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Control of polyphenol oxidase activity using a catalytic mechanism

  • D. Osuga
  • A. Van Der Schaaf
  • J. R. Whitaker

Abstract

Polyphenol oxidase is one of the most deteriorative of enzymes, especially in tropical fruits, yet it is essential for color of brown tea, cocoa, coffee, raisins, some figs and prunes and plant protection. It is responsible for the unwanted black-spot formation in shrimp but is important for pigmentation of human skin. In this chapter the mechanism of action of polyphenol oxidase is discussed, including the reactions catalyzed, the kinetics with respect to the two substrates, O2 and phenol, substrate specificity and the intermediates in the reaction. Differences between monophenolase and diphenolase activities are shown mechanistically. Complete amino-acid sequences are available for polyphenol oxidases from humans and mice, Neurospora crassa (fungus), and Streptomyces glaucescens (fungus) and S. antibioticus (fungus). There is 86% strict homology in amino-acid sequence between S. glaucescens and S. antibioticus but only 24% between the Streptomyces enzymes and that from N. crassa. The human and mouse enzymes are 43% homologous; they are much larger than the fungal enzymes and have little homology with the fungal enzymes, except in the activesite histidine residues. There is also much homology between the polyphenol oxidases and hemocyanins around the active-site histidine reactions. Several methods of controlling polyphenol oxidase utilize pH, O2 exclusion, heating, ascorbic acid, sodium bisulfite, thiol compounds, kcat inactivation, competitive inhibitors and removal of phenols.

Keywords

Caffeic Acid Chlorogenic Acid Histidine Residue Polyphenol Oxidase Neurospora Crassa 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • D. Osuga
  • A. Van Der Schaaf
  • J. R. Whitaker

There are no affiliations available

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