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The role of thermally generated 3-aminopropionamide as an intermediate in acrylamide formation in the Maillard reaction has been well established. Herein, the effect of epicatechin on the conversion of 3-aminopropionamide into acrylamide under oxidative conditions was investigated at 160–220 °C. Epicatechin promoted acrylamide generation and 3-aminopropionamide degradation. The stable isotope-labeling technique combined with UHPLC-Orbitrap-MS/MS analysis showed adduct formation between 3-aminopropionamide and the oxidized B ring of epicatechin to form a Schiff base. This initially formed Schiff base could directly degrade to acrylamide, undergo reduction or dehydration to other intermediates, and subsequently generate acrylamide. Based on accurate mass analysis, five intermediates with intact or dehydrated C rings were tentatively identified. Furthermore, reaction pathways were proposed that were supported by the changes in the levels of adducts formed during heating. To the authors’ knowledge, this study is the first to reveal pathways through which flavanols promoted the formation of acrylamide in Maillard reactions.

Pea protein hydrolysates (PPHs) possess good hypoglycemic effects; however, their dipeptidyl peptidase-4 (DPP-4) inhibitory activity is poorly understood, and none of the DPP-4 inhibitory peptides have been identified from PPHs. This paper aims to rapidly screen these peptides from PPHs by combining peptidomics and molecular docking. In this study, 543 peptides were identified by peptidomics, and four peptides (IPYWTY, IPYWT, LPNYN, and LAFPGSS) with DPP-4 half-maximal inhibitory concentration (IC50) values <100 μM were screened for the first time. Significantly, peptide IPYWTY exhibited the most potent DPP-4 inhibitory activity (IC50= 11.04 μM) mainly because it formed hydrophobic interactions with the S1 pocket in DPP-4. These results indicated that combining peptidomics and molecular docking is an effective strategy for rapidly screening DPP-4 inhibitory peptides.

Soluble dietary fibers being fermented by gut microbiota constitute a pivotal prerequisite for soluble dietary fibers exhibiting physiological functions. However, the relationship between fiber type and gut microbiota metabolism remains unclear. The purpose of this study was to investigate and compare the effect of fiber types on short-chain fatty acid (SCFA) biosynthesis in a simulated colon. Results showed that different soluble dietary fibers caused distinct metabolic profiles both in SCFAs and organic acids. Further analysis revealed that the SCFA biosynthesis pathway was related to the chain structure of fiber polysaccharides. Moreover, the microbial community structure showed substantial difference among experimental groups. Parabacteroideswas substantially elevated in the resistant starch group, while Lactobacilluswas the predominant genus in other groups. Correlation analysis further revealed that SCFA biosynthesis was correlated with microbial taxa at different taxonomic levels. Totally, the present study provided an insight into targeted intervention of gut microorganisms for dictating SCFA and organic acid production.

Dipeptidyl Peptidase 4 inhibitory peptides (DPP-4IPs) could exhibit their hypoglycemic effects by preventing Glucagon-like peptide 1 (GLP-1) degradation. However, identifying DPP-4IPs by traditional approach is laborious. Therefore, this study aims to rapidly identify DPP-4IPs by an in silicomethod. After in silicodigestion, 509 peptide fragments were obtained from pea proteins. Subsequently, two novel DPP-4IPs SPGDVF and EPF with the in vitrohalf-maximal inhibitory concentrations (IC50) values of 277.61 and 406.47 μM were obtained by virtual screening and molecular docking. Interestingly, their in situDPP-4 IC50values in Caco-2 cells were increased to 918.82 and 1868.27 μM, respectively. Lineweaver−Burk double-reciprocal plots revealed that SPGDVF and EPF were competitive and mixed-type DPP-4IPs, respectively. Significantly, molecular docking suggested that SPGDVF could bond with DPP-4 active pockets. While EPF only bound outside of these active pockets, which may be the reason that EPF was weaker than SPGDVF in DPP-4 inhibition. Overall, this work provides a convenient strategy for identifying DPP-4IPs from food proteins.

