Continuous-flow biocatalysis using immobilized lipases and transaminases in order to synthesize chiral alcohols and amines respectively.

Sustainability in chemistry heavily relies on heterogeneous catalysis. Enzymes, the main catalyst for biochemical reactions in nature, are an elegant choice to catalyze reactions due to their high activity and selectivity, although they usually suffer from lack of robustness. To overcome this drawback, enzyme‐decorated nanoporous heterogeneous catalysts were developed. Three different approaches for Candida antarctica lipase B (CAL‐B) immobilization on a covalent organic framework (PPF‐2) were employed: physical adsorption on the surface, covalent attachment of the enzyme in functional groups on the surface and covalent attachment into a linker added post‐synthesis. The influence of the immobilization strategy on the enzyme uptake, specific activity, thermal stability, and the possibility of its use through multiple cycles was explored. High specific activities were observed for PPF‐2‐supported CAL‐B in the esterification of oleic acid with ethanol, ranging from 58 to 283 U mg−1, which was 2.6 to 12.7 times greater than the observed for the commercial Novozyme 435.

BACKGROUND: In this work, lipase B from Candida antarctica (CaLB) was immobilized on Purolite ® ECR8205F, Purolite ® ECR8214F and Immobead ® IB150 P epoxy resins with no modification to their surfaces. Biocatalysts were evaluated for thermal stability and applied in reactions of hydrolysis, esterification and the synthesis of glyceryl carbonate by transesterification with dimethyl-carbonate both with glycerol and Macauba oil as well as dynamic kinetic resolution of -methylbenzylamine, all of them compared with commercial Novozyme 435 ® .

Abstract:In order to confirm the traditional use of Baccharis trimera (Less.) DC., Asteraceae, for the reduction of weight, plant extracts were evaluated on the activity of pancreatic lipase (PL), an enzyme responsible for hydrolysis of triacylglycerols in the diet for its subsequent absorption. The aqueous and infused extracts did not show inhibitory activity on the PL, the ethanol inhibited 16% (66 ALI/g) and methanol extract inhibited 78% (241 ALI/g). The methanol extract of B. trimera (MEB) was subjected to a wash with decreasing solvent polarity (n-hexane, ethyl acetate and methanol) and only the methanol fraction inhibited the lipase by 72% (230 ALI/g). We evaluated the MEB and infused inhibitory activity on the enzymes α-amylase and α and β-glycosidases. The α-amylase was not inhibited by any of the extracts, the enzyme α-glucosidase was inhibited by both extracts in the same proportion (46.9±0.1) and β-glucosidase was inhibited by 73% by the methanol extract and 65% by the infused. We also evaluated the presence of anti-nutrients. We detected the presence of saponins, polyphenols and trypsin inhibitors in the two samples. Tests performed in vivo can assess at which therapeutic concentration the presence of these anti-nutrients can be harmful to health.