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- W2024376504 abstract "A total of nine lipases and three proteases were tested for enzymatic regioselective acylation(s) of cordycepin with vinyl acetate in organic media. The highest conversion with better initial reaction rate was achieved with immobilized Candida antarctica lipase B (Novozym 435). An eco-friendly solvent 2-methyltetrahydrofuran (MeTHF) was thought to be the most suitable reaction medium. Novozym 435 was found to be a useful biocatalyst for the 25-g scale syntheses of cordycepin acetate (96.2% isolated yield), and the biocatalyst displayed excellent regioselectivity and high operational stability during the transformation. The 5′-substituted cordycepin derivative was the sole detectable product from each acylation reaction. Novozym 435 could be recycled for the synthesis of cordycepin derivative on a 25-g scale and 63% of its original activity was maintained after being reused for 7 batches. MeTHF could be considered as an eco-friendly solvent for the large scale use in biotransformation." @default.
- W2024376504 created "2016-06-24" @default.
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- W2024376504 date "2013-04-01" @default.
- W2024376504 modified "2023-10-16" @default.
- W2024376504 title "Highly efficient and regioselective acylation of pharmacologically interesting cordycepin catalyzed by lipase in the eco-friendly solvent 2-methyltetrahydrofuran" @default.
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- W2024376504 doi "https://doi.org/10.1016/j.biortech.2013.01.117" @default.
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