This study analyzed the thermostability and effect of calcium ions on the enzymatic activity of α-amylase produced by Bacillus licheniformis strain LB04 isolated from Espinazo Hot springs in Nuevo Leon, Mexico. The enzyme was immobilized by entrapment on agar-agarose beads, with an entrapment yield of 19.9%. The identification of the bacteria was carried out using 16s rDNA sequencing. The enzyme was purified through ion exchange chromatography (IEX) in a DEAE-Sephadex column, revealing a protein with a molecular weight of ≈130 kDa. The enzyme was stable at pH 3.0 and heat stable up to 80 °C. However, the optimum conditions were reached at 65 °C and pH 3.0, with a specific activity of 1851.7 U mg⁻¹ ± 1.3. The agar-agarose immobilized α-amylase had a hydrolytic activity nearly 25% higher when compared to the free enzyme. This study provides critical information for the understanding of the enzymatic profile of B. licheniformis strain LB04 and the potential application of the microorganisms at an industrial level, specifically in the food industry.

Chlorophene is an important antimicrobial agent present in disinfectant products which has been related to health and environmental effects, and its detection has been limited to chromatographic techniques. Thus, there is a lack of research that attempts to develop new analytical tools, such as biosensors, that address the detection of this emerging pollutant. Therefore, a new biosensor for the direct detection of chlorophene in real water is presented, based on surface plasmon resonance (SPR) and using a laccase enzyme as a recognition element. The biosensor chip was obtained by covalent immobilization of the laccase on a gold-coated surface through carbodiimide esters. The analytical parameters accomplished resulted in a limit of detection and quantification of 0.33 mg/L and 1.10 mg/L, respectively, fulfilling the concentrations that have already been detected in environmental samples. During the natural river’s measurements, no significant matrix effects were observed, obtaining a recovery percentage of 109.21% ± 7.08, which suggested that the method was suitable for the fast and straightforward analysis of this contaminant. Finally, the SPR measurements were validated with an HPLC method, which demonstrated no significant difference in terms of precision and accuracy, leading to the conclusion that the biosensor reflects its potential as an alternative analytical tool for the monitoring of chlorophene in aquatic environments.

Glycine, a simple amino acid, is not only essential due to its potential insufficiency in vivo, but also has significant metabolic functions. It serves as a crucial building block for proteins. At the same time, as a bioactive molecule, it regulates gene expression for cytoprotection, protein configuration and activity, and other critical biological processes, including glutathione synthesis. The intriguing, beneficial effects of glycine in medical applications have piqued the research community’s interest in recent decades. This work delves into the compelling discoveries about the pivotal role of glycine in cardiovascular health and its intricate mechanisms of action for alleviating several medical conditions. Glycine’s broad spectrum of impact spans numerous diseases, encompassing not only acute myocardial infarction, aortic dissection, and cardiac hypertrophy, but also transplant rejections of aortic allografts, insulin resistance, and endothelial dysfunction, thereby providing a comprehensive understanding of its medical applications.

This research investigates the biosynthesis optimization of the red pigment prodigiosin produced by Serratia marcescens 11E through submerged fermentation utilizing an alternative cheese whey-based medium, focusing on process parameters and antimicrobial properties. Four types of whey sourced from a local dairy industry were characterized, and the fermentation conditions were optimized using Plackett–Burman and central composite design methodologies, yielding up to 1.43 g/L of prodigiosin under optimal conditions, 25 °C, 200 rpm, pH 7, and 48 h of dark incubation, with whey serving as the sole carbon source. Normalization to biomass yielded 110 mg of prodigiosin per gram of dried cell weight (post-optimization), enabling meaningful comparison with prior studies. Pigment extraction was performed with acidic methanol, and identity was confirmed by UV–Vis spectrophotometry and Fourier transform infrared spectroscopy (FTIR). The antimicrobial activity of the purified pigment was also evaluated. Although cheese whey has significant nutritional value, nearly half of the global production is discarded due to high treatment costs. This study demonstrates that whey can be repurposed as a sustainable and economical fermentation medium for pigment production, which is compatible with dairy plants. This makes it a promising solution to address the underutilization of whey by cheese local producers in Mexico. Prodigiosin has diverse industrial applications, including antimicrobial, insecticidal, and antioxidant properties. These findings highlight the potential for dairy waste valorization in a circular bioeconomy, reducing environmental impacts and promoting the creation of valuable bioproducts.