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1.The inactivation temperature of the oxidase of fruits is of interest in

connection with the processing of fruits and fruit products by heat, as inactivation

of the oxidase is essential to retention of the original fruit color.

OVERHOLSER and CRUESS (4) in 1923 reported that the organic peroxide

of fresh apple juice was temporarily inactivated by 20 minutes heating at

73.5° C. and the peroxidase by 20 minutes at 900 C. While the inactivation

of fruit catalase by heat was not investigated by us except incidentally, it

is of interest to mention the results reported by MORGULIS, BEBER and

RABKIN (3) who found that the pH value of the medium exerted a marked

effect on the temperature required for inactivation of catalase from beef

kidneys.

GALLAGHER (2) has reported on the behavior of the peroxidase of the

mangold after heating at 1000 C. but gives no data on the effect of hydrogenion

concentration. CRUESS and FONG (1) have reported preliminary observations

on the effect of pH value on the inactivation temperature of oxidase

in certain fruit juices.

2.Summary

The temperature required for the inactivation of the peroxidase of apricots,

pears, peaches, prunes, figs, lemon peel, tomato, banana and dates was

found to vary with the hydrogen-ion concentration. Resistance to heat was

greatest in the range of pH 5 to 7. Resistance decreased with decrease in

pH value between pH 5 and 2, and decreased with increase in pH value

between pH 8 and 12. At pH 12 and pH 2-2.2 the peroxidase was inactivated

at room temperature in 24 hours or less.

The organic peroxide behaved similarly to the peroxidase between pH 2

and 7. At pH values above pH 8 the organic peroxide failed to give positive

tests. There was considerable evidence that the inactivating effect of

temperature at any given pH is progressive rather than abrupt.

FRUIT PRODUCTS LABORATORY,

UNIVERSITY OF CALIFORNIA.

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