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Surface Modification of Cellulose Acetate with Cutinase and ...

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General Introduction: Application <strong>of</strong> Enzymes for Textile Fibres Processing<br />

covalent conjugation <strong>of</strong> polyamines, lipid esterification, or the deamidation <strong>of</strong><br />

glutamine residues (Folk <strong>and</strong> Cole, 1966; Folk et al., 1968; Folk, 1969; Folk, 1980;<br />

Lor<strong>and</strong> <strong>and</strong> Conrad, 1984). Transglutaminases are widely distributed among bacteria,<br />

plants <strong>and</strong> animals.<br />

The first characterized microbial transglutaminase (MTG) was that <strong>of</strong> the bacterium<br />

Streptomyces mobaraensis (Ando et al., 1989). This enzyme is secreted as a zymogen<br />

that is sequentially processed by two endogenous enzymes to yield the mature form<br />

(Zotzel et al., 2003). The mature enzyme is a monomeric protein <strong>with</strong> a molecular<br />

weight <strong>of</strong> 38 kDa. It contains a single catalytic cysteine residue (Cys64) <strong>and</strong> an<br />

isoelectric point (pI) <strong>of</strong> 9 (Pasternack et al., 1998; Kanaji et al., 1993).<br />

The optimum pH for MTG activity was found to be between 5 <strong>and</strong> 8. However, MTG<br />

showed some activity at pH 4 or 9, <strong>and</strong> was thus considered to be stable over a wide pH<br />

range (Ando et al., 1989). The optimum temperature for enzymatic activity was 55 °C;<br />

it maintained full activity for 10 min at 40 °C, but lost activity <strong>with</strong>in a few minutes at<br />

70 °C. It was active at 10 °C, <strong>and</strong> retained some activity at near-freezing temperatures.<br />

MTG does not require calcium for activity, shows broad substrate specificity <strong>and</strong> can<br />

be produced at relatively low cost. These properties are advantageous for industrial<br />

applications.<br />

9.1 Attempst for treatment <strong>of</strong> wool <strong>and</strong> leather<br />

The study <strong>of</strong> TGs for the treatment <strong>of</strong> wool textiles has been shown to improve shrink<br />

resistance, tensile strength retention, h<strong>and</strong>le, s<strong>of</strong>tness, wettability <strong>and</strong> consequently dye<br />

uptake, as well as, reduction <strong>of</strong> felting tendency <strong>and</strong> protection from the damage caused<br />

by the use <strong>of</strong> common detergents (Cortez et al., 2004; Cortez et al., 2005).<br />

Treatment <strong>of</strong> leather <strong>with</strong> TG, together <strong>with</strong> keratin or casein, has a beneficial effect on<br />

the subsequent dyeing <strong>and</strong> colour properties <strong>of</strong> leather (Collighan et al., 2002). The<br />

application <strong>of</strong> TG for leather <strong>and</strong> wool treatment seems to be a promising strategy, but<br />

is still in the research level. There is no industrial application.<br />

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