Enhancing stability and oxidation activity of cytochrome c by immobilization in the nanochannels of mesoporous aluminosilicates

The hydrothermal stability and oxidation activity of cytochrome c (cty c) by immobilization in the nanochannels of mesoporous aluminosilicates were discussed. The cytochrome c immobilized in MAS-9 undergo facile unfolding during hydrothermal stability. The stability and high catalytic activity of cyt c immobilized in mesoporous silicas were attributed to the electrostatic attraction between the pore surface and cyt c and the confinement provided by nanochannels. It was found that by increasing the concentration of the spin trapping agent, cyt c catalyzes a homolytic cleavage of the O-O bond of hydroperoxide and generates a protein cation radicals.