Insights into Cysteine Protease Complexes with Grafted Chitosan–Poly(<i>N</i>-vinylpyrrolidone) Copolymers: Catalytic Activity and Storage Stability
2025
Maria S. Lavlinskaya | Andrey V. Sorokin | Anastasia N. Dubovitskaya | Anastasia I. Yutkina | Maxim S. Kondratyev | Marina G. Holyavka | Yuriy F. Zuev | Valeriy G. Artyukhov
The investigation of structure–function relationships in enzyme polysaccharide complexes provides a theoretical foundation for modulating enzyme properties and expanding their industrial applications. In this study, the interaction of cysteine proteases—bromelain, ficin, and papain—with a grafted chitosan–poly(<i>N</i>-vinylpyrrolidone) copolymers, Cs-<i>g</i>-PVP, was examined, and its effect on the catalytic and stability properties of the enzymes was assessed. Molecular docking and Fourier-transform infrared spectroscopy were used to analyze the topology of the resulting complexes and identify macromolecular fragments involved in binding. Based on the obtained results, it was hypothesized that complex formation would lead to a slight reduction in the catalytic activity of cysteine proteases. In vitro studies of the complexes confirmed this hypothesis, showing that the enzymes retained more than 63% of their proteolytic activity while their half-inactivation time during storage increased by up to ~12-fold. The investigated Cs-<i>g</i>-PVP copolymers demonstrated high efficiency as supports for the studied enzymes, capable of retaining up to 100% of the added enzymes.
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