| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6490916 | Journal of Biotechnology | 2015 | 53 Pages |
Abstract
An elastin-like polypeptide (ELP) was fused to d-amino acid oxidases (DAAO). ELP-DAAO exhibited a better solubility in aqueous solutions than DAAO, and its enzymatic activity is about 1.6 times that of DAAO. The stability of the proteins was investigated by interacting with urea at various concentrations. The circular dichroism and fluorescence spectra were measured. The results demonstrated that that ELP-DAAO exhibited a much better stability than DAAO, and ELP-DAAO has retained the α-helix content with a high percentage even at a high urea concentration. The results of this work have demonstrated that the ELP tag can be utilized to purify DAAO, in the meantime the solubility and stability of the enzyme are improved.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Kun Du, Jian Sun, Xiaoqiang Song, Cuidan Song, Wei Feng,