Co-Authors:
DRAETTA, I.S., Institute de Tecnologia de Alimentos Campinas, SP. -Brasil Department of Food Technology ARO, The Volcani Center, Bet Dagan, Israel
BEN‐SHALOM, N., Institute de Tecnologia de Alimentos Campinas, SP. -Brasil Department of Food Technology ARO, The Volcani Center, Bet Dagan, Israel
Abstract:
Palmito (Euterpe edulis Mart.) peroxidase was initially prepared as an acetone powder to eliminate phenols and lipids. A 30–80% (NH4)2SO4 fraction was used to characterize some biochemical properties of this enzyme. The main interference during enzyme purification was found to be the interaction of acid carbohydrates with peroxidase. The optimum condition to eliminate this interference was found to be extraction at pH 4.0, which preferentially extracts most of the carbohydrates but not the enzyme. CaCl2 was found to be a compound which selectively precipitates with acid carbohydrates and proteins and increased peroxidase activity. Gel isoelectrofocusing was used to study the interaction between the acid polymers and the proteins. The pH optimum of the enzyme was found to be around 4.0. The molecular weight of the enzyme was estimated to be 40,000. The Km of peroxidase with H2O2 was 2times10−3M and with guaiacol, 4.8 times 10−3M. NaCl, NaF and NaN3 were found to inhibit peroxidase as a function of pH; as the pH decreased, the inhibition increased. Copyright © 1984, Wiley Blackwell. All rights reserved
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