OXIDATIVE DAMAGE TO PROTEOLYTIC-ENZYMES - INACTIVATION OF PAPAIN AND FICIN BY FERRYLMYOGLOBIN

Citation
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
Citations number
15
Categorie Soggetti
Food Science & Tenology
ISSN journal
14314630
Volume
206
Issue
3
Year of publication
1998
Pages
199 - 202
Database
ISI
SICI code
1431-4630(1998)206:3<199:ODTP-I>2.0.ZU;2-6
Abstract
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.