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Enzymatic hydrolysis and modifi cation of core polymer fi bres   83


                 O         O             O          O              O
              O  C         C  O  CH  CH  O  C       C  O    CH 2  O  C
                                  2  2                   CH 2



                 Cutinase
                 Polyesterase
                              1 1      22              33       44
                 Lipase


                  2  3   TPA
                  1  4   BHET
                  1  3 or  2  4  MHET
                   4.1  Enzymatic hydrolysis of poly(ethylene terephthalate) by cutinase,
                   polyesterase and lipase.


            a lid, the oxyanion hole is preformed but considerably flexible in solution.
            Today, cutinases seem to have a large potential in the enzymatic surface
            modifi cation of PET (Nierstrasz, 2009). The optimum pH and temperature
            for cutinase from Fusarium solani pisi are pH 8–8.5 at around 25 °C; above
            35 °C the activity decreases rapidly. The relatively low reaction rate and
            limited temperature stability hinder industrial application of cutinases.
            Araújo et al. (2007) succeeded in increasing the reaction rate of cutinases
            on PET by modifying (enlarging) the active site through site-directed muta-
            genesis of cutinase from  Fusarium solani pisi, whereas researchers from
            Novozymes improved the temperature stability to as high as 65–80 °C (Liu
            et al., 2008).
              An advantage of a cutinase or lipase treatment is that it does not result
            in pitting corrosion, as seen in alkaline treatments, but a more or less homo-
            geneous surface treatment of PET (Brueckner et al., 2008; Donelli et al.,
            2009; Kim and Song, 2006, 2008). The homogeneity of the treatment depends
            on enzyme, enzyme concentration and incubation time. Using X-ray
            photoelectron spectrometry (XPS), Vertommen et al. (2005) demonstrated
            that cutinases strongly adsorb to the PET surface.  This hinders proper
            determination of surface properties, such as wetting characteristics or for-
            mation of carboxyl or hydroxyl groups in the surface. Proper procedures
            have been developed to remove the adsorbed enzyme using proteases
            (Donelli et al., 2009; Liu et al., 2008) or using a thorough washing and extrac-
            tion method (Brueckner et al., 2008). After protein (cutinase) removal from
            the surface it is possible to properly evaluate the surface modifi cation.
            Donelli and co-workers (2009) measured water contact angles on PET fi lms
            treated with cutinase, ∼75° for untreated PET and ∼58° for cutinase-treated
            PET. Brueckner et al. (2008) and Liu et al. (2008) measured wetting times




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