RT Journal Article SR Electronic T1 Purification and Some Properties of Peroxidase from de Chaunac Grapes JF American Journal of Enology and Viticulture JO Am J Enol Vitic. FD American Society for Enology and Viticulture SP 128 OP 129 DO 10.5344/ajev.1983.34.2.128 VO 34 IS 2 A1 C. Y. Lee A1 A. P. Pennesi A1 N. L. Smith YR 1983 UL http://www.ajevonline.org/content/34/2/128.abstract AB 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.