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Surface Modification of Cellulose Acetate with Cutinase and ...

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Subchapter 3.3<br />

Abstract<br />

In this work, we propose the construction <strong>of</strong> a novel high molecular weight subtilisin<br />

based on the fusion <strong>of</strong> prosubtitlin E DNA sequence from Bacillus subtilis <strong>with</strong> a DNA<br />

sequence that codifies to an elastin-like polymer. Wool yarns were treated <strong>with</strong> both<br />

commercial <strong>and</strong> chimeric subtilisins. It was shown that using the chimeric subtilisin<br />

there was a significant reduction <strong>of</strong> felting, pilling <strong>and</strong> tensile strength loss <strong>of</strong> wool<br />

yarns since the hydrolysis is restricted to the cuticle <strong>of</strong> wool.<br />

The results stated here are <strong>of</strong> great importance once it is reported for the first time the<br />

microbial production <strong>of</strong> a chimeric high molecular weight protease for wool surface<br />

hydrolysis. This novel process <strong>of</strong> enzymatic-controlled hydrolysis overcomes the<br />

unrestrained diffusion <strong>and</strong> extended fibre damage which is the major obstacle on the use<br />

<strong>of</strong> enzymes for wool finishing applications.<br />

204

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