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Surface Modification of Cellulose Acetate with Cutinase and ...

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Influence <strong>of</strong> Mechanical Agitation on <strong>Cutinase</strong>s <strong>and</strong> Protease Activity Toward Polyamide Substrates<br />

reaching a high level <strong>of</strong> about 60% <strong>of</strong> adsorption. Orbital agitation provided values <strong>of</strong><br />

protein adsorption in the order <strong>of</strong> 30%.<br />

K/S variation (%)<br />

80<br />

60<br />

40<br />

20<br />

0<br />

-20<br />

-40<br />

no discs <strong>with</strong> discs 4 h 24 h 48 h<br />

vertical agitation<br />

orbital agitation<br />

50ºC<br />

60ºC<br />

70ºC<br />

Figure 3. K/S variation, proportional to the amino groups at the surface <strong>of</strong> the treated<br />

fabric (4% <strong>of</strong> reactive dye; liquor ratio 1:100; 90 minutes).<br />

As obtained for polyamide model substrate (Table I), on fabric the L182A cutinase<br />

mutant presented a considerably higher activity when compared <strong>with</strong> the native one.<br />

(Figures 4 a) <strong>and</strong> 4 b)) Protein adsorption values are similar for both enzymes <strong>and</strong><br />

presented higher values when stainless steel discs were included on the enzymatic<br />

system.<br />

97

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