As the focus on green chemistry intensifies, researchers are progressively looking to incorporate biodegradable and environmentally friendly solvents. Given the prevalent use of inorganic solvents in conventional methods for detecting selenium content, this study utilized a mixture design approach to create four deep eutectic solvents (DESs). The elements of the DESs consisted of six different compounds: guanidine hydrochloride, fructose, glycerol, citric acid, proline, and choline chloride. The synthesized deep eutectic solvents (DESs) exhibited a uniform and transparent appearance. The ideal ratios for each DES were established based on their density and viscosity measurements, leading to the formulations of DES1 (34% guanidine hydrochloride, 21% fructose, 45% water), DES2 (23% guanidine hydrochloride, 32% glycerol, 45% water), DES3 (27.5% citric acid, 27.5% proline, 45% water), and DES4 (30% choline chloride, 25% citric acid, 45% water). The characterization of the deep eutectic solvents (DESs) was performed using nuclear magnetic resonance (NMR) spectroscopy and infrared (IR) spectroscopy, which confirmed the molecular formation of each DES. Following this, the DESs were applied as extraction solvents in a process involving ultrasonic-assisted microextraction (UAE) combined with inductively coupled plasma mass spectrometry (ICP-MS) to assess the selenium levels in selenium-rich rice. The results were benchmarked against traditional microwave-assisted acid digestion (TM-AD), revealing selenium recovery rates ranging from 85.5% to 106.7%. These results indicate that UAE is an effective method for extracting selenium from selenium-rich rice, thereby establishing a solid data foundation for the environmentally friendly analysis of selenium content in rice.

Collagen and its peptides exhibit remarkable antioxidant activity, superior biocompatibility, and water solubility, making them a significant research focus in skin care. Hence, the recombinant humanized collagen types I, III, and XVII complexed with niacinamide were developed to address damage in human foreskin fibroblasts (HFF-1) caused by ultraviolet radiation and to evaluate basement membrane proteins in a rat skin model. The Cell Counting Kit-8 (CCK-8) assay showed that higher concentrations of the complex increased the survival of damaged cells by approximately 10% and 22%, respectively, compared to the normal group after 16 and 48 h of treatment. Further biochemical analyses using ELISA and immunofluorescence (IF) confirmed that the complex enhanced the expression of collagen type IV, laminin, P63, and transforming growth factor-β (TGF-β) in the damaged cells. Additionally, the complex boosted the activity of the basement membrane in rat skin and stimulated the secretion of integrin, laminin, and perlecan. Overall, the recombinant humanized collagen complex effectively reinforced the skin’s basement membrane.

The fibrinolytic kinase identified in the nereid worm (Perinereis aibuhitensis Grub) displays exceptional kinase activity, stability, and specificity, suggesting its potential as a promising candidate for the advancement of new thrombolytic drugs. In this study, a process was optimized for the production of fibrinolytic kinase using Escherichia coli, and the effects of factors such as inoculum, pH, OD, temperature, inducer concentration, and time on the protein yield were investigated. The optimum points of key parameters were determined by single-factor experiments, and the initial pH, OD, and time were determined to be significant by PB (Plackett–Burman design) with six factors at two levels of experiments. The response surface experiments highlighted the key roles of initial pH and induced OD values, and the convergence of the model and experimental data confirmed the optimal conditions and reasonable fluctuation intervals, which proved the reliability of the model.

As an essential thrombolytic agent, the tissue plasminogen activator receives increasing attention due to its longer half-life, lower immunogenicity, and easier administration, which are superior to other thrombolytic agents. In this study, the isolated and purified plasminogen activator from the sandworm (Perinereis aibuhitensis) was expressed in E. coli (Escherichia coli) to investigate its potential for simplifying the development process. The sandworm plasminogen activator was previously successfully cloned and expressed in E. coli with low yield and activity in the culture supernatant. This low yield and activity prompted us to optimize its DNA sequence. Furthermore, to raise the efficiency in the separation of the target protein, the protein’s solubility was enhanced by fusing it with maltose-binding protein (MBP) tags. Eventually, the fibrinolytic activity was successfully restored after digestion with tobacco etch virus (TEV) protease. This study provides an innovative method of efficiently expressing and purifying plasminogen activators from sandworm in E. coli and broadens its applications in therapeutic treatment of cardiovascular diseases, including thrombosis, stroke, and coronary atherosclerotic heart disease.