PROPERTIES OF IAA OXIDASE FROM RIPENING TOMATO FRUIT
ANN E. HUANG
Department of Food Science Rutgers, The State University Cook College New Brunswick, New Jersey 08903
Search for more papers by this authorNORMAN F. HAARD
Department of Food Science Rutgers, The State University Cook College New Brunswick, New Jersey 08903
Department of Biochemistry, Memorial University of Newfoundland, St. John's, Newfoundland, Canada A1C-5S7
Search for more papers by this authorANN E. HUANG
Department of Food Science Rutgers, The State University Cook College New Brunswick, New Jersey 08903
Search for more papers by this authorNORMAN F. HAARD
Department of Food Science Rutgers, The State University Cook College New Brunswick, New Jersey 08903
Department of Biochemistry, Memorial University of Newfoundland, St. John's, Newfoundland, Canada A1C-5S7
Search for more papers by this authorAbstract
An indoleacetic acid (IAA) oxidizing enzyme was isolated from the pericarp of ripening tomato fruit by column chromatography fractionation. IAA oxidase from extracts of tomato pericarp exists in a high molecular weight form (>200,000) or in a low molecular weight form (∼40,000) or both depending upon extraction procedures. When IAA was oxidized by the high molecular weight form of IAA oxidase, a relatively long lag time was observed. The low molecular weight form of IAA oxidase activity showed no lag or a very short, 1- to 2-minute lag period. Enzyme activity was optimal at pH 6.1 and was stimulated by 2,4-dichlorophenol (DCP) and MnCl2. Neither 3-methyleneoxindole nor indolealdehyde were found as a major IAA oxidation products. Moderate increase in activity of IAA oxidase activity was observed during ripening of tomato fruit.
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