期刊
PROTEIN EXPRESSION AND PURIFICATION
卷 156, 期 -, 页码 50-57出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2019.01.001
关键词
Inclusion bodies; Active aggregation; Insoluble expression; Halophilic; Metal binding protein; Biosorption
类别
资金
- Sankei Science Foundation
Insoluble expression of intrinsically soluble proteins with native activity is potentially a promising alternative to soluble expression of folded protein or insoluble expression of unfolded protein requiring refolding. Here, we attempted to express highly soluble halophilic His-rich metal binding protein (HP) as insoluble inclusion bodies with native metal-binding activity using insolubilizing nona-peptide (Ins), GILQINSRW, derived from hen egg white lysozyme (His-InsHP). About 80% of expressed His-InsHP was localized in inclusion bodies in Na-phosphate/NaCl buffer, pH 7.4, while His-HP without Ins peptide was exclusively expressed in soluble supernatant. We report expression, purification and characterization of this insoluble His-InsHP, and its possible application for efficient biosorption and recovery of environmental metal ions, for example, by using whole bacterial cells expressing insoluble His-insHP as a new cost-effective metal ion-adsorbent.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据