Sulfhydryl oxidases: Sources, properties, production and applications

Greta Faccio (Corresponding Author), Outi Nivala, Kristiina Kruus, Johanna Buchert, Markku Saloheimo

    Research output: Contribution to journalArticleScientificpeer-review

    23 Citations (Scopus)


    The formation of disulfide bonds in proteins and small molecules can greatly affect their functionality. Sulfhydryl oxidases (SOXs) are enzymes capable of oxidising the free sulfhydryl groups in proteins and thiol-containing small molecules by using molecular oxygen as an electron acceptor. SOXs have been isolated from the intracellular compartments of many organisms, but also secreted SOXs are known. These latter enzymes are generally active on small compounds and their physiological role is unknown, whereas the intracellular enzymes prefer proteins as substrates and are involved in protein folding. An increasing number of scientific publications and patent applications on SOXs have been published in recent years. The present mini-review provides an up-to-date summary of SOXs from various families, their production and their actual or suggested applications. The sequence features and domain organisation of the characterised SOXs are reviewed, and special attention is paid to the physicochemical features of the enzymes. A review of patents and patent applications regarding this class of enzymes is also provided.
    Original languageEnglish
    Pages (from-to)957-966
    Number of pages10
    JournalApplied Microbiology and Biotechnology
    Issue number4
    Publication statusPublished - 2011
    MoE publication typeA1 Journal article-refereed


    • Application
    • disulfide bond
    • glutathione
    • sulfhydryl oxidase
    • thiol oxidase


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