This study aimed to investigate the inhibitory mechanism of epicatechin (EC) on the formation of acrylamide in Maillard reactions. The glucose + asparagine model is a typical chemical system used to investigate acrylamide formation. 5-Hydroxymethylfurfural (HMF) is an important carbonyl intermediate in Maillard reactions and can also react with asparagine to form acrylamide. Time courses showed that EC inhibited more HMF than acrylamide in the glucose + asparagine model heated at 180 °C. The reduction of EC on acrylamide formation in the HMF + asparagine model was about 70%, while that in the glucose + asparagine model was about 50%. Moreover, HMF decreased significantly faster when it was heated in the presence of EC. Liquid chromatography–mass spectrometry analysis revealed the formation of adducts between EC and HMF, and the dimeric adducts were verified in fried potato chips. These results suggested that the condensation of EC and HMF was one of the key steps leading to the inhibition of acrylamide. UV–visible spectra analysis showed that some polymerization products had absorption in the visible region and contributed to the development of browning, which was underestimated in the past.

Owing to the poor ability of cells to decompose triglycerides, most studies of edible oil have depended on animal or clinical trials. However, such trials are expensive and time-consuming, and the results are limited to considerable individual differences. This is the first study to comprehensively investigate the effect of different oils on the lipid accumulation and reactive oxygen species (ROS) production in HepG2 cells by hydrolyzing oil to fatty acids with integrated fat content. In addition, the key components of fatty acid composition, phytosterol, polyphenols, and tocopherol/tocotrienol in different oils, contributing to a decrease in content of lipid accumulation, cholesterol, ROS, and malondialdehyde (MDA), were analyzed using multivariate analysis. The results showed that the lipid accumulation content of coconut oil, Pu’er tea oil, olive oil, and flaxseed oil at a concentration of 200 μM decreased by 45.98 ± 0.75, 50.35 ± 1.37, 40.43 ± 2.44, and 42.76 ± 1.88%, respectively, compared with the lard. In addition, the ROS contents of Pu’er tea oil, olive oil, and flaxseed oil had no significant difference from that of control cells (p< 0.05). In the results, (3β,5α)-stigmastan-3-yl, cholane-5,20(22)-diene-3b-ph, and β-sitosterol were determined to be the key components in edible oils associated with lipid accumulation and ROS production.

During the freezing process, ice crystal formation leads to the deterioration in physicochemical properties and networks of gluten proteins. The cryoprotective effects of recombinant carrot (Daucus carota) antifreeze protein (rCaAFP), type II antifreeze protein from Epinephelus coioides(rFiAFP), and Tenebrio molitorantifreeze protein (rTmAFP) produced from Pichia pastorisGS115 on hydrated gluten, glutenin, and gliadin during freezing were investigated. The thermal hysteresis (TH) activity and ice crystals’ morphology modification ability of recombinant antifreeze proteins (rAFPs) were analyzed by differential scanning calorimetry (DSC) and cryomicroscope, respectively. The freezing and melting properties, water state, rheological properties, and microstructure of hydrated gluten proteins were studied by DSC, low field nuclear magnetic resonance, rheometer, and scanning electron microscopy, respectively. The rTmAFP exhibited strongest TH activity and ice crystals’ morphology modification ability, followed by rFiAFP and rCaAFP. The addition of the three rAFPs caused freezing hysteresis and weakened the damage of freezing to the networks of hydrated gluten, glutenin, and gliadin. During freezing, the cryoprotective effects of the three rAFPs on the freezable water content, water mobility and distribution, and rheological properties of hydrated gluten were achieved by protecting these corresponding properties of hydrated glutenin. Among the three rAFPs, rTmAFP was most effective in the cryoprotective activities on hydrated gluten proteins during freezing. The results demonstrate the potential of these rAFPs, especially rTmAFP, to preserve the above properties of hydrated gluten proteins during the freezing process.

Geniposide is the main bioactive constituent of gardenia fruit. Skeletal-muscle fibrosis is a common and irreversibly damaging process. Numerous studies have shown that geniposide could improve many chronic diseases, including metabolic syndrome and tumors. However, the effects of geniposide on skeletal-muscle fibrosis are still poorly understood. Here, we found that crude extracts of gardenia fruit pomace could significantly decrease the expression of profibrotic genes in vitro. Moreover, geniposide could also reverse profibrotic-gene expression induced by TGF-β and Smad4, a regulator of skeletal-muscle fibrosis. In addition, geniposide treatment could significantly downregulate profibrotic-gene expression and improve skeletal-muscle injuries in a mouse model of contusion. These results together suggest that geniposide has an antifibrotic effect on skeletal muscle through the suppression of the TGF-β–Smad4 signaling pathway.

