A new cuticle scale hydrolysing protease from Beauveria brongniartii

Biotechnol Lett. 2006 May;28(10):703-10. doi: 10.1007/s10529-006-9047-1. Epub 2006 May 23.

Abstract

From a screening for the production of new proteases specific for cuticle scales, Beauveria brongniartii was selected producing an alkaline Ca(++) dependent protease. The purified had a molecular weight of 27 kDa and a pI value of 8.0. Substrate specificities of model substrates (wool with partially removed cuticles treated with SDS) were analyzed by protein release, dissolved organic carbon (DOC) and nitrogen analysis. The C/N ratio of released material turned out to be a good parameter to determine the site of action of proteases on fibres. Compared to other enzymes, the fungal protease preferentially hydrolyzed cuticle scales and has thus a potential for anti-shrinking pre-treatment of wool fabrics.

MeSH terms

  • Animals
  • Beauveria / enzymology*
  • Calcium / metabolism
  • Carbon / chemistry
  • Caseins / chemistry
  • Endopeptidases / chemistry
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Mass Spectrometry
  • Microscopy, Electron, Scanning
  • Nitrogen / chemistry
  • Peptide Hydrolases / chemistry*
  • Substrate Specificity
  • Temperature
  • Wool / metabolism
  • Wool / microbiology

Substances

  • Caseins
  • azocasein
  • Carbon
  • Endopeptidases
  • Peptide Hydrolases
  • Nitrogen
  • Calcium