Subunit fusion of two yeast D-amino acid oxidases enhances their thermostability and resistance to H2O2

doi:10.1007/s10529-008-9694-5

機構典藏 > College of Sciences > Graduate Institue of Life Sciences > Journal Article > Item 987654321/61895

Please use this identifier to cite or link to this item: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/61895

Title:	Subunit fusion of two yeast D-amino acid oxidases enhances their thermostability and resistance to H2O2
Authors:	Wang, Shih-juei;Yu, Chi-yang;Lee, Cheng-kang;Chern, Ming-kai;Kuan, I-ching
Contributors:	淡江大學生命科學研究所
Keywords:	D-Amino acid oxidase;Gene fusion;Rhodosporidium toruloides;Stability;Trigonopsis variabilis
Date:	2008-08
Issue Date:	2011-10-17 01:01:05 (UTC+8)
Publisher:	Dordrecht: Springer Netherlands
Abstract:	D-Amino acid oxidases from Rhodosporidium toruloides and Trigonopsis variabilis (RtDAO and TvDAO) are both yeast homodimeric flavoenzymes. Two of their cDNA genes were connected by a hexanucleotide linker and heterologously expressed in E. coli to produce the corresponding double DAOs (dRtDAO and dTvDAO) with two subunits fused into a single polypeptide. The specific activities of double DAOs remained similar to those of native dimeric DAOs, although the catalytic efficiencies (kcat/KM) were decreased due to higher KM values. The Tm value for dRtDAO was shifted 5°C higher while that for dTvDAO was increased only by 2°C, in comparison with the corresponding native counterparts. In the presence of 10 mM H2O2, dRtDAO and dTvDAO exhibited half-lives of about 60 and 40 min, respectively, which were 2- and 1.5-fold, respectively, longer than their native DAOs. These yeast DAOs can therefore be thermally and oxidatively stabilized by linking their subunits together.
Relation:	Biotechnology Letters 30(8), pp.1415-1422
DOI:	10.1007/s10529-008-9694-5
Appears in Collections:	[Graduate Institue of Life Sciences] Journal Article

Files in This Item:

File	Size	Format
index.html	0Kb	HTML	52	View/Open

Loading...