Abstract
A non-particulate o-diphenol: O2 oxidoreductase (phenolase) has been isolated from leaves of sugar cane. Gel filtration produced two fractions MW 32000 and 130000. The preferred substrate was chlorogenic acid. Other o-diphenols (caffeic acid, catechol, pyrogallol, dihydroxyphenylalanine) all of which were slowly oxidized when tested alone, increased the rates of O2 consumption obtained with catalytic amounts of chlorogenic acid. Both enzyme fractions were inhibited by thiols; thioglycollate, which acted in a non-competitive manner, was most effective.
Original language | English (US) |
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Pages (from-to) | 2703-2708 |
Number of pages | 6 |
Journal | Phytochemistry |
Volume | 13 |
Issue number | 12 |
DOIs | |
State | Published - Dec 1974 |
Externally published | Yes |
Keywords
- Gramineae
- MW determination, chlorogenic acid, substrate specificity, inhibition, thioglycollic acid.
- Saccharum sp.
- phenoloxidase
- sugar cane
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Plant Science
- Horticulture