Record ID No. |
273 |
Author(s) |
Zarivi O., Bonfigli A. , Cesare P., Amicarelli F., Pacioni G., Miranda M. , 2003 |
Affiliation |
Department of Basic and Applied Biology, Faculty of Sciences, University of L'Aquila, Via Vetoio, I-67010 Coppito, L'Aquila, Italy. |
Title |
Truffle thio-flavours reversibly inhibit truffle tyrosinase |
Source. Vol.(no):Page |
FEMS Microbiology Letters. 220(1): 81-88p. |
Categories |
Ectomycorrhiza |
Subjects |
Biochemistry |
Sub-subjects |
Miscellaneous |
Host |
n.a. |
Organism |
n.a. |
Country |
Italy, Europe |
Abstracts |
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 MWr 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. (C) 2003 Published by Elsevier Science B.V. On behalf of the Federation of European Microbiological Societies |