Abstract
<p style="text-align: justify;">4-mercapto-4-methylpentan-2-one (4-MMP), a strongly odorant compound responsible for the « boxtree » or « broom plant » odour of the Sauvignon wines, can be enzymaticaly released <em>in vitro</em> from an odourless must extract. The enzyme source used is a cell-free extract of the gastrointestinal bacterium <em>Eubacterium limosum</em>. This crude preparation exhibits a cysteine β-lyase activity which requires the presence of pyridoxal phosphate. The release of 4-MMP is inhibited when the substrate is previously treated with N-hydroxysuccimide acetate which reacts with a primary amine. The same bacterial extract is also able to release 4-MMP, pyruvic acid and ammonium, from S-(4-méthylpentan-2-one)-L-cysteine. On the other hand, the cleavage of S-(4-méthylpentan-2-one)D,L-homocysteine and S-(4-méthylpentan-2-one)- glutathione is very limited. These results suggest that the precursor of 4-MMP in Sauvignon must is a S-cysteine conjugate. Such an aroma precursor in grapes or in other fruits has never been round berore.</p>
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