Polymolecular Complexes of Chitosan with the Bombyx Mori Protein

O. Avazova, R.Yu. Milushevа, I. Nurgaliev, S. Rashidova
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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 iono-genicity. 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 occur-rence 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. Quantum-chemical DFT study of ChS complexes with amino acids (AAs) was carried out. The stability of complexes 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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壳聚糖与家蚕蛋白的多分子配合物
研究了壳聚糖(ChS)与家蚕蛋白在不同pH范围内的相互作用,揭示了壳聚糖与家蚕蛋白获得配合物的基本可能性。用理化方法证实了ChS与蛋白质在水溶液中形成的多分子复合物。结果表明,ChS结构具有一定的刚性和离子原性。结果表明,在pH = 4.8 ~ 6.7范围内,蛹蛋白与ChS的络合作用为2%醋酸。红外光谱中检测到的吸收带的变化和移位证实了在pH = 4.8 ~ 6.7时,ChS分子与蛋白质之间发生了络合形成反应,并在1641、1538和1068 cm-1处的红外光谱中进行了表征。利用量子化学DFT研究了ChS与氨基酸配合物(AAs)的关系。除与组氨酸在气相中形成的配合物外,ChS- aa均表现出稳定性。计算结果表明,ChS与AAs的络合反应存在较强的热力学驱动力。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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