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Surface Modification of Cellulose Acetate with Cutinase and ...

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Chapter 1<br />

targeted enzymatic surface functionalisation <strong>of</strong> PET <strong>and</strong> PA, polymers formerly<br />

considered as being resistant to biodegradation.<br />

Recently, Nechwatal <strong>and</strong> collaborators have tested several commercial lipases/esterases<br />

for their ability to hydrolyse oligomers formed during manufacture <strong>of</strong> PET (Nechwatal<br />

et al., 2006). These low-molecular-weight molecules are insoluble in water <strong>and</strong> can<br />

deposit themselves onto the dye apparatus, damaging it. The authors found that lipase<br />

from Triticum aestivum removed 80 wt % <strong>of</strong> oligomers from liquor bath treatment,<br />

however the observed decrease seems to be more related <strong>with</strong> adsorption <strong>of</strong> oligomers<br />

on the enzyme than <strong>with</strong> catalytic hydrolysis <strong>of</strong> ester groups (Nechwatal et al., 2006).<br />

11. Nitrilases <strong>and</strong> Nitrile Hydratases<br />

Nitrilase was the first nitrile-hydrolysing enzyme described some 40 years ago. It was<br />

known to convert indole 3-acetonitrile to indole 3-acetic acid (Thimann <strong>and</strong><br />

Mahadevan, 1964; Kobayashi <strong>and</strong> Shimizu, 1994). The nitrilase superfamily,<br />

constructed on the basis <strong>of</strong> the structure <strong>and</strong> analyses <strong>of</strong> aminoacid sequence, consists <strong>of</strong><br />

13 branches. Members <strong>of</strong> only one branch are known to have true nitrilase activity,<br />

whereas 8 or more branches have apparent amidase or amide condensation activities<br />

(Pace <strong>and</strong> Brenner, 2001; Brenner, 2002). All the superfamily members contain a<br />

conserved catalytic triad <strong>of</strong> glutamate, lysine <strong>and</strong> cysteine, <strong>and</strong> a largely similar α-β-β-α<br />

structure.<br />

Nitrilases are found relatively frequently in nature. This enzyme activity exists in 3 out<br />

<strong>of</strong> 21 plant families (Gramineae, Cruciferae <strong>and</strong> Musaceae) (Thimann <strong>and</strong> Mahadevan,<br />

1964), in a limited number <strong>of</strong> fungal genera (Fusarium, Aspergillus, Penicillium)<br />

(Harper, 1977; Šnajdrová et al., 2004; Vejvoda et al., 2006; Kaplan et al., 2006) but it is<br />

more frequently found in bacteria. Several genera such Pseudomonas, Klebsiella,<br />

Nocardia <strong>and</strong> Rhodococcus are known to utilize nitriles as sole sources <strong>of</strong> carbon <strong>and</strong><br />

nitrogen (Dhillon et al., 1999; Kiziak et al., 2005; Bhalla <strong>and</strong> Kumar, 2005; Hoyle et<br />

al., 1998; Bhalla et al., 1995). Manly due to the biotechnological potential <strong>of</strong> nitrilases<br />

different bacteria <strong>and</strong> fungi capable <strong>of</strong> hydrolysing nitriles were isolated (Singh et al.,<br />

2006).<br />

26

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