[Enzyme immobilization on hydrated oxides of transition metals and aluminum].
The immobilization of alpha-chymotrypsin, trypsin and invertase on hydrated oxides of tin, titanium and aluminium was investigated. The degree at which the enzymes were bound upon immobilization was 83.2-2.6%. The amount of bound proteins was 64.2 mg/g carrier. The specific activity of enzymes reached the highest level in the case of hydrated tin oxide and amounted to 76.8%, 49.9% and 99.6%, of activity of native alpha-chymotrypsin, trypsin and invertase, respectively. The thermal stability of immobilized proteases was considerably higher and that of immobilized invertase was significantly lower than that of native enzymes. The pH optimum of immobilized enzymes shifted by 0.6-2.6 units towards the alkaline region.
[Enzyme immobilization on hydrated oxides of transition metals and aluminum]. The immobilization of alpha-chymotrypsin, trypsin and invertase on hydrated oxides of tin, titanium and aluminium was investigated. The degree at which the enzymes were bound upon immobilization was 83.2-2.6%. The amount of bound proteins was 64.2 mg/g carrier. The specific activity of enzymes reached the highest level in the case of hydrated tin oxide and amounted to 76.8%, 49.9% and 99.6%, of activity of native alpha-chymotrypsin, trypsin and invertase, respectively. The thermal stability of immobilized proteases was considerably higher and that of immobilized invertase was significantly lower than that of native enzymes. The pH optimum of immobilized enzymes shifted by 0.6-2.6 units towards the alkaline region.