PURIFICATION AND CHARACTERIZATION OF AN INTRACELLULAR PEROXIDASE FROM STREPTOMYCES-CYANEUS

An intracellular peroxidase (EC 1.11.1.7) from Streptomyces cyaneus was purified to homogeneity. The enzyme had a molecular weight of 185,000 and was composed of two subunits of equal size. It had an isoelectric point of 6.1. The enzyme had a peroxidase activity toward o-dianisidine with a K(m) of 17.8-mu-M and a pH optimum of 5.0. It also showed catalase activity with a K(m) of 2.07 mM H2O2 and a pH optimum of 8.0. The purified enzyme did not catalyze C-alpha-C-beta bond cleavage of 1,3-dihydroxy-2-(2-methoxyphenoxy)-1-(4-ethoxy-3-methoxyphenyl) propane, a nonphenolic dimeric lignin model compound. The spectrum of the peroxidase showed a soret band at 405 nm, which disappeared after reduction with sodium dithionite, indicating that the enzyme is a hemoprotein. Testing the effects of various inhibitors on the enzyme activity showed that it is a bifunctional enzyme having catalase and peroxidase activities.