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Dipeptidyl Peptidase IV Inhibitory Peptides Derived from Oat (Avena sativa L.), Buckwheat (Fagopyrum esculentum), and Highland Barley (Hordeum vulgare trifurcatum (L.) Trofim) Proteins.
Wang, Feng; Yu, Guoyong; Zhang, Yanyan; Zhang, Bolin; Fan, Junfeng.
Afiliación
  • Wang F; Department of Food Science and Engineering, College of Biological Sciences and Technology, Beijing Key Laboratory of Forest Food Process and Safety, Beijing Forestry University , Beijing 100083, China.
  • Yu G; Department of Food Science and Engineering, College of Biological Sciences and Technology, Beijing Key Laboratory of Forest Food Process and Safety, Beijing Forestry University , Beijing 100083, China.
  • Zhang Y; Food Science and Engineering College, Beijing University of Agriculture , Beijing 102206, China.
  • Zhang B; Department of Food Science and Engineering, College of Biological Sciences and Technology, Beijing Key Laboratory of Forest Food Process and Safety, Beijing Forestry University , Beijing 100083, China.
  • Fan J; Department of Food Science and Engineering, College of Biological Sciences and Technology, Beijing Key Laboratory of Forest Food Process and Safety, Beijing Forestry University , Beijing 100083, China.
J Agric Food Chem ; 63(43): 9543-9, 2015 Nov 04.
Article en En | MEDLINE | ID: mdl-26468909
Peptides released from oat, buckwheat, and highland barley proteins were examined for their in vitro inhibitory effects on dipeptidyl peptidase IV (DPP4), an enzyme that deactivates incretin hormones involved in insulin secretion. All of the hydrolysates exhibited DPP4 inhibitory activities, with IC50 values ranging from 0.13 mg/mL (oat glutelin alcalase digestion) to 8.15 mg/mL (highland barley albumin tryptic digestion). The lowest IC50 values in gastrointestinal, alcalase, and tryptic digestions were 0.99 mg/mL (oat flour), 0.13 mg/mL (oat glutelin), and 1.83 mg/mL (highland barley glutelin). In all, 35 peptides of more than seven residues were identified in the tryptic hydrolysates of oat globulin using liquid chromatography-mass spectroscopy. Peptides LQAFEPLR and EFLLAGNNK were synthesized and their DPP4 inhibitory activities determined. LQAFEPLR showed high in vitro DPP4 inhibitory activity with an IC50 value of 103.5 µM.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Péptidos / Proteínas de Plantas / Hordeum / Extractos Vegetales / Avena / Fagopyrum / Inhibidores de la Dipeptidil-Peptidasa IV Idioma: En Revista: J Agric Food Chem Año: 2015 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Péptidos / Proteínas de Plantas / Hordeum / Extractos Vegetales / Avena / Fagopyrum / Inhibidores de la Dipeptidil-Peptidasa IV Idioma: En Revista: J Agric Food Chem Año: 2015 Tipo del documento: Article País de afiliación: China