Abstract
β-Glucuronidase (EC 3.2.1.31), From Patella vulgala, was immobilized on a pellicular, polyethyleneimine-derivatized nylon net. Several types of nylon nets were used in order to ensure the best relationship between activity of the immobilized enzyme and net characteristics. No differences were observed between the two most used reagents for nylon activation by alkylation under standard working conditions. The influence of attachment by several protein aminoacidic side chains was determined, and enzyme immobilization involving lysyl and tyrosyl protein residues showed better activity. Coupling conditions for these derivatives have been optimized by studying the influence of pH, temperature and reaction time on derivative activity. The saturation profiles obtained for these derivatives showed a high protein content, 30mg/g, for a non-porous support. Characterization of these derivatives against pH, ionic strength and temperature was also studied, and no differences were found between soluble and immobilized ...
Published Version
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