ИСТИНА

Oral presentation D-amino acid oxidase from Trigonopsis variabilis (TvDAAO) is a FAD-containing enzyme which catalyses the oxidative deamination of various D-amino acids. TvDAAO is used in biosensors, fine organic synthesis and two-enzyme biocatalytic process of preparation of 7-aminocephalosporanic acid from cephalosporine C (CephC). TvDAAO shows moderate stability and wide spectrum of substrate specificity. That is why in most cases properties of the enzyme have to be tuned to get maximum efficiency in certain process. Construction of model 3D structure of TvDAAO [1] provided efficient background for protein engineering of catalytic properties and stability of the enzyme using rational design approach. We prepared more than 25 mutant TvDAAOs with amino acid changes in different parts of active site. New mutants showed increased thermal stability and improved activity and selectivity with different D amino acids including CephC.