Page 79 - Advances in Textile Biotechnology

58 Advances in textile biotechnology

3.2 Smart materials containing enzymes
3.2.1 Wound dressings

Cotton-based wound dressings were functionalized by immobilization of
various biomolecules. These include peptides acting as inhibitors of human
neutrophil elastase or enzymes to impart haemostatic or antibacterial prop-
erties (Edwards and Goheen, 2006). Similarly, woven polyester fabrics
(Dacron) were activated with ethylenediamine followed by surface immo-
bilization of thrombin. Thrombin functionalized fabrics lead to thrombus
formation after 1 min whereas on control fabrics there was only blood
protein adsorption (Phaneuf et al., 2005).

3.2.2 Functional textiles

Enzyme immobilization onto textiles was used to create smart materials
with novel properties such as self-detoxifying or anti-microbial activity. For
military purposes, organophosphorous hydrolase was covalently immobi-

lized on cotton for detoxification of organophosphorus warfare agents such
as sarin, soman, tabun (Edwards and Goheen, 2006). Cotton was fi rst ester-

ified with glycine followed by coupling of the enzymes with carbonyldiimid-
azole and glutaraldehyde. Organophosphorous hydrolase (EC 3.1.8.1),
organophosphorous acid anhydrolase (EC 3.1.8.2), diisopropylfl uorophos-
phatase (EC 3.1.8.2), phosphotriesterases (PTE) (EC 3.1.8) and combina-
tions of these enzymes were suggested for immobilization on cotton textiles
within polyelectrolyte multilayers allowing degradation of a wide range of
toxic agents. Catalytic enzyme-modified textiles for active protection from

toxins (USPTO Application #: 20070014838, 2009).
Textiles with antimicrobial properties have been produced by immobili-
zation of a variety of enzymes. Attachment of alkaline pectinase, alpha-
amylase or laccase lead to antimicrobial fabrics retaining full activity for at
least ten consecutive wash cycles (Ibrahim et al., 2007).
Lysozyme has also been used for the construction of antimicrobial tex-
tiles and packaging materials. This muramidase hydrolyzes the β-1,4 gluco-
sidic linkages between N-acetylmuramic acid and N-acetylglucosamine of
the cell wall of many micro-organisms. Lysozyme was covalently attached
to cotton fabrics which were activated via esterification with glycine and a

glycine dipeptide. Higher activity recovery was measured when the glycine
dipeptide was used as a spacer. Consequently, in models of lysozyme-
attached through Asp-87, Glu-7, Asp-119, Asp-18, and COOH-terminal
Leu-129 to cellopentaose-(3) gly-O-6-glycyl-glycine no steric hindrance of
the active site was seen (Edwards et al., 2000). Lysozyme was also covalently
immobilized on wool fabric activated with glutaraldehyde. Compared with
control fabrics, antimicrobial activity of lysozyme-functionalized wool

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