Mathematical modelling of amino acid resolution catalyzed by L-amino acid oxidases from Crotalus adamanteus and Crotalus atrox

Amino acid resolutionwas studied in this paper. L-Methionine and DL-methioninewere used as substr for the two snake venom L-amino acid oxidases (from Crotalus adamanteus and Crotalus atrox). E though these enzymes have similar background, they exhibit differences as well as similarities. It found that both enzymes are active towards L-methionine as substrate (Vm = 0.78 mmol min 1 g ) have similar affinities (KL met m (C. adamanteus) = 0.19 mM, K L met m (C. atrox) = 0.25 mM). Both enzy were inhibited in the presence of 2-oxo-4-methylthiobutyric acid (K2 oxo i (C. adamanteus) = 0.83 m K2 oxo i (C. atrox) = 2.04 mM), a reaction product of L-methionine oxidative deamination. L-Amino oxidase from C. atrox was found to be inhibited by the substrate as well. L-Amino acid oxidase fro adamanteus was inhibited by D-enantiomer of L-methionine (KD met i 1⁄4 1:41mM). Both enzymes w successful in L-methionine oxidation in the batch reactor (100% conversion). This was not the case in continuously operated enzyme membrane reactor where enzyme deactivation occurred. 2008 Elsevier Ltd. All rights reser