Cloning, Expression and Functional Characterization of the D-Amino Acid Oxidase from Rhodosporidium Diobovatum
Journal Title: International Journal of Engineering and Science Invention - Year 2018, Vol 7, Issue 5
Abstract
D-Amino Acid Oxidases(DAAO) Catalyze The Enantioselective Oxidation Of A Broad Variety Of D-Amino Acids To Their Corresponding Α-Amino Acids, Which Spontaneously Hydrolyze To Α-Keto Acids And Ammonium. The Enzyme Of Some Species Has Been Reported. But, In This Study, The Complete Nucleotide Sequence Of The DAAO In The Basidiomycetes Rhodosporidium Diobovatum Has Been Determined. The DAAO Gene Of R. Diobovatum Was Isolated Using Methods Of RACE And RT-PCR. The Results Showed That The Encoded Polypeptide Holds A Sequence Of 357 Amino Acid Residues With Homology To Those Of DAAO From Other Yeasts. The Deduced Protein Molecular Weight Is 38.33 Kda, Theoretical Isoelectric Point Is 7.60. The Expression Vectors Pet-DAAO Was Constructed And Expressed In Escherichia Coli. D-Amino Acid Oxidase Activity On Cephalosporin C Showed A Maximum Around 24℃ And The Optimum Reaction Ph Range From 7.5-8.5.
Authors and Affiliations
Wen Xu, Min Kong, Hongpeng Wang, Hui Tang, Liping Zhang
Keywords
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