between the molecules of ChS and protein at pH = 4.8–6.7, which is characterized by absorption bands in the IR spectra at 1641 cm–1, 1538 cm–1 and 1068 cm–1. Quan-tum-chemical DFT study of ChS complexes with amino acids (AAs) was carried out. The stability of com-plexes of ChS with AAs (ChS-AA) was shown except for the complex formed with histidine in the gas phase. The calculation results indicate the presence of a strong thermodynamic driving force in the complexation of ChS with AAs.

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