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Choline oxidase catalyzes the four-electron oxidation of choline to glycine-betaine, with betaine-aldehyde as intermediate and molecular oxygen as primary electron acceptor. The enzyme can also accept betaine-aldehyde as a substrate. This allows the investigation of the reaction mechanism for the conversion of choline to the aldehyde intermediate and of betaine-aldehyde to glycine-betaine. The enzyme is a flavoprotein with a molecular weight of approximately 83,000 Da according to gel filtration or approximately 71,000 Da according to SDS gel electrophoresis. The optimum pH is found to be around pH 7.5 and the isoelectric point (pI) around pH 4.5.