Zeitschrift für Lebensmitteluntersuchung und -Forschung A

, Volume 206, Issue 3, pp 199–202

Oxidative damage to proteolytic enzymes: inactivation of papain and ficin by ferrylmyoglobin

  • Anni Mikkelsen
  • L. H. Skibsted
ORIGINAL PAPER

DOI: 10.1007/s002170050242

Cite this article as:
Mikkelsen, A. & Skibsted, L. Z Lebensm Unters Forsch (1998) 206: 199. doi:10.1007/s002170050242

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 peroxynitrite or the Fenton reaction. Metmyoglobin and oxymyoglobin could not inactivate papain and ficin. Oxidation of papain and ficin by ferrylmyoglobin occurs in enzyme/haem-protein complexes with binding constants of approximately 105 l · mol–1; inactivation of proteolysis by papain plateaus at neutral pH to about 1/3 whereas the inactivation under acidic conditions was larger.

Key words Proteolytic enzymesOxidative damageHypervalent myoglobin

Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • Anni Mikkelsen
    • 1
  • L. H. Skibsted
    • 1
  1. 1.Department of Dairy and Food Science, The Royal Veterinary and Agricultural University, Rolighedsvej 30, DK-1958 Frederiksberg C, DenmarkDK