Preparation and characterization of isolubilized L ‐amino acid oxidase

The enzyme L‐amino acid oxidase of Crotalus adamanteus was covalently coupled to porous 96% silica glass particles. The insolubilized enzyme was active on several L‐amino acids including: leucine, isoleucine, cysteine, phenylalanine, tryptophane, and methionine. No activity was observed with D‐amino acids, L‐asparagine, or L‐proline. Maximum activity was observed at pH 7.8. Stability of the enzyme derivative was demonstrated by continuous operation of an enzyme column for 35 days, during which the bound enzyme oxidized over 5000 times its own weight of substrate.