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Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity

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Resumo:Fish protein hydrolysates (FPH) obtained from industrial processing residues are sources of bioactive peptides. The enzymatic hydrolysis process is essential in obtaining specific bioactivities such as inhibition of the enzyme acetylcholinesterase (AChE). In this study the effect of different hydrolysis conditions on the properties of FPH to inhibit the enzyme acetylcholinesterase. A chemometric evaluation, based on a central composite rotatable design and principal component analysis, was applied to select hydrolysis conditions with best yield, degree of hydrolysis and acetylcholinesterase inhibition. Experimental design results for AChE inhibition were between 10.51 and 40.45% (20, 30 and 50 mg.mL-1 of FPH), and three hydrolysis conditions were selected based on PCA evaluation. The amino acids profile, FTIR and AChE inhibition kinetics were evaluated. Results showed a mixed type of inhibition behavior and, the docking molecular analyzes suggest that the inhibition AChE occurred due to the basic amino acids, mainly by arginine.
Autores principais:Moreira, Thaysa Fernandes Moya
Outros Autores:Pessoa, Luiz Gustavo Antunes; Seixas, Flávio Augusto Vicente; Ineu, Rafael P.; Gonçalves, Odinei Hess; Leimann, Fernanda Vitória; Ribeiro, Ricardo Pereira
Assunto:Fish protein hydrolysates Enzymatic hydrolysis Experimental design Acetylcholinesterase
Ano:2022
País:Portugal
Tipo de documento:artigo
Tipo de acesso:acesso aberto
Instituição associada:Instituto Politécnico de Bragança
Idioma:inglês
Origem:Biblioteca Digital do IPB

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