A. Mikkelsen et Lh. Skibsted, OXIDATIVE DAMAGE TO PROTEOLYTIC-ENZYMES - INACTIVATION OF PAPAIN AND FICIN BY FERRYLMYOGLOBIN, ZEITSCHRIFT FUR LEBENSMITTEL-UNTERSUCHUNG UND-FORSCHUNG A-FOOD RESEARCH AND TECHNOLOGY, 206(3), 1998, pp. 199-202
Ferrylmyoglobin [MbFe(IV)=O], formed by activation of metmyoglobin by
hydrogen peroxide, inactivates the cysteine proteinases papain (EC 3.4
.22.2) and ficin (EC 3.4.22.3) more efficiently than hydrogen peroxide
, but less efficiently than hydroxyl radicals as generated by peroxyni
trite nitrite or the Fenton reaction. Metmyoglobin and oxymyoglobin co
uld not inactivate papain and ficin. Oxidation of papain and ficin by
ferrylmyoglobin occurs in enzyme/ haem-protein complexes with binding
constants of approximately 10(5) 1 mol(-1); inactivation of proteolysi
s by papain plateaus at neutral pH to about 1/3 whereas the inactivati
on under acidic conditions was larger.