Abstract
Abstract Pectinesterase (PE) was immobilized by covalent attachment on nylon-polyethylenimine co-polymer and the properties of the immobilized enzyme was investigated. The nylon support was activated both by using dimethyl sulphate (DMS) and triethyloxonium tetrafluoroborate (TOTFB). The suitable conditions for an operative and stable system were investigated. The immobilization of PE on nylon which had been by polyethylenimine (PEI) resulted in some loss of activity because of steric hindrance of pectin. The activity immobilization yielded 8.2% for DMS and 12.7% for TOTFB and higher than the previously reported in the literature. The pH optima and temperature stability of the immobilized PE significantly increased.
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