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The thermal analysis methods were used for the description of the adsorption behaviour of selected proteins differing in internal stability (ovalbumin (OVA) and lysozyme (LSZ)). These proteins were immobilised on the surface of activated biocarbon obtained from the horsetail herb precursor. The values of the hydrodynamic radius of both biopolymer macromolecules in the solution were determined by the use of the viscosimetry method. This parameter is important for the specification of the possibility of proteins nano-molecules to penetrate the nano-pores of the adsorbent which leads to the increase of biopolymers adsorption. Such behaviour is observed at the pH value which is very close to the pI value of specific biopolymer (the greatest adsorption of proteins on the activated carbon surface occurs- at pH 5 for OVA being 323 mg/g, as well as at pH 11 for LSZ which is 464 mg/g). Under such conditions, the proteins macromolecules assume conformations characterized by the lowest values of hydrodynamic radius, i.e. 2.76 nm for OVA and 1.07 nm for LSZ. The data obtained from the analysis of gaseous products of thermal decomposition of the samples indicated the types of biocarbon surface groups as well as the enabled specification of the protein macromolecules adsorption mechanism.

applied nanoscience

Adsorption, viscosity and thermal behaviour of nanosized proteins with different internal stability immobilised on the surface of mesoporous activated biocarbon obtained from the horsetail herb precursor