Lipases as Tools in the Synthesis of Prodrugs from Racemic 9-(2,3-Dihydroxypropyl)adenine

Abstract

Lipases from Geotrichum candidum 4013 (extracellular lipase and cell-bound lipase) were immobilized by adsorption on chitosan beads. The enzyme preparations were tested in the synthesis of ester prodrugs from racemic 9-(2,3-dihydroxypropyl)adenine in dimethylformamide with different vinyl esters (acetate, butyrate, decanoate, laurate, palmitate). The transesterification activities of these immobilized enzymes were compared with commercially available lipases (lipase from hog pancreas, Aspergillus niger, Candida antarctica, Pseudomonas fluorescens). Lipase from Candida antarctica was found to be the most efficient enzyme regarding chemical yield of the desired products, while transesterification by lipase from Aspergillus niger resulted in lower yields.

Regioselective Palmitoylation of 9-(2,3-Dihydroxy- propyl)adenine Catalyzed by a Glycopolymer-enzyme Conjugate

“…Thus, the biotransformation was performed using different DMF-solvent combinations, considering our experience with the solubility of the DHPA in water and specially the ester derivative [31].…”

“…Aldehyde-activated dextran (glycopolymer D1500) and monocarboxylated PEG1500 were prepared as previously described [22]. ( S )-9-(2,3-dihydroxypropyl)adenine (DHPA) was prepared as previously described [31]. All organic solvents and other reagents were of analytical grade.…”

Comparison of the performances of four hydrophilic polymers as supports for lipase immobilisation

“…Then, the beads were removed by decantation, washed with deionised water until reaching pH 8.0, and soaked in hexane for 1 h under agitation (120 rpm). After hexane excess removal, lipase immobilisation was performed by physical absorption, according to the methodology reported in the literature [ 8 , 21 ] by chitosan beads immersing into a lipase solution for 3 h under stirring at ambient temperature, followed by 24-h static adsorption at 4 °C. The enzyme solution was prepared by dissolving 10 mg of lyophilised lipase into 40 mL of double-distilled water.…”

The three‐dimensional structure and catalytic activity of Candida rugosa lipase against acetaldehyde

“…Lipases catalyze a variety of reactions such as hydrolysis, esterification, transesterification and so on. In particular, lipases catalyze the hydrolysis of carboxylic acid esters, for they have high stability in various reaction media, low cost production and broad substrate specificity . However, the byproduct acetaldehyde is unavoidably generated in the reactions, and can affect enzyme stability and activity.…”