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In this study, three different approaches for the covalent immobilisation of the horseradish peroxidase
(HRP) onto epoxy-activated acrylic polymers (Eupergit®C) were explored for the first time, direct HRP
binding to the polymers via their oxirane groups, HRP binding to the polymers via a spacer made from
adipic dihydrazide, and HRP binding to hydrazido polymer surfaces through the enzyme carbohydrate
moiety previously modified by periodate oxidation. The periodate-mediated covalent immobilisation
of the HRP on hydrazido Eupergit®C was found to be the most effective method for the preparation of
biocatalysts. In this case, amaximumvalue of the immobilised enzyme activity of 127 U/gsupport was found
using an enzyme loading on the support of 35.2 mg/gsupport. The free and the immobilised HRP were used
to study the elimination of phenol in two batch reactors. As expected, the activity of the immobilised
enzyme was lower than the activity of the free enzyme. Around 85% of enzyme activity is lost during
the immobilisation. However, the reaction using immobilised enzyme showed that it was possible to
reach high degrees of phenol removal (around 50%) using about one hundredth of the enzyme used in
the soluble form.
CitationPramparo, L. [et al.]. Immobilisation of horseradish peroxidase on Eupergit®C for the enzymatic elimination of phenol. "Journal of hazardous materials", 15 Maig 2010, vol. 177, núm. 1-3, p. 990-1000.
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