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 inFEMS microbiology letters Vol. 220; no. 1; pp. 81 - 88
Main Authors Zarivi, Osvaldo, Bonfigli, Antonella, Cesare, Patrizia, Amicarelli, Fernanda, Pacioni, Giovanni, Miranda, Michele
Format Journal Article
LanguageEnglish
Published Oxford, UK Elsevier B.V 14.03.2003
Blackwell Publishing Ltd
Blackwell
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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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ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(03)00065-X