The aim of this study was to evaluate the in situ insulinotropic effects of pea protein hydrolysates (PPHs) mediated by active glucagon-like peptide-17–36(active GLP-1) using a 2D and dual-layered coculture cell model. Following this model, a mixed Caco-2 and NCI-H716 cell monolayer was differentiated on the apical side to study the effects of PPHs on active GLP-1 levels; meanwhile, the beta-TC-6 cells were seeded on the basolateral side to investigate the insulin responses induced by active GLP-1. The in situ DPP-4 half-maximal inhibitory concentration (IC50) of PPHs, PPHs-120G, and PPHs-120I was 2.94, 3.43, and 2.26 mg/mL, respectively. They directly stimulated active GLP-1 secretion in NCI-H716 cells by 3.03 ± 0.21, 1.99 ± 0.03, and 2.24 ± 0.02 times, respectively. Insulin release in beta-TC-6 cells was directly stimulated by PPHs but not by PPHs-120G and PPHs-120I. Interestingly, PPHs-120G and PPHs-120I indirectly stimulated insulin release in this coculture cell model by enhancing active GLP-1 concentrations. More importantly, PPHs, PPHs-120G, and PPHs-120I increase active GLP-1 levels by their dual function of stimulating active GLP-1 secretion and DPP-4 inhibition. This study suggests that the 2D and dual-layered coculture cell model supports a more comprehensive assessment of in situ insulinotropic effects of protein hydrolysates mediated by active GLP-1.

There is currently no appropriate cell model suitable for evaluating the insulinotropic effects of DPP-4 inhibitory peptides (DPP-4IPs) mediated by active glucagon-like peptide-17–36(active GLP-1). The study aims to evaluate the transepithelial transport of IPYWTY on its in situinsulinotropic effects by using a 2D and dual-layered coculture cell model that consists of Caco-2 and NCI-H716 cells on the apical (AP) side and β-TC-6 cells on the basolateral (BL) side. During transportation, IPYWTY was absorbed in its intact form through PepT1 and paracellular transport. Meanwhile, it was degraded to several peptide fragments, including PYWTY, YWTY, WTY, and IPY, which decreased its in situDPP-4 inhibitory activity. IPYWTY does not directly stimulate insulin release in β-TC-6 cells, while it increased the active GLP-1 level from 76.57 ± 15.16 to 95.63 ± 1.99 pM (1.25 times) in NCI-H716 cells. Interestingly, IPYWTY indirectly increased insulin levels from 426.91 ± 6.07 to 573.94 ± 2.97 μIU/mL (1.34 times) in the 2D and dual-layered coculture cell model for its dual function of stimulating active GLP-1 secretion and DPP-4 inhibition. These results suggested that the 2D and dual-layered coculture cell model is an alternative strategy for effectively evaluating the insulinotropic effects of DPP-4IPs mediated by active GLP-1.

β-Glucan in grains has been included in almost every diet, however, biological mechanism and affecting factor of β-glucan metabolism in the gut remain unclear. In this study, we performed an in vitrofermentation experiment that was aimed at investigating the effect of gut microbial source on oat β-glucan metabolism by using mice and human fecal microbiota. It was found that, in both cases, acetate, propionate, and butyrate were the main end products from gut microbial fermentation of β-glucan. Notably, butyrate was the main product from the mice group while propionate was considered particularly enriched in the human group. β-Glucan contents at different time points were analyzed and results showed that β-glucan was nearly undetectable in the human group after 12 h of fermentation while a small amount of β-glucan was still detectable in mice group until the end of the fermentation. Further analysis of gut microbiota composition revealed that, at the genus level, Barnesiella, Holdemanella, Lactobacillus, Olsenellaand Escherichia/Shigellawere significantly enriched in the mice group whereas Bacteroides, Prevotella, Megamonas, Faecalibacteriumand Collinsellawere significantly enriched in the human group (p < 0.05). Moreover, a probable catabolic process of β-glucan was proposed. Overall, our data suggested that β-glucan could be completely hydrolyzed by human fecal microbiota but not thoroughly degraded by mice fecal microbiota. The notion shed some light on the effect of gut microbial source on β-glucan degradation, providing new information for the relationship between β-glucan metabolism and gut microbiota.

Obesity has been a main risk for the development of diabetes mellitus, cardiovascular diseases and many other chronic problems worldwide. Lifestyle modification is the best way to lose weight but very hard to implement, thus pharmacotherapy is regarded as a good add-on to dietary and lifestyle therapies. This review provides an overview of the olistat, a drug for obesity approved by FDA, about its mechanism of action, efficacy for obesity and some other diseases including cardiovascular disease, type 2 diabetes and some cancers, as well as its safety and adverse effects.