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William S. Conway, Carl E. Sams, George A. Brown, William B. Beavers, Rowel B. Tobias, and Larry S. Kennedy

A pilot test was conducted over a 3-year period to determine the feasibility of using postharvest pressure infiltration of calcium into apples to maintain and/or improve the quality of fruit under commercial storage conditions. Fruits obtained from three different orchards were treated each year. `Golden Delicious' fruits were treated the first year, while `Delicious' fruits were treated the 2nd and 3rd years. In all treatments and years, there was a significant increase in calcium concentration of apples from all calcium chloride (CaCl2) treatments. In general, calcium concentration of treated fruit varied significantly among the three orchards. Firmness also varied among orchards, and was related to fruit calcium concentration. `Golden Delicious' apples were more susceptible to skin injury caused by CaCl2 treatment than were `Delicious' fruits. There was also an increase in infection as a result of some of the treatments, possibly due to injury caused to lenticels by the pressure applied or as a result of calcium injury.

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William S. Conway, Rowel B. Tobias, Stephane Roy, Alley E. Watada, Stephane Roy, William P. Wergin, and Carl E. Sams

Decay caused by Botrytis cinerea is significantly reduced by increasing the calcium concentration of apple fruit tissue. Electron microscope studies have revealed that cracks in the epicuticular wax may be an important pathway by which calcium penetrates into the fruit and increases the calcium concentration. In fruit inoculated with B. cinerea, the decay induced compositional changes in the cell walls of high-calcium fruit were smaller than those observed in the low calcium treatment. The effect of calcium in reducing decay is associated with maintaining cell wall structure by delaying chemical changes in cell wall composition. B. cinerea produced five polygalacturonase isozymes in vitro but only one in vivo. Among the cations studied-m was the most potent inhibitor of polygalacturonase activity in in vitro studies. Its mode of inhibition appears to involve the alteration of substrate availability for hydrolysis, rather than any direct effect on the active sites of the enzyme.