Redesigning the synthesis of vidarabine via a multienzymatic reaction catalyzed by immobilized nucleoside phosphorylases
2015
Serra, Immacolata | Daly, Simona | Alcantara, Andres R. | Bianchi, Davide | Terreni, Marco | Ubiali, Daniela
We here report on the enzymatic synthesis of the antiviral drug vidarabine (arabinosyladenine, araA) starting from arabinosyluracil and adenine. To this aim, uridine phosphorylase from Clostridium perfringens (CpUP) and a purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP) were used as covalently immobilized biocatalysts. Upon investigation of the optimal conditions for the enzyme activity (phosphate buffer 25 mM, pH 7.5, 25 °C, DMF 12.5–30%), the synthesis of araA was scaled up (2 L) and the product was isolated in 53% yield (3.5 g L⁻¹) and 98.7% purity. An E-factor comparison between the enzymatic synthesis of araA and the classical chemical procedure clearly highlighted the “greenness” of the enzymatic route over the chemical one (E-factor: 423 vs. 1356, respectively).
اظهر المزيد [+] اقل [-]الكلمات المفتاحية الخاصة بالمكنز الزراعي (أجروفوك)
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