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PARTIAL PURIFICATION AND PROPERTIES OF PUMPKIN LIPOXYGENASE WITH CAROTENE‐BLEACHING ACTIVITY
Author(s) -
HIDAKA TOSHIRO,
KATSUKI SUNAO,
NAGATA YASUO,
NAKATSU SEIICHIRO
Publication year - 1986
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.1745-4514.1986.tb00089.x
Subject(s) - chemistry , lipoxygenase , carotene , chromatography , size exclusion chromatography , ammonium sulfate , cyanide , ascorbic acid , enzyme , ion chromatography , enzyme assay , biochemistry , inorganic chemistry , food science
From locally grown pumpkins, an active lipoxygenase preparation with an active carotene‐bleaching factor was partially purified by ammonium sulfate fractionation, gel filtration, and ion‐exchange chromatography. The enzyme had a pH optimum at 6.5 and was inactive at pH below 3 and above 10. The maximum activity occurred at 30°C. The apparent K m determined in the presence of linoleate was 0.33 × 10 −3 M. The heavy metals Hg 2+ , Cu 2+ , Co 2+ , and Fe 3+ were effective inhibitors of this enzyme. Cyanide, fluoride, and L‐ascorbic acid also inhibited lipoxygenase activity. Carotene‐bleaching activities operated strongly on the lipoxygenase fraction and slightly on the denatured lipoxygenase and hemoproteins treated with heat.