Zhongqiu Hu

There are currently no FDA-approved drugs for the treatment of alcohol-related liver diseases (ALD) due to their lack of effectiveness. Selenium-modified Lycium barbarum polysaccharides (SeLBP), as a promising agent for ALD, has not been studied before. In this study, with LBP and sodium selenite (Na₂SeO₃) as controls, and silymarin capsules, a clinical therapeutic agent, as a positive control, the therapeutic effects and mechanisms of SeLBP on ALD were systematically evaluated in an acute ALD mouse model. The results demonstrated that SeLBP, at the same dose, showed superior therapeutic effects on ALD compared to the use of LBP or Na₂SeO₃ alone, exhibiting a significant dose-response effect and significantly reversing alcohol-induced liver cell damage and inflammation (p < 0.05). Furthermore, 5.7 mg/kg BW of SeLBP demonstrated comparable efficacy to 50 mg/kg BW of silymarin (p > 0.05), highlighting a low-dose advantage. Mechanistic studies revealed that SeLBP significantly enhanced the activities of ADH and ALDH (p < 0.05) and significantly inhibited the activity and expression levels of cytochrome P450 2E1 (CYP2E1) and NADPH oxidase (NOX) that produce reactive oxygen species (ROS) (p < 0.05), thereby reducing ROS generation and restoring redox homeostasis (p < 0.05). Additionally, SeLBP significantly decreased the elevated levels of TG, TC, MDA, AST, and ALT caused by alcohol, while enhancing the activities of GSH-Px and SOD (p < 0.05), highlighting SeLBP's significant functions in promoting the normal metabolism of ethanol and preventing lipid peroxidation and oxidative damage. This study provides new insights and evidence for the potential use of SeLBP in ALD treatment.

To address the poor thermal stability and excessive reliance on sucrose of high-methoxy citrus pectin (HM-CP) hydrogels, this study investigated the characteristics and mechanism of curdlan gum (CG) as a sucrose substitute in binary hydrogels with various HM-CP/CG ratios. Results demonstrated that increasing the CG proportion significantly enhanced the rheological properties, hardness, gumminess, chewiness, thermal stability, and water-holding capacity of the hydrogels at a concentration of 7%. Among the tested proportions, the optimal 7% HM-CP/CG-2:8 binary hydrogel had the highest gelation temperature at 62.46 °C and the highest hardness at 245.11 g. Moreover, the hydrogel exhibited optimal gel properties, with the dense and uniform three-dimensional network structure primarily attributed to intermolecular hydrogen bonding. Application tests confirmed that the optimal binary hydrogel can be successfully used to produce gummy candies with improved textural and sensory characteristics, providing a theoretical basis for the application of HM-CP and CG in food products.

Diosgenin is an important raw material used in the synthesis of steroid drugs, and it is widely used in the pharmaceutical industry. The traditional method of producing diosgenin is through using raw materials provided via the plant Dioscorea zingiberensis C. H. Wright (DZW), which is subsequently industrially hydrolyzed using a high quantity of hydrochloric and sulfuric acids at temperatures ranging from 70 °C to 175 °C. This process results in a significant amount of unmanageable wastewater, creates issues of severe environmental pollution and consumes high quantities of energy. As an alternative, the enzymolysis of DZW to produce diosgenin is an environmentally and friendly method with wide-ranging prospects for its application. However, there are still only a few enzymes that are suitable for production on an industrial scale. In this study, three new key enzymes, E1, E2, and E3, with a high conversion stability of diosgenin, were isolated and identified using an enzyme-linked-substrate autography strategy. HPLC-MS/MS identification showed that E1, a 134.45 kDa protein with 1019 amino acids (AAs), is a zinc-dependent protein similar to the M16 family. E2, a 97.89 kDa protein with 910 AAs, is a type of endo-β-1,3-glucanase. E3, a 51.6 kDa protein with 476 AAs, is a type of Xaa-Pro aminopeptidase. In addition, the method to immobilize these proteins was optimized, and stability was achieved. The results show that the optimal immobilization parameters are 3.5% sodium alginate, 3.45% calcium chloride concentration, 1.4 h fixed time, and pH 8.8; and the recovery rate of enzyme activity can reach 43.98%. A level of 70.3% relative enzyme activity can be obtained after employing six cycles of the optimized technology. Compared with free enzymes, immobilized enzymes have improved stability, acid and alkaline resistance and reusability, which are conducive to large-scale industrial production.

The influence of water-soluble selenium-containing proteins (WSSeP) in chicken on ulcerative colitis (UC) is not known. This work aims to investigate the effect of two WSSeP including h-Se with 1.78 μg Se/g and l-Se with 1.04 μg Se/g on mice UC induced by dextran sodium sulfate (DSS) versus 5-aminosalicylic acid (5-ASA). Seventy C57BL/6 mice were randomly divided into seven groups: groups 1 and 7 were given normal saline. Group 2 to group 4 were administrated orally 500, 1500, and 3000 mg/kg/day h-Se, respectively. Group 5 was given 1500 mg/kg/day l-Se as the control of group 3. From day 14 to day 21, groups 2 to 7 were fed with 3% DSS. Synchronously, group 6 was fed with 150 mg/kg/day 5-ASA. On day 21, the disease activity index, colon length, the histopathological changes, the expressions of claudin-1, occludin, ZO-1, TLR4, and MyD88 in colons, the levels of inflammatory cytokines (IFN-γ, IL-1β, IL-6, TNF-α), and antioxidant markers (LPS, GSH-Px, SOD, MDA) in serum were determined. WSSeP can effectively improve the damages of DSS to the colon, thymus, and spleen, which present protein and Se dose-dependent. 1.50 g h-Se dose can significantly promote the expression levels of claudin-1, occludin, and ZO-1, to surround crypt gland and goblet and epithelial cells and inhibit the attack of DSS, suppress TLR4/MyD88 pathway, decrease the levels of IL-1β, IL-6, TNF-α, IFN-γ, LPS, and MDA, and increase the activities of GSH-Px and SOD, which are better than those of 5-ASA. Therefore, WSSeP would be a natural and potential anti-inflammatory agent for UC.

Glucose-6-phosphate isomerase (GPI) is a highly conserved glycolytic enzyme in nature, and less information was available for GPI from hens. In this study a newly discovered selenocysteine (Sec)-containing GPI in common chicken breast meat was first isolated, purified and identified. Data about LC–MS/MS, FTIR and Se species analyses show that the molecular weight of the enzyme is 62,091 Da and only one Sec is inserted at the 403rd position in the highly conserved primary domain SIS_PGI with sugar conversion function. The enzyme shows excellent activity against hydroxyl radicals as vitamin C (Vc) in vitro. It is deduced that the Sec-containing GPI in the chicken meat may depend on Sec in its molecular structure to resist reactive oxygen species (ROS) stress produced by the accompanying biochemical reactions in cells, to protect its stability and maintain its efficient function that catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate in the critical glycolytic pathway.