Surface Modification of Cellulose Acetate with Cutinase and ...
Surface Modification of Cellulose Acetate with Cutinase and ...
Surface Modification of Cellulose Acetate with Cutinase and ...
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<strong>Surface</strong> <strong>Modification</strong> <strong>of</strong> <strong>Cellulose</strong> <strong>Acetate</strong> <strong>with</strong> <strong>Cutinase</strong> <strong>and</strong> <strong>Cutinase</strong> Fused to Carbohydrate-binding Modules<br />
were competitively dyed at 60º C. Relative protein adsorption was calculated as<br />
P<br />
P<br />
0h<br />
0hcutinase<br />
− P<br />
− P<br />
18h<br />
18hcutinase<br />
4. Concluding remarks<br />
<strong>and</strong> relative K/S was calculated as<br />
K / S<br />
K / S<br />
enzyme<br />
cutinase<br />
− K / S<br />
− K / S<br />
The biomodification <strong>of</strong> the surface <strong>of</strong> cellulose acetate <strong>with</strong> high degree <strong>of</strong> substitution<br />
<strong>with</strong> cutinase was demonstrated by the acetic acid release <strong>and</strong> the improvement in the<br />
chemically specific staining <strong>of</strong> the fabrics <strong>with</strong> a reactive dye. From the acetic acid<br />
release, the hydrolysis yield is higher for the less substituted cellulose acetate fabric, but<br />
the consequences <strong>of</strong> the acetyl hydrolysis are more pronounced for CTA, as shown by<br />
the differences in colour, morphology <strong>of</strong> the fibres surface <strong>and</strong> crystallinity between<br />
controls <strong>and</strong> treated samples. Further studies will be necessary to evaluate the impact <strong>of</strong><br />
cutinase activity in the physical properties <strong>of</strong> the fabrics <strong>and</strong> to assess the contribution<br />
<strong>of</strong> the incomplete protein removal <strong>and</strong> <strong>of</strong> the physical, rather than chemical,<br />
modifications on the differences seen upon enzymatic treatment.<br />
The design <strong>of</strong> hybrid enzymes mimics the strategies that nature uses to evolve <strong>and</strong> it is a<br />
powerful tool in biotechnology. The production <strong>and</strong> application <strong>of</strong> the cutinase fused to<br />
CBMs, especially to the fungal CBM <strong>of</strong> CBHI <strong>of</strong> T. reesei, provided strong evidences<br />
<strong>of</strong> being an interesting strategy to pursuit. Future work is needed to improve the<br />
recombinant production <strong>of</strong> modular cutinases <strong>and</strong> to study in detail their affinities<br />
toward the cellulose acetates.<br />
From the above considerations, it could be suggested that the cutinase has potential in<br />
textile industry for the surface modification <strong>and</strong> consequently on the “bicomponent<br />
yarns/fibres” production <strong>of</strong> cellulose acetate.<br />
control<br />
control<br />
.<br />
153