Bioquímica

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http://repositorio.ufes.br/handle/10/17561
Programa de Pós-Graduação em Bioquímica

Centro: CCS
Telefone: (27) 3335 7342
URL do programa: https://bioquimicaefarmacologia.ufes.br/pt-br/pos-graduacao/PPGBiq

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Navegando Bioquímica por Autor "Araujo, Marlonni Maurastoni"

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    Avaliação Físico-Química Da Interação De Betaciclodextrina Com Isoformas Alfa- E Psi- Tripsina
    (Universidade Federal do Espírito Santo, 2024-02-26) Oliveira, Daniel de Jesus de; Rosa, Dayanne Pinho; https://orcid.org/0000-0002-1483-5848; http://lattes.cnpq.br/7576001371663181; Santos, Alexandre Martins Costa; https://orcid.org/0000-0002-8801-8875; http://lattes.cnpq.br/4144105396879016; https://orcid.org/0009-0007-0082-9547; http://lattes.cnpq.br/5786173815850998; Araujo, Marlonni Maurastoni ; https://orcid.org/0000-0002-6064-3126; http://lattes.cnpq.br/6052184072658200; Cicilini, Maria Aparecida ; https://orcid.org/0000-0003-2751-117X; http://lattes.cnpq.br/7082425279468970
    Cyclodextrins are cyclic polysaccharides with a structure composed of glycopyranose. Studies have shown that cyclodextrins can form promising interactions with proteins, which has several applications in biotechnology and biochemistry, such as the solubilization of hydrophobic compounds and the protection of compounds sensitive to thermal, oxidative degradation, among others. In this work, in order to evaluate the influence of this polysaccharide on conformational stability and protein activity, physicochemical tools were used, adopting bovine trypsin as an enzymatic model of study, due to the knowledge of its structure and enzymatic activity. This enzyme belongs to the class of serine proteases and has several isoforms, α-trypsin, β-trypsin and ψ-trypsin being the most studied. The results showed that protease amidasic activity increased up to about 76% in commercial trypsin, 82% in alpha isoform, and 45% in psi isoform, suggesting that the addition of β-cyclodextrin optimized the amidsis activity of the trypsin isoforms tested. Fluorescence and absorption spectroscopy revealed changes in the structural properties of trypsin due to the interaction with βcyclodextrin, affecting the activity and conformational stability of trypsin. The formation of supramolecular states of trypsin isoforms in the presence of β-cyclodextrin by means of dynamic light scattering (DLS) was also evaluated, in which an increase in the size and dispersivity of the molecule suggestive of the formation of supramolecular states was verified. The joint evaluation of these results suggested that there was the formation of stabilizing interactions between β-cyclodextrin and trypsin isoforms through the formation of supramolecular states, with possible formation of inclusion complexes. Thus, it is suggested that β-cyclodextrin may interact with trypsin and affect its proteolytic activity and stability and thus the influence of the osmolyte can be understood at the molecular level.