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Phytochemistry

Miklos Faust

ATPase was found in 1000g, 13 000g and 80 00Og fractions from strawberry fruits. The optima pH for ATPase was the same (i.e. 6) for the 3 fractions, which also showed similar substrate specificity. However, the enzyme associated with the 80 000 g fraction showed the highest affinity for ATP and the maximum Vmax/Km value. As the fruit ripened, from the green to dark-red stage, ATPase activity in the 80 000 g fraction increased more than three times. The ATP content of the fruit pulp, which was high at the green stage, decreased as the fruit matured and ripened. Na+ and K+ slightly stimulated enzyme activity associated with the 1000 g,80 000 g and soluble fractions, whereas, Ca2+ and Mg2+ inhibited the enzyme activity in all fractions. However, the extent of inhibition due to divalent cations lessened as the fruit ripened.

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ATPase in ripening strawberries
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Miklos Faust

ATPase in ripening strawberries

ATPase was found in 1000g, 13 000g and 80 00Og fractions from strawberry fruits. The optima pH for ATPase was the same (i.e. 6) for the 3 fractions, which also showed similar substrate specificity. However, the enzyme associated with the 80 000 g fraction showed the highest affinity for ATP and the maximum Vmax/Km value. As the fruit ripened, from the green to dark-red stage, ATPase activity in the 80 000 g fraction increased more than three times. The ATP content of the fruit pulp, which was high at the green stage, decreased as the fruit matured and ripened. Na+ and K+ slightly stimulated enzyme activity associated with the 1000 g,80 000 g and soluble fractions, whereas, Ca2+ and Mg2+ inhibited the enzyme activity in all fractions. However, the extent of inhibition due to divalent cations lessened as the fruit ripened.

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