Author： Villalonga Reynaldo Fragoso Alex Cao Roberto Ortiz Pedro D. Villalonga Maria L. Damiao Angelo E.
Publisher： Taylor & Francis Ltd
ISSN： 1061-0278
Source： Supramolecular Chemistry, Vol.17, Iss.5, 2005-08, pp. : 387-391
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Abstract
Bovine pancreatic trypsin was immobilized on β- and γ-cyclodextrin coated gold nanospheres via supramolecular associations. The enzyme retained 100%–120% of its catalytic activity and its thermal stability at 50°C was 2–2.5 fold increased in the presence of the β- and γ-cyclodextrin modified metal nanoparticles, respectively. The influence of these immobilization processes on the conformational properties of the enzyme was studied by fluorescence spectroscopy. These results open a new perspective to the possible application of cyclodextrin-modified gold nanospheres as water-soluble carriers for enzyme immobilization.
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