Influence of pH, benzoic acid, EDTA, and glutathione on the pressure and/or temperature inactivation kinetics of mushroom polyphenoloxidase

• Published in: Biotechnology progress 1997, Vol.13 (1), p.25-32
• Main Authors: Weemaes, Carla A., De Cordt, Susanna V., Ludikhuyze, Linda R., Van den Broeck, Ilse, Hendrickx, Marc E., Tobback, Paul P.
• Format: Article
• Language: English
• Subjects: Basidiomycota - enzymology; Benzoates - pharmacology; Benzoic Acid; Biological and medical sciences; Biotechnology; Catechol Oxidase - antagonists & inhibitors; Catechol Oxidase - chemistry; champignon comestible; Edetic Acid - pharmacology; edible fungi; Enzyme engineering; Enzyme Stability; Fundamental and applied biological sciences. Psychology; Glutathione - pharmacology; Growth, nutrition, metabolism, transports, enzymes. Molecular biology; Hydrogen-Ion Concentration; Kinetics; Methods. Procedures. Technologies; Microbiology; Miscellaneous; Mycology; oxidoreductases; oxidorreductasas; oxydoreductase; Pressure; setas comestibles; Temperature
• ISSN: 8756-7938; 1520-6033
• DOI: 10.1021/bp960065z

The pressure and/or temperature inactivation of mushroom polyphenoloxidase (PPO) in the absence and presence of EDTA, benzoic acid, and glutathione was studied on a kinetic basis. In addition, the effect of pH was evaluated. The temperature stability of PPO at atmospheric pressure increased with increasing pH up to pH 6.5. The pressure stability of PPO at room temperature (25 °C) also increased with increasing pH. EDTA slightly increased the thermal stability of the enzyme but did not alter the pressure stability of PPO. Benzoic acid protected the enzyme toward temperature but caused sensitization toward pressure when used at a concentration of 50 mM. Glutathione produced sensitization to both temperature and pressure. It is suggested that the sensitizing effect of glutathione is due to an interaction with a disulfide bond of the enzyme.