IDENTIFICATION AND CHARACTERIZATION OF SOME OXIDIZING ENZYMES OF THE MC FARLIN CRANBERRY

SUMMARY– Enzyme extracts were prepared from acetone powders with and without phenol‐binding agents such as polyethylene glycol (PEG) and polyvinylpyrrolidone (PVP) and buffered PVP. The acetone‐PVP combination was found most effective in reducing the polyphenolic content of the enzyme extract. Highest specific activity was obtained by using a buffered PVP extract. The pH optimum of cranberry peroxidase activity was 6.0. Heat inactivation of cranberry peroxidase was determined to follow first order kinetics. There was 90% destruction at 70, 80, and 90°C requiring 9.40, 1.60, and 0.47 min of heat treatment, respectively. Activation energy for the thermal inactivation of cranberry peroxidase was observed to be 37.2 kcal/mole. Guaicol, o‐phenylene diamine (OPDA), and pyrogallol were tested for their sensitivity to cranberry peroxidase with OPDA determined as most sensitive. The pH optimum for catalse activity was found to range from 7.5 to 9.2. Kinetics for the heat inactivation of cranberry catalase was observed not to be of the first order nor zero order. Approximately 50% of the catalase activity was inactivated after heating for 17, 1.8, and 0.6 min at temperatures of 50, 60, and 70°C, respectively. The pH optimum for cranberry polyphenolase activity was determined to be 7.0. Heat inactivation of cranberry poly‐phenolase was found to follow first order kinetics. There was 90% destruction at 50, 60, and 70°C requiring 15.85, 7.05, and 1.37 min of heat treatment, respectively. The activation energy for the inactivation of cranberry polyphenolase was observed to be 27.7 kcal/mole.