ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
The anthocyanin-decolorizing enzyme which was previously found to he a polyphenol oxidase in eggplant fruits was further purified by DEAE-cellulose column chromatography. At least two different enzymes were prepared, both of which equally oxidized catechol to its o-qui-none as a primary product, indicating their polyphenol oxidase nature, but differed from each other in substrate specificity. One of the two enzymes showed higher activity toward the eggplant anthocyanin and catechol than toward chlorogenic acid. When the anthocyanin was used as a substrate, the pH of maximum enzyme activity was 6.5. The second enzyme was more active on chlorogenic acid, with maximum activity near pH 5.0, and less active on the anthocyanin.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1966.tb00499.x
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