Comment on “Direct Electrochemistry and Electrocatalysis of Heme Proteins Entrapped in Agarose Hydrogel Films in Room-Temperature Ionic Liquids”

Kinetics of oxidation of hydrogen peroxide at hemin-modified electrodes in nonaqueous solvents

“…The lower values of k cat / K m app are compensated by the higher surface concentration of hemin compared to the lower coverages obtained with native enzymes [42], leading to higher catalytic currents and sensitivity for the hemin sensor. Hemin-modified electrodes displayed higher currents in aqueous buffer than in all nonaqueous solvents tested.…”

Evidence for heme release in layer-by-layer assemblies of myoglobin and polystyrenesulfonate on pyrolitic graphite

“…Using this kind of indirect evidence, we have shown that myoglobin (Mb) in films of didodecyldimethylammonium bromide (DDAB) on pyrolitic graphite can undergo heme release under certain conditions [15,16], although our conclusions were disputed by Guto and Rusling [17]. Another case in which partial or complete heme removal from Mb has been suggested is for Mb in agarose hydrogel films in ionic liquids [18].…”

Compatibility of Ionic Liquids with Enzymes

“…Immobilization of enzymes on the solid carriers or supports is a routine method for improving the enzyme stability in organic solvents as well as in ionic liquids. The supports can be resins [14] (e.g., Novozym 435, lipase B from Candida antartica immobilized on acrylic resin, the most commercially available well-known immobilized enzyme), carbon nanotube [62][63][64], agarose hydrogel film [65][66][67], and magnetic silica particles [68]. Furthermore, enzymes can be immobilized by sol-gel encapsulation which is a technique for entrapping biomolecules in polymer matrix via non-covalent interactions between the polymer network and biomolecules [69,70].…”