Regioselective hydroxylation in the production of 25-hydroxyvitamin D by Coprinopsis cinerea peroxygenase
Monohydroxylated metabolites of vitamin D3 (cholecalciferol) and vitamin D2 (ergocalciferol), generically known as 25-hydroxycalciferol, are better for several diseases, and other applications, than vitamin D (calciferol). This work describes a novel biotechnological approach for the preparation of 25-hydroxycalciferols, starting from readily available cholecalciferol and ergocalciferol. This approach enables the regioselective (100%) hydroxylation of these compounds (at the C-25 position) under mild and environmentally friendly conditions by using a peroxidase from the fungus Coprinopsis cinerea (gene model CC1G_08427T0 from the sequenced genome), which catalyzes monooxygenation with H2O2 as the only co-substrate (peroxygenase). Hydroxylation of cholecalciferol and ergocalciferol is a true peroxygenation, as demonstrated by incorporation of 18O from H218O2 into the products. The peroxygenase has additional advantages related to its recombinant nature, enabling enzyme engineering and low-cost overexpression in an industrial host. Therefore, the peroxygenase is a promising biocatalyst for the production of vitamin D active metabolites.
Main Authors: | , , , , |
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Format: | artículo biblioteca |
Language: | English |
Published: |
Wiley-VCH
2015
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Subjects: | Peroxygenase, Vitamin D, Hydroxylation, Cholecalciferol, Ergocalciferol, |
Online Access: | http://onlinelibrary.wiley.com/doi/10.1002/cctc.201402795/abstract http://hdl.handle.net/10261/113232 |
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Summary: | Monohydroxylated metabolites of vitamin D3 (cholecalciferol) and vitamin D2 (ergocalciferol), generically known as 25-hydroxycalciferol, are better for several diseases, and other applications, than vitamin D (calciferol). This work describes a novel biotechnological approach for the preparation of 25-hydroxycalciferols, starting from readily available cholecalciferol and ergocalciferol. This approach enables the regioselective (100%) hydroxylation of these compounds (at the C-25 position)
under mild and environmentally friendly conditions by using a peroxidase from the fungus Coprinopsis cinerea (gene model CC1G_08427T0 from the sequenced genome), which catalyzes monooxygenation with H2O2 as the only co-substrate (peroxygenase).
Hydroxylation of cholecalciferol and ergocalciferol is a true peroxygenation, as demonstrated by incorporation of 18O from H218O2 into the products. The peroxygenase has additional advantages related to its recombinant nature, enabling enzyme engineering and low-cost overexpression in an industrial host. Therefore, the peroxygenase is a promising biocatalyst for the production of vitamin D active metabolites. |
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