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Orientador(es)
Resumo(s)
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.
Descrição
Palavras-chave
Fish protein hydrolysates Enzymatic hydrolysis Experimental design Acetylcholinesterase
Contexto Educativo
Citação
Moreira, Thaysa Fernandes Moya; Pessoa, Luiz Gustavo Antunes; Seixas, Flavio Augusto Vicente; Ineu, Rafael Porto; Gonçalves, Odinei Hess; Leimann, Fernanda Vitória; Ribeiro, Ricardo Pereira (2022). Chemometric evaluation of enzymatic hydrolysis in the production of fish protein hydrolysates with acetylcholinesterase inhibitory activity. Food Chemistry. ISSN 0308-8146. 367, p. 1-9