Page 82 - Advances in Textile Biotechnology
P. 82

Smart materials containing enzymes or enzyme substrates   61


              Tyrosinase (EC 1.14.18.1) has recently found applications for grafting and
            coating protein-based textile materials such as wool and silk (Anghileri
            et al., 2007, Freddi et al., 2006, Jus et al., 2008, 2009, Sampaio et al., 2005).
            In chemical synthesis, it is used for the production of  l-DOPA (3,4-
            dihydroxyphenyl-l-alanine) from tyrosin which is used for the treatment of
            Parkinson’s disease. Tyrosinase immobilization not only allows the design
            of continuous processes reusing the enzyme but also stabilization of
            l-DOPA by carrier autodegradation (Acharya et al., 2008). Using glutaral-
            dehyde as crosslinking agent, tyrosinase has been immobilized on fi broin
            (Acharya et al., 2008) and on nylon 6,6 (Pialis and Saville, 1998, Pialis et al.,
            1996). Apart from glutaraldehyde attachment, other approaches were based
            on tyrosinase entrapment in alginate, polyacrylamide and gelatin (Munjal
            and Sawhney, 2002).
              Laccase (EC 1.10.3.2) is used for a variety of applications including the
            treatment of textile dyeing effl uents (Kandelbauer et al., 2004), elimination
            of off-flavors in food products (Schroeder et al., 2008) and for lignocellulose

            processing (Kudanga et al., 2008). For numerous applications laccase has
            been immobilized on inorganic carrier materials such as alumina pellets
            (Abadulla et al., 2000). Also, laccase has been bound to organic polymers
            (i.e. PEG) to obtain water-soluble immobilized proteins with enlarged

            molecular weight and modified sorption properties. Such constructs have
            been used in detergents to prevent dye transfer (Schroeder et al., 2006). A
            novel approach for laccase immobilization on polyamide 6,6 involved
            limited surface hydrolysis of polyamide 6,6 by protease to introduce func-

            tional groups. Thereafter, first the spacer 1,6-hexanediamine followed by
            laccase were attached by glutaraldehye (Silva et al., 2007).
              Glucose oxidase (EC 1.1.3.4) is widely used in many applications includ-
            ing novel approaches for bleaching of textiles (Buschle-Diller, 2001, Tzanov
            et al., 2001). For example, glucose oxidase was immobilized on viscose
            rayon, polyethyleneterephthalate, nylon-6, polypropylene and non-woven
            fabrics of silk fi broin (Asakura et al., 1992). Urease (EC 3.5.1.5) was immo-
            bilized on cellulose fabrics to remove urea in an electrodialysis cell. Immo-
            bilization was achieved by biotinylation of both the enzyme and the
            cellulose fi bres (Magne et al., 2002).


            3.2.5 Enzyme immobilization strategies
            Various strategies have been developed for incorporation of enzymes into
            polymers including entrapment (Kim  et al., 2001b), covalent attachment
            (Dessouki  et al., 2001) and adsorptive binding (Akgol  et al., 2001).
            Polydimethylsiloxanes have been used for covalent entrapment of enzymes
            including lipases and proteases (Gill and Ballesteros, 2000a, 2000b, Kim

            et al., 2001a). The biocatalytic films and paints can be applied to a wide



                              © Woodhead Publishing Limited, 2010
   77   78   79   80   81   82   83   84   85   86   87