title: Restricting detergent protease action to surface of protein fibres by chemical modification.
abstract: Due to their excellent properties, such as thermostability, activity over a broad range of pH and efficient stain removal, proteases from Bacillus sp. are commonly used in the textile industry including industrial processes and laundry and represent one of the most important groups of enzymes. However, due to the action of proteases, severe damage on natural protein fibres such as silk and wool result after washing with detergents containing proteases. To include the benefits of proteases in a wool fibre friendly detergent formulation, the soluble polymer polyethylene glycol (PEG) was covalently attached to a protease from Bacillus licheniformis. In contrast to activation of PEG with cyanuric chloride (50%) activation with 1,1'-carbonyldiimidazole (CDI) lead to activity recovery above 90%. With these modified enzymes, hydrolytic attack on wool fibres could be successfully prevented up to 95% compared to the native enzymes. Colour difference (DeltaE) measured in the three dimensional colour space showed good stain removal properties for the modified enzymes. Furthermore, half-life of the modified enzymes in buffers and commercial detergents solutions was nearly twice as high as those of the non-modified enzymes with values of up to 63 min. Out of the different modified proteases especially the B. licheniformis protease with the 2.0-kDa polymer attached both retained stain removal properties and did not hydrolyse/damage wool fibres.
authors.affiliation: Department of Environmental Biotechnology, Graz University of Technology, Petersgasse 12, A-8010 Graz, Austria.
authors.forename: M
authors.initials: M
authors.lastname: Schroeder
authors.forename: H B M
authors.initials: HB
authors.lastname: Lenting
authors.forename: A
authors.initials: A
authors.lastname: Kandelbauer
authors.forename: C J S M
authors.initials: CJ
authors.lastname: Silva
authors.forename: A
authors.initials: A
authors.lastname: Cavaco-Paulo
authors.forename: G M
authors.initials: GM
authors.lastname: Gübitz
mesh_terms: D000818:Animals; D001407:Bacillus / Q000201:enzymology* / Q000378:metabolism; D003902:Detergents / Q000737:chemistry*; D004795:Enzyme Stability; D008422:Materials Testing; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism*; D014935:Wool / Q000737:chemistry* / Q000648:ultrastructure
chemical_list: D003902:Detergents; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases