Inhibitory effects of oat peptides on lipolysis: A physicochemical perspective.
Contact angle
Emulsion stability
Lipase inhibition
Lipid digestion
Proteomics
Rheological properties
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
01 Dec 2022
01 Dec 2022
Historique:
received:
12
01
2022
revised:
21
05
2022
accepted:
28
06
2022
pubmed:
17
7
2022
medline:
30
8
2022
entrez:
16
7
2022
Statut:
ppublish
Résumé
Studies on the control of lipid digestion by food-derived active substances have prioritized the direct inhibition of lipase, ignoring the influence of these substances on the stability of bile salt (BS)-stabilized oil emulsions, which are essential for the hydrolysis of triglycerides by lipase. This study aimed to demonstrate the inhibitory potential of oat peptides (OPs) on lipolysis due to lipase inhibition, in particular, the physicochemical destruction of BS-stabilized emulsions. OPs were characterized by an enterostatin-like X-Pro-Y-Pro-Arg terminal sequence, competitively and/or noncompetitively inhibited lipase, and even caused lipase conformational changes. Interestingly, OPs destabilized BS-stabilized emulsions by weakening the rheological cross-linking structure of the emulsions through competitive hydrophobic binding to BS. Further analysis revealed that the H-bond binding of OP to BS significantly destroyed the hydrophilic and lipophilic balance of BS by increasing the surface hydrophobicity. These findings provided novel insights into the action mechanism of bioactive peptides on lipid digestion.
Identifiants
pubmed: 35841683
pii: S0308-8146(22)01583-7
doi: 10.1016/j.foodchem.2022.133621
pii:
doi:
Substances chimiques
Bile Acids and Salts
0
Emulsions
0
Peptides
0
Triglycerides
0
Lipase
EC 3.1.1.3
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
133621Informations de copyright
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