Pingyin Rose Essential Oil Restores Intestinal Barrier Integrity in DSS-induced Mice Colitis Model.

Rosa rugosa cv. Plena is a 'drug homologous food' in China with a long history. Pingyin rose essential oil (PREO) is a mixture of compounds extracted from blooming R. rugosa cv. Plena. With its elegant smell and excellent effects on oxidative stress and inflammation alleviation, PREO is wildly used in the food industry as a popular additive. We aimed to decipher if the PREO could alleviate and restore dextran sodium sulfate (DSS)-induced barrier integrity damages. The results showed that a 7-day PREO (15 µL/kg) treatment alleviated the colitis symptoms by improving disease activity index (DAI) scores through weight loss, occult blood, and colon shortening. The expression of tight junction proteins and the enzyme activities of superoxide dismutases (SOD), and catalase (CAT) increased while nitric oxide (NO), malondialdehyde (MDA), and myeloperoxidase (MPO) production decreased in PREO-treated C57BL6 female mice. PREO treatment inhibited the expression of pro-inflammatory cytokines tumor necrosis factor (TNF-α), interleukin (IL)-1ß, and IL-6. Further, PREO modulated the composition of the gut microbiota and Spearman's correlation analysis revealed a positive effect. The transcriptome analysis and western blot results indicated that PREO might ameliorate intestinal barrier dysfunction in this study via the TLR4-NF-kB signaling pathway. We hypothesized that PREO has preventive potential against gut disorders and could serve as a functional food additive.

Quantitative Modeling of the Degradation of Pesticide Residues in Wheat Flour Supply Chain.

Pesticide residues in grain products are a major issue due to their comprehensive and long-term impact on human health, and quantitative modeling on the degradation of pesticide residues facilitate the prediction of pesticide residue level with time during storage. Herein, we tried to study the effect of temperature and relative humidity on the degradation profiles of five pesticides (carbendazim, bensulfuron methyl, triazophos, chlorpyrifos, and carbosulfan) in wheat and flour and establish quantitative models for prediction purpose. Positive samples were prepared by spraying the corresponding pesticide standards of certain concentrations. Then, these positive samples were stored at different combinations of temperatures (20 °C, 30 °C, 40 °C, 50 °C) and relative humidity (50%, 60%, 70%, 80%). Samples were collected at specific time points, ground, and the pesticide residues were extracted and purified by using QuEChERS method, and then quantified by using UPLC-MS/MS. Quantitative model of pesticide residues was constructed using Minitab 17 software. Results showed that high temperature and high relative humidity accelerate the degradation of the five pesticide residues, and their degradation profiles and half-lives over temperature and relative humidity varied among pesticides. The quantitative model for pesticide degradation in the whole process from wheat to flour was constructed, with R2 above 0.817 for wheat and 0.796 for flour, respectively. The quantitative model allows the prediction of the pesticide residual level in the process from wheat to flour.

Inhibition of Three Diabetes-Related Enzymes by Procyanidins from Lotus (Nelumbo nucifera Gaertn.) Seedpods.

The inhibitory effects of procyanidins from lotus (Nelumbo nucifera Gaertn.) seedpods on the activities of α-amylase, α-glucosidase and protein tyrosine phosphatase 1B (PTP1B), were studied and compared with those of (+)-catechin, (-)-epicatechin, epigallocatechin gallate (EGCG), procyanidin dimer B2 and trimer C1. The results showed that Lotus procyanidin extract (LPE) significantly inhibited α-amylase, α-glucosidase and PTP1B with IC50 values of 5.5, 1.0, and 0.33 µg/mL, respectively. The inhibition increased with the degree of polymerization and the existence of galloyl or gallocatechin units. Kinetic analysis showed that LPE inhibited α-glucosidase activity in a mixed competitive and noncompetitive mode. Fluorescence quenching revealed that α-glucosidase interacted with LPE or EGCG in an apparent static mode, or the model of "sphere of action". The apparent static (K) and bimolecular (kq) constants were 4375 M-1 and 4.375 × 1011 M-1 s-1, respectively, for LPE and 1195 M-1 and 1.195 × 1011 M-1 s-1, respectively, for EGCG. Molecular docking analysis provided further information on the interactions of (+)-catechin, (-)-epicatechin, EGCG, B2 and C1 with α-glucosidase. It is hypothesized that LPE may bind to multiple sites of the enzyme through hydrogen bonding and hydrophobic interactions, leading to conformational changes in the enzyme and thus inhibiting its activity. These findings first elucidate the inhibitory effect of LPE on diabetes-related enzymes and highlight the usefulness of LPE as a dietary supplement for the prophylaxis of diabetes.