Adsorption of enzymes at the solid-liquid interface: I. Trypsin on polystyrene latex

Abstract

The enzyme, trypsin, has been used to study conformational changes which occur when protein adsorption onto well-characterized, emulsifier-free, polystyrene latex surface takes place. The adsorption isotherm is of the high affinity, Langmuirian type with plateau adsorption of trypsin of 2.8 mg m −2. The enzymic activity of adsorbed trypsin to low molecular weight substrate is found to decrease as the surface coverage decreases indicating that ‘spreading’ or unfolding of the native protein conformation, with consequent loss of enzymic activity, occurs. On the close packed surface such ‘spreading’ is inhibited by steric factors. The view that protein adsorption onto hydrophobic surfaces is dominated by the entropy gain due to protein unfolding to maximize hydrophobic interactions is thus supported.