Production, characterisation, and biological properties of Tenebrio molitor-derived oligopeptides.
Food Chem
; 450: 139400, 2024 Aug 30.
Article
en En
| MEDLINE
| ID: mdl-38640536
ABSTRACT
Three protein hydrolysates from Tenebrio molitor were obtained by enzymatic hydrolysis employing two food-grade proteases (i.e. Alcalase and Flavourzyme), and a complete characterisation of their composition was done. The digestion-derived products were obtained using the INFOGEST protocol. In vitro antioxidant activity and anti-inflammatory activities were evaluated. Tenebrio molitor flour and the protein hydrolysates showed a high ability to scavenge the DPPH radical (EC50 values from 0.30 to 0.87 mg/mL). The hydrolysate obtained with a combination of the two food-grade proteases could decrease the gene expression of pro-inflammatory genes after being digested. Furthermore, the peptidome was fully determined for the first time for T. molitor hydrolysates and digests, and 40 peptides were selected based on their bioactivity to be evaluated by in silico tools, including prediction tools and molecular docking. These results provide new perspectives on the use of edible insects as sustainable and not nutritionally disadvantageous food for human consumption.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Oligopéptidos
/
Tenebrio
/
Proteínas de Insectos
/
Antioxidantes
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Food Chem
Año:
2024
Tipo del documento:
Article
País de afiliación:
España