Enzymatic ethanolysis of oils (for example, high oleic sunflower oil containing 90% of oleic acid) may yield two different reaction products depending on the regioselectivity of the immobilized lipase biocatalyst. Some lipase biocatalysts exhibit a 1,3-regioselectivity and they produced 2 mols of fatty acid ethyl ester plus 1 mol of sn2-monoacylglycerol (2-MAG) per mol of triglyceride without the release of glycerol. Other lipase biocatalysts are completely non-regioselective releasing 3 mols of fatty acid ethyl ester and 1 mol of glycerol per mol of triglyceride. Lipase from Thermomyces lanuginosus (TLL) adsorbed on hydrophobic supports is a very interesting biocatalyst for the ethanolysis of oil. Modulation of TLL regioselectivity in anhydrous medium was intended via two strategies of TLL immobilization: a. - interfacial adsorption on different hydrophobic supports and b.- interfacial adsorption on a given hydrophobic support under different experimental conditions. Immobilization of TLL on supports containing divinylbenezene moieties yielded excellent 1,3-regioselective biocatalysts but immobilization of TLL on supports containing octadecyl groups yielded non-regioselective biocatalysts. On the other hand, TLL immobilized on Purolite C18 at pH 8.5 and 30 °C in the presence of traces of CTAB yielded a biocatalyst with a perfect 1,3-regioselectivity and a very interesting activity: 2.5 μmols of oil ethanolyzed per min per gram of immobilized derivative. This activity is 10-fold higher than the one of commercial Lipozyme TL IM. Immobilization of the same enzyme on the same support, but at pH 7.0 and 25 °C, led to a biocatalyst which can hydrolyze all ester bonds in TG backbone. Activity and regioselectivity of TLL in anhydrous media can be easily modulated via Biocatalysis Engineering producing very active immobilized derivatives able to catalyze the ethanolysis of triolein. When the biocatalyst was 1,3-regioselective a 33% of 2-monoolein was obtained and it may be a very interesting surfactant. When biocatalyst catalyzed the ethanolysis of the 3 positions during the reaction process, a 99% of ethyl oleate was obtained and it may be a very interesting drug-solvent and surfactant. The absence of acyl migrations under identical reaction conditions is clearly observed and hence the different activities and regioselectivities seem to be due to the different catalytic properties of different derivatives of TLL.

A novel Fourier transform infrared (FT-IR) microscopy method was developed and used to analyze the diffusion of lipase CalB in two different resins during immobilization. The method consisted of a streamlined sample preparation process and an automated transmission FT-IR microscopic measurement using a commercial benchtop device. The immobilization of CalB was performed on a hydrophobic resin containing aromatic groups (ECR1030M based on divinylbenzene) and on a hydrophilic resin containing ester groups and thus oxygen (ECR8204M based on methacrylate) and FT-IR revealed that the kinetic of immobilization and the distribution of the enzyme on the two resins were completely different. Furthermore, the technique revealed that CalB was immobilized on the external surface only in the case of the hydrophobic ECR1030M in a layer of about 50–70 µm, whereas when immobilized on the hydrophilic carrier ECR8204M the interaction of the enzyme with the carrier was uniform over the full diameter of the polymer bead. The enzyme activity however was higher on the hydrophobic support ECR1030M.

Diethylene glycol dimethacrylate (DEG)-crosslinked polystyrene (PS) resin offers a promising alternative to traditional divinyl benzene (DVB)-PS resin for solid-phase peptide synthesis (SPPS), particularly for challenging sequences with hydrophobic or bulky amino acids. DEG-PS resin's reduced hydrophobicity and enhanced flexibility improve synthesis efficiency, yielding peptides up to 28 residues with higher purities and yields compared to DVB-PS. In various syntheses, DEG-PS outperformed DVB-PS resin, with higher purities and yields for challenging peptides such as ABC analogue (73.2%, 58.3% vs. 72.5%, 46.3%) and Thymosin (58.4%, 48.6% vs. 54.0%, 39.2%). In addition, DEG-PS resin effectively suppressed common side reactions, such as dipeptide formation, typically encountered with Wang PS-based resins. Incorporating green chemistry principles, DEG-PS enabled the synthesis of complex peptides with satisfactory results using environmentally friendly solvents and reagents. Three challenging peptides; β (34–42), Jung and Redemann (JR), and ABRF 1992 – were synthesized on DEG-PS resin, achieving purities of 41.4%, 41.0%, and 68.0%, and yields of 50.5%, 52.6%, and 56.2%, respectively. These findings highlight DEG-PS resin's advantages for classical, green, and automated SPPS, offering superior performance and scalability for industrial applications.