TY - JOUR T1 - Purification and Some Properties of Peroxidase from de Chaunac Grapes JF - American Journal of Enology and Viticulture JO - Am J Enol Vitic. SP - 128 LP - 129 DO - 10.5344/ajev.1983.34.2.128 VL - 34 IS - 2 AU - C. Y. Lee AU - A. P. Pennesi AU - N. L. Smith Y1 - 1983/01/01 UR - http://www.ajevonline.org/content/34/2/128.abstract N2 - By using two columns, DEAE-cellulose and phenyl sepharose CL-4B resins, a homogeneous grape peroxidase could be isolated. The specific activity was increased to nearly 16-fold, and the enzyme gave a single band on gel electrophoresis. The temperature and pH optima of the purified enzyme were 47°C and 6.0, respectively. The apparent Km for guaiacol as a substrate was 1.2 mM at optimum hydrogen peroxide concentration. ER -