Autor(es): Moreira, Thaysa F. M. ; Oliveira, Anielle ; Rodrigues, Vanessa de Carvalho ; Carvalho, Amarilis Santos ; Quichaba, Michely B. ; Peron, Ana P. ; Gonçalves, Odinei Hess ; Gozzo, Angela M. ; Leimann, Fernanda Vitória ; Ribeiro, Ricardo P.
Data: 2024
Identificador Persistente: http://hdl.handle.net/10198/30281
Origem: Biblioteca Digital do IPB
Assunto(s): Enzymatic hydrolysis; Food application; Homogenization; Pre-treatment; Sterilization
Thermal and mechanical treatments may affect the structure of hydrolyzed proteins, thus influencing the obtaining of peptides with improved bioactivity. In this work, tila- pia muscle was treated by thermal sterilization or homogenization with ultra-turrax (UT) and hydrolyzed with alcalase to obtain FPHs with antioxidant properties in salad dressing. To evaluate the bioactive potential of FPHs, the acetylcholinesterase inhibi- tion assay was applied, resulting in up to 45.87% inhibition for the UT sample (60 mg/mL). Also, no cytotoxicity was detected by Allium cepa model for all FPHs. The emulsifying activity index and emulsifying stability index of FPHs indicated better emulsifying capacity in basic pH. As a proof of concept, FPHs were used as an emulsi- fying/antioxidant agent to prepare a salad dressing. FPHs increased the formulation's protein content, pseudoplastic behavior, color, and texture. In addition, FPHs aided the oxidative stability of salad dressing (evaluated by oil's extinction coefficient), dem- onstrating potential application in emulsified foods by acting on the elimination of radicals generated in lipid oxidation. Practical applications Fish protein hydrolysates (FPHs) offer diverse bioactive properties such as antioxi- dant, antimicrobial, anticancer, antihypertensive, and acetylcholinesterase (associated with Alzheimer's disease) inhibitory effects. However, optimizing their technological properties poses a challenge, affecting applicability and bioactivity. Industrial pro- cesses such as thermal and mechanical treatments can alter protein structures, influencing peptide bioactivity post enzymatic hydrolysis. This study investigates the impact of substrate pre-treatments, sterilization via thermal heating, and homogeniza- tion using a rotor-stator system (ultra-turrax) on FPHs' technological properties after hydrolysis with alcalase, including emulsifying capacity and acetylcholinesterase inhibitory capacity. In addition, it explores the application of pre-treated FPHs in a real food system (French salad dressing), assessing rheological properties, texture, and oxidative stability. Such evaluations are crucial for ensuring the feasibility of industrial FPHs production and their application.
