Truffle thio-flavours reversibly inhibit truffle tyrosinase
Tyrosinase is an enzyme having two copper atoms at the reactive site occurring in prokaryotic and eukaryotic organisms. In animals tyrosinase is responsible for pigmentation, in plants for protection of injured tissues or, as in fungi, to harden cell walls. Some of us have previously shown that tyro...
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Published in | FEMS microbiology letters Vol. 220; no. 1; pp. 81 - 88 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford, UK
Elsevier B.V
14.03.2003
Blackwell Publishing Ltd Blackwell |
Subjects | |
Online Access | Get full text |
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Summary: | Tyrosinase is an enzyme having two copper atoms at the reactive site occurring in prokaryotic and eukaryotic organisms. In animals tyrosinase is responsible for pigmentation, in plants for protection of injured tissues or, as in fungi, to harden cell walls. Some of us have previously shown that tyrosinase is involved in truffle development and differentiation. Here we present the purification, the molecular properties and the reversible inhibition of
Tuber melanosporum tyrosinase by dimethyl-sulfide and bis[methylthio]methane, the main flavour compounds of black and whitish truffles. The MW
r is 39 000.
L-3,4-dihydroxyphenylalanine and
L-tyrosine stain corresponding bands as expected for a true tyrosinase. Phenylthiourea, diethyldithiocarbamate and mimosine inhibit
L-tyrosine and
L-3,4-dihydroxyphenylalanine oxidation. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0378-1097 1574-6968 |
DOI: | 10.1016/S0378-1097(03)00065-X |