通过与类弹性蛋白多肽融合提高D-氨基酸氧化酶的溶解度和稳定性。
Enhancement of the solubility and stability of D-amino acid oxidase by fusion to an elastin like polypeptide.
作者信息
Du Kun, Sun Jian, Song Xiaoqiang, Song Cuidan, Feng Wei
机构信息
Department of Biochemical Engineering, Beijing University of Chemical Technology, Beijing 100029, China.
Department of Biochemical Engineering, Beijing University of Chemical Technology, Beijing 100029, China.
出版信息
J Biotechnol. 2015 Oct 20;212:50-5. doi: 10.1016/j.jbiotec.2015.07.016. Epub 2015 Jul 26.
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.
一种类弹性蛋白多肽（ELP）与D-氨基酸氧化酶（DAAO）融合。ELP-DAAO在水溶液中的溶解度比DAAO更好，其酶活性约为DAAO的1.6倍。通过与不同浓度的尿素相互作用来研究蛋白质的稳定性。测量了圆二色光谱和荧光光谱。结果表明，ELP-DAAO的稳定性比DAAO好得多，即使在高尿素浓度下，ELP-DAAO仍保留了高比例的α-螺旋含量。这项工作的结果表明，ELP标签可用于纯化DAAO，同时提高了该酶的溶解度和稳定性。
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