Pyridine nucleotide oxidizing enzymes of Lactobacillus casei

摘要: Abstract The soluble DPNH oxidase and peroxidase activities of Lactobacillus casei were isolated in partially purified form their properties examined. two could not be separated by any the techniques protein separation that employed. is an FAD enzyme retains its flavin tenaciously during purification. It very specific for hydrogen peroxide as electron acceptor effective with methylene blue, indophenol, benzoquinone, similar compounds. inhibited strongly p -hydroxymercuribenzoate moderately N -ethylmaleimide, but cyanide, amytal, or versene. also a flavoprotein, loses activity isolation on storage reaches maximal only when incubated thiol compound FAD. Oxygen, FAD, blue will serve acceptor, FMN ferri-cyanide are totally inactive. was affected significantly inhibitors tested.