Applied Microbiology and Biotechnology

, Volume 85, Issue 6, pp 1735–1750

Biochemical features of microbial keratinases and their production and applications

Authors

    • Laboratório de Bioquímica e Microbiologia Aplicada, Departamento de Ciência de AlimentosUniversidade Federal do Rio Grande do Sul
    • ICTA-UFRGS
  • Daniel J. Daroit
    • Laboratório de Bioquímica e Microbiologia Aplicada, Departamento de Ciência de AlimentosUniversidade Federal do Rio Grande do Sul
  • Alessandro Riffel
    • Embrapa-Empresa Brasileira de Pesquisa AgropecuáriaCentro de Pesquisa Agropecuária dos Tabuleiros Costeiros-UEP Alagoas
Mini-Review

DOI: 10.1007/s00253-009-2398-5

Cite this article as:
Brandelli, A., Daroit, D.J. & Riffel, A. Appl Microbiol Biotechnol (2010) 85: 1735. doi:10.1007/s00253-009-2398-5

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.

Keywords

FeatherKeratinMicrobial proteaseSerine proteaseMetalloproteaseProteolysis

Copyright information

© Springer-Verlag 2009