L'hydrolyse des hétérosides terpéniques du Muscat a petits grains par les enzymes périplasmiques de Saccharomyces cerevisiae

Abstract

Osidases located in periplasmic space of Saccharomyces cerevisiae are able to hydrolyse monoterpenes heterosides of Muscat grapes. To prepare the periplasmic extract, yeast cell walls are digested with Zymolyase in the presence of an osmotic protector to prevent lysis of the resulting protoplasts; periplasmic enzymes are liberated into the supernatant medium. Monoterpenes heterosides are incubated 48 or 72 hours at 25° C with either intact yeast cells or periplasmic enzymatic extract. Monoterpenes, especially gerianol and nerol, are liberated in these conditions. β-glucosidase activity seems to play an important rôle in these reactions.

Fungal extracellular β-glucosidases are commonly strongly inhibited by glucose. Surprisingly, the activity of periplasmic yeast β-glucosidase is quite glucose independant. These results suggest that some periplasmic enzymes from yeast may be involved in the hydrolysis of varietal aroma precursors in wines.