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Proteolytic enzyme engineering: a tool for wool.

Abstract
One of the goals of protein engineering is to tailor the structure of enzymes to optimize industrial bioprocesses. In the present work, we present the construction of a novel high molecular weight subtilisin, based on the fusion of the DNA sequences coding for Bacillus subtilis prosubtilisin E and for an elastin-like polymer (ELP). The resulting fusion protein was biologically produced in Escherichia coli , purified and used for wool finishing assays. When compared to the commercial protease Esperase, the recombinant subtilisinE-VPAVG(220) activity was restricted to the cuticle of wool, allowing a significant reduction of pilling, weight loss and tensile strength loss of wool fibers. Here we report, for the first time, the microbial production of a functionalized high molecular weight protease for controlled enzymatic hydrolysis of wool surface. This original process overcomes the unrestrained diffusion and extended fiber damage which are the major obstacles for the use of proteases for wool finishing applications.
AuthorsRita Araújo, Carla Silva, Raul Machado, Margarida Casal, António M Cunha, José Carlos Rodriguez-Cabello, Artur Cavaco-Paulo
JournalBiomacromolecules (Biomacromolecules) Vol. 10 Issue 6 Pg. 1655-61 (Jun 08 2009) ISSN: 1526-4602 [Electronic] United States
PMID19459642 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Serine Endopeptidases
  • Subtilisins
  • mesentericopeptidase
Topics
  • Animals
  • Calorimetry, Differential Scanning
  • Hydrolysis
  • Microscopy, Electron, Scanning
  • Microscopy, Fluorescence
  • Serine Endopeptidases (chemistry, isolation & purification, metabolism)
  • Subtilisins (chemistry, isolation & purification, metabolism)
  • Tensile Strength
  • Wool

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