4 research outputs found
Restricting detergent protease action to surface of protein fibres by chemical modification
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 (ΔE) 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