Inhibition by yeast strain of tyrosinase activity in must and wine
DOI:
https://doi.org/10.5073/vitis.1975.14.302-314Abstract
The course of tyrosinase activity in musts is related to the strain of yeast used; with strain 633 the activity becomes practically non-detectable during the first days of growth. With other strains a drastic drop always occurs during the first 48 hours, followed by a recovery during the exponential phase of growth, in correlation to a substantial fall of phenols and to the exponential rise in colour. The inhibitory power on the tyrosinase in vitro is a widespread character in the yeast, even if quantitatively different: this character is not always associated with colour stability. Such a character, possessed to a remarkable measure by strains 633 and 36, is bound to the biosynthesis, even in synthetical media, of a compound capable of becoming bound to the protein units of enzyme, thus preventing the enzyme activity.
Inhibition par la souche de levure de l'activité de la tyrosinase du moût et du vin
Le cours de l'activité de la tyrosinase dans les moûts est rélié à la souche de levure employée: la souche 633 rend l'activité pratiquement inexistante pendant les premiers jours de son dévéloppement. D'autres souches provoquent une baisse drastique pendant les premières 48 heures, suivie par un récouvrement de l'activité de la tyrosinase pendant la phase exponentielle de leur dévéloppement en corrélation à une chute substantielle des composés phénoliques totaux et à la hausse exponentielle de la couleur. Le pouvoir inhibiteur sur la tyrosinase in vitro est un caractère diffusé des levures bien que quantitativement différent; ce caractère n'est pas toujours associé à la stabilité de la couleur des vins blancs. Tel caractère, possedé d'une façon remarquable par les souches 633 et 36, est lié à la biosynthèse, même dans les substrats synthétiques, d'un composé capable de se lier aux unités protéiques de l'enzyme, de façon à prévenir l'activité enzymatique.
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