RESUMEN
BACKGROUND & AIM: When considered separately, long-term immediate-release niacin and fatty meals enriched in monounsaturated fatty acids (MUFA) decrease postprandial triglycerides, but their effects on postprandial inflammation, which is common in individuals with metabolic syndrome, are less known. Moreover, successful combination is lacking and its impact on acute disorders of the innate immune cells in the metabolic syndrome remains unclear. Here, we aimed to establish the effects from combination with niacin of different fats [butter, enriched in saturated fatty acids (SFA), olive oil, enriched in MUFA, and olive oil supplemented with eicosapentaenoic (EPA) and docosahexaenoic (DHA) acids] on plasma inflammatory markers and circulating monocyte subsets, activation and priming at the postprandial period in individuals with metabolic syndrome. METHODS: A random-order within-subject crossover experiment was performed, in which 16 individuals with metabolic syndrome and 16 age-matched healthy volunteers took 2 g immediate-release niacin together with the corresponding fatty meal or a meal with no fat as control. In total, 128 postprandial curves were analysed. We sampled hourly over 6 h for plasma concentrations of soluble inflammatory markers and triglycerides. Circulating monocyte subsets (CD14/CD16 balance), activation (CCL2/CCR2 axis) and priming (M1/M2-like phenotype) at the time of postprandial hypertriglyceridemic peak were also addressed. RESULTS: Dietary SFA (combined with niacin) promote postprandial excursions of circulating IL-6, IL-1ß, TNF-α and CD14/CCR2-rich monocytes with a pro-inflammatory M1-like phenotype, particularly in individuals with metabolic syndrome. In contrast, dietary MUFA (combined with niacin) postprandially increased circulating CD16-rich monocytes with an anti-inflammatory M2-like phenotype. Omega-3 PUFA did not add to the effects of MUFA. CONCLUSION: The co-administration of a single-dose of immediate-release niacin with a fatty meal rich in MUFA, in contrast to SFA, suppresses postprandial inflammation at the levels of both secretory profile and monocyte response in individuals with metabolic syndrome. These findings highlight a potential role of combining niacin and dietary MUFA for the homeostatic control of inflammation and the innate immune system, identifying a new search direction for the management of disorders associated with the metabolic syndrome.
Asunto(s)
Síndrome Metabólico , Niacina , Masculino , Humanos , Ácidos Grasos Monoinsaturados/farmacología , Monocitos/metabolismo , Síndrome Metabólico/tratamiento farmacológico , Síndrome Metabólico/metabolismo , Grasas de la Dieta/metabolismo , Niacina/metabolismo , Aceite de Oliva , Periodo Posprandial , Ácidos Grasos/metabolismo , Triglicéridos , Inflamación/tratamiento farmacológico , Inflamación/metabolismo , ComidasRESUMEN
Dipeptidyl peptidase IV (DPP-IV) is considered a key target for the diabetes treatment, since it is involved in glucose metabolism. Although lupin protein consumption shown hypoglycemic activity, there is no evidence of its effect on DPP-IV activity. This study demonstrates that a lupin protein hydrolysate (LPH), obtained by hydrolysis with Alcalase, exerts anti-diabetic activity by modulating DPP-IV activity. In fact, LPH decreased DPP-IV activity in a cell-free and cell-based system. Contextually, Caco-2 cells were employed to identify LPH peptides that can be intestinally trans-epithelial transported. Notably, 141 different intestinally transported LPH sequences were identified using nano- and ultra-chromatography coupled to mass spectrometry. Hence, it was demonstrated that LPH modulated the glycemic response and the glucose concentration in mice, by inhibiting the DPP-IV. Finally, a beverage containing 1 g of LPH decreased DPP-IV activity and glucose levels in humans.
Asunto(s)
Diabetes Mellitus , Inhibidores de la Dipeptidil-Peptidasa IV , Lupinus , Humanos , Animales , Ratones , Lupinus/química , Células CACO-2 , Inhibidores de la Dipeptidil-Peptidasa IV/farmacología , Inhibidores de la Dipeptidil-Peptidasa IV/química , Péptidos/química , Dipeptidil Peptidasa 4/metabolismo , GlucosaRESUMEN
In this research, scallops (Argopecten purpuratus) visceral meal (SVM) and defatted meal (SVMD) were analysed for their proximal composition, protein solubility, and amino acid profile. Hydrolysed proteins isolated from the scallop's viscera (SPH) were optimised and characterised using response surface methodology with a Box-Behnken design. The effects of three independent variables were examined: temperature (30-70 °C), time (40-80 min), and enzyme concentration (0.1-0.5 AU/g protein) on the degree of hydrolysis (DH %) as a response variable. The optimised protein hydrolysates were analysed for their proximal composition, yield, DH %, protein solubility, amino acid composition, and molecular profile. This research showed that defatted and isolation protein stages are not necessaries to obtain the hydrolysate protein. The conditions of the optimization process were 57 °C, 62 min and 0.38 AU/g protein. The amino acid composition showed a balanced profile since it conforms to the Food and Agriculture Organisation/World Health Organisation recommendations for healthy nutrition. The predominant amino acids were aspartic acid + asparagine, glutamic acid + Glutamate, Glycine, and Arginine. The protein hydrolysates' yield and DH % were higher than 90% and close to 20%, respectively, with molecular weight between 1-5 kDa. The results indicate that the protein hydrolysates of scallops (Argopecten purpuratus) visceral by product optimised and characterised was suitable a lab-scale. Further research is necessary to study the bioactivity properties with biologic activity of these hydrolysates.
RESUMEN
Chickpea protein isolate was hydrolyzed using Flavourzyme immobilized on glyoxyl-agarose beads by multipoint covalent attachment. This Flavourzyme-glyoxyl derivative, produced after 1 h of immobilization at 4 °C followed by 5.5 h at room temperature, presented approximately 51% of the endoprotease activity of Flavourzyme but was around 700 times more stable than soluble enzyme. Chickpea protein hydrolysates ranging from 1% to 10% degree of hydrolysis were produced and their chemical composition was very close to that of protein isolate used as starting material. Solubility, oil absorption, emulsifying activity and stability, and foaming capacity and stability were determined. All protein hydrolysates showed higher solubility than intact proteins, especially at pHs near isoelectric point of native chickpea proteins. Moreover, all hydrolysates had better functional properties, except emulsifying activity, than the original protein isolate.