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INTERFERENCE OF CARBOHYDRATES DURING PURIFICATION OF PEROXIDASE FROM PALM ( EUTERPE EDULIS MART. ) *
Author(s) -
DRAETTA IACY S.,
BENSHALOM NOACH
Publication year - 1984
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1984.tb00319.x
Subject(s) - guaiacol , peroxidase , chemistry , enzyme , acetone , extraction (chemistry) , phenols , biochemistry , chromatography , food science
Palmito (Euterpe edulis Mart. ) peroxidase was initially prepared as an acetone powder to eliminate phenols and lipids. A 30–80% (NH 4 ) 2 SO 4 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. CaCl 2 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 H 2 O 2 was 2times10 −3 M and with guaiacol, 4.8 times 10 −3 M. NaCl, NaF and NaN 3 were found to inhibit peroxidase as a function of pH; as the pH decreased, the inhibition increased.