Abstract
Adsorption of globular protein, lysozyme, on thermosensitive poly( N-isopropylacrylamide) coated nanomagnetic particles was studied at different temperatures and pHs. It was observed that a maximum amount of lysozyme was adsorbed at a temperature above the lower critical solution temperature (LCST) (32 °C ) of the polymer and at the isoelectric point ( p I = 11 ) of lysozyme. Desorption was carried out using either NaH 2PO 4 (pH 4) or NaSCN (pH 6) as the desorbing agents. Conformational changes in lysozyme on desorption from nanomagnetic particles was studied by circular dichroism and intrinsic fluorescence spectroscopy. Lysozyme desorbed by NaH 2PO 4 showed very little conformational changes while lysozyme desorbed by NaSCN showed significant conformational changes, and 87% enzymatic activity was retained in the desorbed enzyme for desorption by NaH 2PO 4.
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