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Biochemical features of microbial keratinases and their production and applications

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Abstract

Keratinases are exciting proteolytic enzymes that display the capability to degrade the insoluble protein keratin. These enzymes are produced by diverse microorganisms belonging to the Eucarya, Bacteria, and Archea domains. Keratinases display a great diversity in their biochemical and biophysical properties. Most keratinases are optimally active at neutral to alkaline pH and 40–60°C, but examples of microbial keratinolysis at alkalophilic and thermophilic conditions have been well documented. Several keratinases have been associated to the subtilisin family of serine-type proteases by analysis of their protein sequences. Studies with specific substrates and inhibitors indicated that keratinases are often serine or metalloproteases with preference for hydrophobic and aromatic residues at the P1 position. Keratinolytic enzymes have several current and potential applications in agroindustrial, pharmaceutical, and biomedical fields. Their use in biomass conversion into biofuels may address the increasing concern on energy conservation and recycling.

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Acknowledgements

AB is research fellow of Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Brazil.

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  1. Laboratório de Bioquímica e Microbiologia Aplicada, Departamento de Ciência de Alimentos, Universidade Federal do Rio Grande do Sul, 91501-970, Porto Alegre, Brazil

    Adriano Brandelli & Daniel J. Daroit

  2. Embrapa-Empresa Brasileira de Pesquisa Agropecuária, Centro de Pesquisa Agropecuária dos Tabuleiros Costeiros-UEP Alagoas, 57061-970, Maceió, Brazil

    Alessandro Riffel

  3. ICTA-UFRGS, Av. Bento Gonçalves 9500, 91501-970, Porto Alegre, Brazil

    Adriano Brandelli

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  1. Adriano Brandelli
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Correspondence to Adriano Brandelli.

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Brandelli, A., Daroit, D.J. & Riffel, A. Biochemical features of microbial keratinases and their production and applications. Appl Microbiol Biotechnol 85, 1735–1750 (2010). https://doi.org/10.1007/s00253-009-2398-5

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