Abstract-In the present research work, the multi-enzyme polypeptide carbamoyl synthetase-aspartate transcarbamoylase-dihydroorotase (CAD) was used as a novel biocatalyst to catalyze a multi-step reaction in a unitary reaction medium. Using organic solvent as reaction medium, we have observed formation of the final product, dihydroorotate, from initial substrates. Study on substrate specificity showed that the enzyme is capable of converting various amine to the corresponding dihydroortate (DHO). The multienzyme polypeptide CAD has an apparent molecular weight of 215,000-222,000.

Abstract. S-Naproxenal oleins are compounds of S-Naproxen ((S)-2-(6-methoxy-2-naphthyl) propionic acid) and olein connected by an ester bond and can be used as potential prodrug in anti-inflammatory. In the present work, we describe for the first time the lipase-catalyzed synthesis of the S-Naproxenal oleins by transesterification between S-Naproxen and triolein in organic solvents medium. The ability of lipases to catalyze the transesterification between S-Naproxen and triolein was investigated. Only the lipase from Candida rugosa and the immobilized lipase B from Candida antarctica (Novozym 435) catalyzed the transesterification. The influences of reaction condition on the combined yield of S-Naproxenal diolein (NDO) and S-Naproxenal monoolein (NMO) were investigated. Water activity (a w ) had an obvious influence on transesterification efficacy. A maximal combined yield of 23.1 % of S-Naproxenal diolein (NDO) and S-Naproxenal monoolein (NMO) was obtained under optimum condition. These results indicated the industrial potential of the operation scheme developed in this study.