A bioactive compound digested chia protein is capable of modulating NFκB mediated hepatic inflammation in mice fed a high-fat diet.

The consumption of diets high in saturated fat can induce damages in liver morphology and function, which leads to increased inflammation, oxidative stress, and hepatic steatosis. Chia seed (Salvia hispanica L.) is rich in protein, which provides bioactive peptides with potential benefits, including antioxidant and anti-inflammatory functions. Then, this study aimed to analyze the effect of digested total protein (DTP) of chia on inflammation, oxidative stress, and morphological changes in liver of C57BL/6 mice fed a diet rich in saturated fat. Male C57BL/6 mice (n = 8/group), 8 weeks old, were fed standard diet (AIN), high-fat diet (HF), standard diet added digested protein (AIN + DTP) or high-fat diet added digested protein (HF + DTP) for 8 weeks. In animals fed a high-fat diet, chia DTP was able to reduce weight gain, food efficiency ratio and hepatosomatic index. In addition, it presented antioxidant capacity, which reduced catalase activity and lipid peroxidation. DTP was also able to reduce hepatic inflammation by reducing p65-NFκB expression and IL-1ß expression and quantification. The APSPPVLGPP peptide present in chia DTP presented binding capacity with PPAR-α, which contributed to the reduction of hepatic fat accumulation evidenced by histological analysis. Thus, chia DTP improved hepatic inflammatory and histological parameters, being an effective food in reducing the liver damage caused by a high-fat diet.

Assessment of the DPP-IV inhibitory activity of a novel octapeptide derived from rapeseed using Caco-2 cell monolayers and molecular docking analysis.

The Octapeptide ELHQEEPL, which was identified from the rapeseed protein napin showed prominent Dipeptidyl peptidase-IV (DPP-IV) inhibitory activity. The objective of this study was to investigate the DPP-IV inhibitory activity and transepithelial transport of ELHQEEPL in an approaching intestinal condition using Caco-2 cell monolayers. ELHQEEPL and its degraded fragments EL, HQEEP, and methylated ELHQEEPL were transported across Caco-2 cell monolayers through different pathways. Compared with the nonbiological enzyme inhibition test, the in vitro experiment on Caco-2 cell monolayers showed that the IC50 value of DPP-IV inhibition increased by 43.11% for ELHQEEPL. There was no significant change in DPP-IV gene expression in the Caco-2 cell monolayers upon treatment with ELHQEEPL. Furthermore, molecular docking predicted that the weaker binding between inhibitory peptide and enzyme for the degradation products from ELHQEEPL during transepithelial transport greatly limited its role in inhibiting DPP-IV. PRACTICAL APPLICATIONS: The DPP-IV inhibitory activity of ELHQEEPL was confirmed using Caco-2 cell monolayers as a novel assessment tool, although its potency was reduced by metabolic degradation. In general, this study reported the use of Caco-2 cell monolayers as a tool for comprehensively studying peptides as sources of DPP-IV inhibitors. A Caco-2 cell-based approach with molecular docking can be adapted for the investigation of intestinal absorption and activity attenuation of food peptides being considered for enzymatic action. Moreover, since the Caco-2 cells express a wide range of enzymes, this method can be used for screening for other active food peptides such as for the inhibitors of ACE and a-glucosidase.

Lunasin promotes apoptosis in human colon cancer cells by mitochondrial pathway activation and induction of nuclear clusterin expression.

Lunasin is a naturally occurring peptide with arginine-glycine-aspartic acid motif associated to its reported biological activity. We aimed to determine the potential of lunasin from soybean to stimulate apoptosis in HT-29 colon cancer cells. Lunasin caused cytotoxicity to HT-29 cells and induced G2/M cell cycle arrest with simultaneous increased in p21 expression. Lunasin-induced apoptosis as evidenced by a twofold increase in the percentage of cells undergoing apoptosis, decreased Bcl-2:Bax ratio from 8.5 to 0.4, increased caspase-3 activity by 77% and increased expression of pro-apoptotic nuclear clusterin by five fold when compared to untreated cells. In conclusion, lunasin stimulated apoptosis in HT-29 cells by activating apoptotic mitochondrial pathways and inducing expression of the pro-apoptotic nuclear clusterin.

Calidad proteínica de tres cepas mexicanas de setas (Pleurotus ostreatus) / Protein quality of Mexican Pleurotus ostreatus strains

Se evaluó la calidad proteínica de los cuerpos fructíferos de tres cepas mexicanas de Pleurotus ostreatus (INIREB-8, CDBB-H-896 y CDBB-H-897), cultivadas en invernadero, temperatura registrada de: 22-28 grados Celsius y 75-85 por ciento de humedad relativa, en paja de trigo como substrato. La concentración de proteína (Nx4.38), osciló entre 17.26 y 19.97 g/100g en peso seco. Sus puntajes químicos estuvieron entre 74 a 93 por ciento la lisina disponible el primer aminoácido limitante para las cepas INIREB-8 y CDBB-H-896 y la leucina para la CDBB-H-897. Los valores de digestibilidad in vitro fueron de: 67.75-68.38 por ciento. El valor protínico relativo varió de 100.06 a 107.85 por ciento, siendo menor que el del frijol soya cocido y huevo entero; e iguales estadísticamente a los de la leche descremada en polvo, caseína más metionina y albúmina; y superiores a los del arroz, maíz, frijol, lenteja, haba y pasta para sopa. En función de lo anterior se puede concluir que por su contenido de aminoácidos esenciales, las proteínas de las setas (especialmente la cepa INIREB-8) se complementan adecuadamente con la de los cereales, por lo cual es altamente recomendable incluirlas en la dieta diaria.