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A novel thermostable d-amino acid oxidase of the thermophilic fungus Rasamsonia emersonii strain YA
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A novel thermostable d-amino acid oxidase of the thermophilic fungus Rasamsonia emersonii strain YA
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Journal Article
A novel thermostable d-amino acid oxidase of the thermophilic fungus Rasamsonia emersonii strain YA
2019
Overview
d-
Amino acid oxidase (DAAO) is a valuable flavoenzyme capable of being used in various practical applications, such as in determining
d
-amino acids and producing a material for semisynthetic cephalosporins, requiring higher thermal stability, higher catalytic activity, and broad substrate specificity. In this study, we isolated the thermophilic fungus
Rasamsonia emersonii
strain YA, which can grow on several
d
-amino acids as the sole nitrogen source, from a compost and characterized DAAO (ReDAAO) of the fungus. ReDAAO expressed in
Escherichia coli
exhibited significant oxidase activity against various neutral and basic
d-
amino acids, in particular hydrophobic
d
-amino acids. In addition, the enzyme also significantly acted on cephalosporin C, a starting material for semisynthetic antibiotics, and
d-
Glu, a general substrate for
d-
aspartate oxidase but not for DAAO, showing its unique and practically useful substrate specificity. The apparent
k
cat
and
K
m
values of the enzyme toward good substrates were comparable to those of higher catalytic fungal DAAOs, and the thermal stability (
T
50
value of ~60 °C) was comparable to that of a thermophilic bacterial DAAO and significantly higher than that of other eukaryotic DAAOs. These results highlight the great potential of ReDAAO for use in practical applications.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 45/23
/ 82/29
/ 82/80
/ 82/83
/ D-Amino-Acid Oxidase - chemistry
/ D-Amino-Acid Oxidase - genetics
/ D-Amino-Acid Oxidase - isolation & purification
/ D-Amino-Acid Oxidase - metabolism
/ E coli
/ Enzymes
/ Escherichia coli - metabolism
/ Fungal Proteins - isolation & purification
/ Fungal Proteins - metabolism
/ Fungi
/ Genetic Vectors - metabolism
/ Humanities and Social Sciences
/ Hydrophobic and Hydrophilic Interactions
/ Kinetics
/ Protein Interaction Domains and Motifs
/ Protein Structure, Secondary
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Science
