Performance of d-amino acid oxidase in presence of ionic liquids
Copyright policy )Performance of d-amino acid oxidase in presence of ionic liquids
The activity and stability of free and immobilized D-amino acid oxidase (DAAO, EC 1.4.3.3) from Trigonopsis variabilis CBS 4095 in different water-soluble and water-insoluble ionic liquids (ILs) as well as in organic solvents were studied for comparison. The most promising ILs ([BMIM][BF(4)] and [MMIM][MMPO(4)]) were investigated in detail. The kinetic parameters (v(max) = 187 nkat/g dry weight, K(M) = 1.38 mM) with D-phenylalanine as substrate were calculated in 40% [BMIM][BF(4)]. Bioconversions of D/L-phenylalanine in 40% [BMIM][BF(4)] and 20% [MMIM][MMPO(4)] on a 3 ml scale using immobilized DAAO were performed by addition of free catalase from Micrococcus lysodeikticus. After total conversion of substrate in presence of 20% [MMIM][MMPO(4)] the residual activity of the immobilized DAAO was 79% and 100% of the free catalase.
- University of Hohenheim Germany
D-Amino-Acid Oxidase, Water, Catalase, Enzymes, Immobilized, Catalysis, Micrococcus, Substrate Specificity, Kinetics, Solubility, Enzyme Stability, Saccharomycetales, Solvents, Feasibility Studies, Organic Chemicals, Biotransformation
D-Amino-Acid Oxidase, Water, Catalase, Enzymes, Immobilized, Catalysis, Micrococcus, Substrate Specificity, Kinetics, Solubility, Enzyme Stability, Saccharomycetales, Solvents, Feasibility Studies, Organic Chemicals, Biotransformation
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