Cyclomethicone 50% / Isopropyl myristate 50% solution

Essential oils are high-valued natural extracts that are involved in industries such as food, cosmetics, and pharmaceutics. The lemon essential oil (LEO) has high economic importance in the food and beverage industry because of its health-beneficial characteristics and desired flavor properties. LEO, similar to other natural extracts, is prone to being adulterated through economic motivations. Adulteration causes unfair competition between vendors, disruptions in national economies, and crucial risks for consumers worldwide. There is a need for cost-effective, rapid, reliable, robust, and eco-friendly analytical techniques to detect adulterants in essential oils. The current research developed chemometric models for the quantification of three adulterants (orange essential oil, benzyl alcohol, and isopropyl myristate) in cold-pressed LEOs by using hierarchical cluster analysis (HCA), principal component regression (PCR), and partial least squares regression (PLSR) based on FTIR spectra. The cold-pressed LEO was successfully distinguished from adulterants by robust HCA. PLSR and PCR showed high accuracy with high R2 values (0.99–1) and low standard error of cross-validation (SECV) values (0.58 and 5.21) for cross-validation results of the raw, first derivative, and second derivative FTIR spectra. The findings showed that FTIR spectroscopy combined with multivariate analyses has a considerable capability to detect and quantify adulterants in lemon essential oil.

Abstract licence: CC BY 4.0

This study investigates the hypothesis that modified shellac nanoparticles (NPs) can effectively stabilize Pickering emulsions. Shellac, a natural polyester resin derived from the secretion of insects, was chemically modified using Jeffamine® M600 and Jeffamine® ED2003 to produce two NP types: Sh-M600 and Sh-ED2003, with sizes ranging from 127 to 183 nm. These NPs were used to stabilize oil-in-water emulsions with isopropyl myristate (IPM). Stability tests revealed that Sh-M600-stabzlized emulsions (up to 40 % oil) remained stable for 6 months, while Sh-ED2003-stabilized emulsions were stable with up to 65 % oil content, even under accelerated conditions. Cryo-SEM imaging confirmed NP accumulation at the oil-water interface, corroborated by reduced interfacial tension in the presence of NP. Adsorption energy calculations demonstrated the superior stabilization capacity of Sh-ED2003 NPs over Sh-M600 NPs. Rheological analysis further supported these findings, showing consistently higher viscosity viscosities for Sh-ED2003-stabilized emulsions across all oil percentages, attributed to the higher molecular weight of its modifier. Collectively, this study demonstrates the effectiveness of tailored shellac NPs in stabilizing robust emulsions, offering potential applications in food, pharmaceuticals, and agriculture.

Abstract licence: CC BY-NC-ND

Free enzymes often face economic problems because of their non-repeatability and variability, which limit their application in industrial production. In this study, KDN lipase was immobilized with the macroporous resin LXTE-1000 and glutaraldehyde. The optimal conditions of enzyme immobilization were defined by a single factor experiment and response surface methodology (RSM). The concentration of the cross-linking agent glutaraldehyde was 0.46% (v/v), the cross-linking temperature was 25.0 °C, and the cross-linking time was 157 min. The enzyme activity of the immobilized KDN lipase after adsorption/cross-linking was 291.36 U/g, and the recovery of the enzyme activity was 9.90%. The optimal conditions for the synthesis of isopropyl myristate were catalyzed by the immobilized KDN lipase in a solvent-free system: immobilized enzyme 53 mg, reaction temperature 36.1 °C, myristic acid 228.4 mg, isopropanol 114 µL, and reaction time 18 h. The yield of isopropyl myristate was 66.62%. After ten cycles, the activity of the immobilized KDN lipase preserved more than 46.87% of its initial enzyme activity, and it demonstrated high tolerance to solvents compared to free KDN lipase.

Abstract licence: CC BY 4.0