PT  - JOURNAL ARTICLE
AU  - D. Temple
AU  - C. S. Ough
TI  - Inhibition of Catalase Activity in Wines
AID  - 10.5344/ajev.1975.26.2.92
DP  - 1975 Jan 01
TA  - American Journal of Enology and Viticulture
PG  - 92--96
VI  - 26
IP  - 2
4099  - http://www.ajevonline.org/content/26/2/92.short
4100  - http://www.ajevonline.org/content/26/2/92.full
SO  - Am J Enol Vitic.1975 Jan 01; 26
AB  - Catalase (fungal source) was found to be essentially completely inhibited by wine concentrations of ethanol. The inhibition is noncompetitive and apparently involves the binding of the ethanol with the enzyme in the compound I form, thereby inhibiting the catalatic reaction. The peroxidatic reaction then is either extremely slow, or does not proceed to form acetaldehyde, but removes the enzyme from further catalatic reactions. The Km of the reaction (H2O2→ H2O + ½ O2) is 0.02 M and Vmax was 2.2 x 103 µ moles/min. Malic acid, grape seed tannin, catechol, chlorogenic acid and gallic acid did not affect catalase activity. The ethanol concentration in wine accounts for essentially all the inhibition found.