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EnglishWe 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) and 98.7% purity. A 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).
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| Titolo: | Redesigning the synthesis of Vidarabine via a multienzymatic reaction catalyzed by immobilized nucleoside phosphorylases |
| Autori: | UBIALI, DANIELA (Corresponding) |
| Data di pubblicazione: | 2015 |
| Rivista: | |
| Citazione: | Redesigning the synthesis of Vidarabine via a multienzymatic reaction catalyzed by immobilized nucleoside phosphorylases / Serra, I.; Daly, S.; Alcantara, A. R.; Bianchi, D.; Terreni, Marco; Ubiali, Daniela. - In: RSC ADVANCES. - ISSN 2046-2069. - STAMPA. - 5:30(2015), pp. 23569-23577. |
| Abstract: | 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) and 98.7% purity. A 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). |
| Handle: | http://hdl.handle.net/11571/1063185 |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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