Volume 2, Number 3/4, p. 89-94
L. Gulua, G. Pruidze, N. Mchedlishvili, N. Omiadze and N. Pruidze
Durmishidze Institute of Biochemistry and Biotechnology, Academy of Sciences of Georgia, David Agmasheneblis Kheivani 10 km, 380059 Tbilisi, Georgia
A novel catechol reductase catalytic activity of tea leaf phenol oxidase
Tea leaf (Camelia sinensis L.) phenol oxidase catalytic activity has been investigated. It has been found out that the phenol oxidase can catalyze conversion of diphenols into monophenols, a kind of intermediate product, an activity that has not yet been reported in the literature. Simultaneously another intermediate product containing an oxygen atom non-covalently bound to the enzyme is supposed to form. It is proposed to call this newly-found catalytic activity “catechol reductase” activity. It has been shown that all the multiple forms of the tea leaf phenol oxidase (Mr = 118 000, 41 000 and 28 000) obtained from gel filtration on a Sephadex G-200 column possess catechol reductase activity. The catechol reductase substrate specificity has been assayed.
Key words: amperometric method, Camelia sinensis L, enzyme activity, phenol oxidase, tea.