Identification and in vitro Characterization of Novel Antidiabetic Peptides Released Enzymatically from Peanut Protein.
Plant Foods Hum Nutr
; 79(1): 66-72, 2024 Mar.
Article
en En
| MEDLINE
| ID: mdl-37994988
ABSTRACT
Bioactive peptides derived from proteins found in various foods provide significant health benefits, including regulating blood sugar levels by inhibiting carbohydrate-hydrolyzing enzymes. Hydrolysates of peanut protein were prepared using alcalase (AH) or trypsin (TH) to generate antidiabetic peptides with high activity against α-amylase (IC50 of 6.46 and 5.71 mg/mL) and α-glucosidase (IC50 of 6.30 and 5.57 mg/mL), as well as antiradical activity to scavenge DPPH⢠(IC50 of 4.18 and 3.12 mg/mL) and ABTSâ¢+ (IC50 of 2.87 and 2.56 mg/mL), respectively. The bioactivities of hydrolysates were greatest in the ultrafiltration-generated F3 fraction (< 3 kDa). The most active fraction was TH-F3, which was purified by gel filtration chromatography to generate sub-fractions (SF). With IC50 values of 1.05 and 0.69 mg/mL, the F3-SF8 fraction was the most effective at inhibiting the activity of α-amylase and α-glucosidase, respectively. This fraction was further purified using RP-HPLC to generate sub-subfractions (SSF), the most active of which were F3-SF8-SSF9 and SSF10. The peptide sequences F3-SF8-SSF9 and SSF10 were determined using LC-MS/MS. Two novel antidiabetic peptides with the potential to inhibit α-amylase and α-glucosidase were identified, with the sequences Asp-Trp-Arg (476.22 Da, IC50 of 0.78, and 0.35 mg/mL) and Phe-Tyr (329.15 Da, IC50 of 0.91, and 0.41 mg/mL). These results suggest that peptides derived from peanut protein are attractive natural ingredients for diabetes management applications.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Arachis
/
Hipoglucemiantes
Idioma:
En
Revista:
Plant Foods Hum Nutr
Asunto de la revista:
BOTANICA
/
CIENCIAS DA NUTRICAO
Año:
2024
Tipo del documento:
Article
País de afiliación:
China