Evidence map›Paper›PMID 42432706›Full record

ArticleBiotechnology for biofuels and bioproducts2026

Comprehensive assessment of fungal peroxygenases for the selective synthesis of 25-hydroxyvitamins D

Alejandro González-Benjumea, Andrés Olmedo, Katharina Ebner, Anton Glieder, Ana Gutiérrez

Abstract read
In one paragraph

Article in Biotechnology for biofuels and bioproducts, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Alejandro González-Benjumea *Instituto de Recursos Naturales y Agrobiología de Sevilla (IRNAS), CSIC, Reina Mercedes 10, 41012, Seville, Spain.
Andrés Olmedo *Instituto de Recursos Naturales y Agrobiología de Sevilla (IRNAS), CSIC, Reina Mercedes 10, 41012, Seville, Spain.
Katharina EbnerBisy GmbH, Hofstätten an der Raab, Austria.
Anton GliederBisy GmbH, Hofstätten an der Raab, Austria.
Ana GutiérrezInstituto de Recursos Naturales y Agrobiología de Sevilla (IRNAS), CSIC, Reina Mercedes 10, 41012, Seville, Spain. anagu@irnase.csic.es.

Funding

European Commission ROBUSTOO Project - grant agreement n° 101135119
6 · The paper itself

Abstract

backgroundThe metabolite 25-hydroxyvitamin D is significantly better for clinical use in several diseases and food supplementations than vitamin D (calciferol) itself. The present study reports an efficient biotechnological method for the synthesis of 25-hydroxyvitamin D

resultsA widespread investigation of a series of up to 71 unspecific peroxygenases (UPOs), including UPO samples from 41 fungal species (together with several isozymes and variants) expressed in Komagataella phaffii (formerly Pichia pastoris), has been performed for the regioselective C25-hydroxylation of vitamin D (D

conclusionsThis approach represents a green and sustainable alternative to the chemical synthesis of these hydroxylated compounds that is tedious, occurs with little regioselectivity, and includes several steps and strong oxidizing agents. Moreover, K. phaffii a widely used yeast platform for recombinant protein production ‒ including high-yield secretory expression of industrial enzymes ‒ has been firmly established as a favorable host for recombinant UPO production in recent years.

Indexed as

CholecalciferolErgocalciferolHypoxylon sp.Komagataella phaffiiUnspecific peroxygenasesUPOsVitamins

Identifiers

PMID42432706
PMCPMC13640091

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