Controlling the amount of MoSe2 loaded SrTiO3 to activate peroxymonosulfate for efficient elimination of organic pollutants.

It is critical to effectively eliminate recalcitrant organic pollutants from wastewater. In this paper, the MoSe2/SrTiO3 (MST) catalysts were synthesized through simply controlling the amount of MoSe2 in the hydrothermal method to activate peroxymonosulfate (PMS) for the degradation of pollutants. The results demonstrated that sulfamethoxazole and tetracycline were almost eliminated by PMS/MST-3 (MoSe2/SrTiO3 mass ratio 0.3: 1) activation system. The effect of inorganic anions (Cl -, H2PO4 -, HCO3 -) and metal ions (Cu2+, Ni2+, Zn2+) commonly found in actual water bodies on catalytic reaction was explored. Moreover, SO4• -, •OH and 1O2 were identified by EPR tests and scavenger experiments, where the SO4• - and •OH were the dominant reactive species. The XPS analysis indicated that the oxygen vacancies and charge transfer on the catalyst surface were the keys of PMS activation. The effect of active sites in SMX and TC on the catalytic degradation activity was explored by density functional theory, and it was obtained that the central nitrogen site of SMX was more vulnerable in the catalytic system, while the edge oxygen site of TC was more susceptible to attack.

[Construction and culture condition optimization of a Saccharomyces cerevisiae strain for production of galactitol].

Galactitol, a rare sugar alcohol, has promising potential in the food industry and pharmaceutical field. The available industrial production methods rely on harsh hydrogenation processes, which incur high costs and environmental concerns. It is urgent to develop environmentally friendly and efficient biosynthesis technologies. In this study, a xylose reductase named AnXR derived from Aspergillus niger CBS 513.88 was identified and characterized for the enzymatic properties. AnXR exhibited the highest activity at 25 ℃ and pH 8.0, and it belonged to the NADPH-dependent aldose reductase family. To engineer a strain for galactitol production, we deleted the galactokinase (GAL1) gene in Saccharomyes cerevisiae by using the recombinant gene technology, which significantly reduced the metabolic utilization of D-galactose by host cells. Subsequently, we introduced the gene encoding AnXR into this modified strain, creating an engineered strain capable of catalyzing the conversion of D-galactose into galactitol. Furthermore, we optimized the whole-cell catalysis conditions for the engineered strain, which achieved a maximum galactitol yield of 12.10 g/L. Finally, we tested the reduction ability of the strain for other monosaccharides and discovered that it could produce functional sugar alcohols such as xylitol and arabinitol. The engineered strain demonstrates efficient biotransformation capabilities for galactitol and other functional sugar alcohols, representing a significant advancement in environmentally sustainable production practices.

Protein engineering of transaminase facilitating enzyme cascade reaction for the biosynthesis of azasugars.

Azasugars, such as 1-deoxynojirimycin (1-DNJ), exhibit unique physiological functions and hold promising applications in medicine and health fields. However, the biosynthesis of 1-DNJ is hindered by the low activity and thermostability of the transaminase. In this study, the transaminase from Mycobacterium vanbaalenii (MvTA) with activity toward d-fructose was engineered through semi-rational design and high-throughput screening method. The final mutant M9-1 demonstrated a remarkable 31.2-fold increase in specific activity and an impressive 200-fold improvement in thermostability compared to the wild-type enzyme. Molecular dynamics (MD) simulations revealed that the mutation sites of H69R and K145R in M9-1 played crucial roles in the binding of the amino acceptor and donor, leading to the stable conformation of substrates within the active pocket. An enzyme cascade reaction was developed using M9-1 and the dehydrogenase from Paenibacillus polymyxa (GutB1) for the production of mannojirimycin (MJ), which provided a new idea for the in vitro biosynthesis of 1-DNJ.

Three Licorice Extracts' Impact on the Quality of Fresh-Cut Sweet Potato (Ipomoea batatas (L.) Lam) Slices.

The quality of fresh-cut produce, particularly sweet potatoes, is crucial for their value. Licorice extract is an optional additive in fresh-cut sweet potatoes. This study examined the impact of three licorice extracts (licorice acid, LA; licorice flavonoids, LF; and licorice polysaccharides, LP) on the quality of fresh-cut sweet potato slices (FCSPSs) for one week of storage. After one week of storage, the extracts showed varying effects on FCSPSs. LA and LF treatments reduced the area proportion of browning (APB), while LP treatments increased APB and decreased L* values. Antioxidant experiments revealed that LP treatments increased PPO and POD activity while reducing SOD activity. The concentrations of the three licorice extracts showed a strong negative correlation with SOD activity. In conclusion, LP harmed the appearance and antioxidant qualities of FCSPSs. LA and LF may be suitable additive components for FCSPSs, and 30 mg/mL LA and LF treatments were found to maintain the appearance and texture quality of FCSPSs during storage. Therefore, careful consideration should be given when using LP as a food additive for FCSPSs.

Pharmacological suppression of the OTUD4/CD73 proteolytic axis revives antitumor immunity against immune-suppressive breast cancers.

Despite widespread utilization of immunotherapy, treating immune-cold tumors remains a challenge. Multiomic analyses and experimental validation identified the OTUD4/CD73 proteolytic axis as a promising target in treating immune-suppressive triple negative breast cancer (TNBC). Mechanistically, deubiquitylation of CD73 by OTUD4 counteracted its ubiquitylation by TRIM21, resulting in CD73 stabilization inhibiting tumor immune responses. We further demonstrated the importance of TGF-ß signaling for orchestrating the OTUD4/CD73 proteolytic axis within tumor cells. Spatial transcriptomics profiling discovered spatially resolved features of interacting malignant and immune cells pertaining to expression levels of OTUD4 and CD73. In addition, ST80, a newly developed inhibitor, specifically disrupted proteolytic interaction between CD73 and OTUD4, leading to reinvigoration of cytotoxic CD8+ T cell activities. In preclinical models of TNBC, ST80 treatment sensitized refractory tumors to anti-PD-L1 therapy. Collectively, our findings uncover what we believe to be a novel strategy for targeting the immunosuppressive OTUD4/CD73 proteolytic axis in treating immune-suppressive breast cancers with the inhibitor ST80.