Enhancement of the solubility and stability of ID-amino acid oxidase by fusion to an elastin like polypeptide
Enhancement of the solubility and stability of ID-amino acid oxidase by fusion to an elastin like polypeptide
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通过与弹性蛋白样多肽融合增强 ID-氨基酸氧化酶的溶解度和稳定性
DOI：
10.1016/j.jbiotec.2015.07.016
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发表时间：
2015
影响因子：
4.1
通讯作者：
Feng Wei
中科院分区：
文献类型：
--
作者：
Du Kun;Sun Jian;Song Xiaoqiang;Song Cuidan;Feng Wei
将弹性蛋白样多肽(ELP)融合为氨基酸氧化酶(DAAO)。ELP-DAAO在水溶液中的溶解度比DAAO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，考察了蛋白质的稳定性。测量了它们的圆二色谱和荧光光谱。结果表明，ELP-DAAO的稳定性明显好于DAAO，即使在较高的尿素浓度下，ELP-DAAO仍能保持较高比例的α-螺旋含量。研究结果表明，ELP标签可用于DAAO的纯化，同时提高了酶的溶解度和稳定性。
An elastin-like polypeptide (ELP) was fused tod-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.