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Insoluble expression of highly soluble halophilic metal binding protein for metal ion biosorption: Application of aggregation-prone peptide from hen egg white lysozyme.

Abstract：

: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.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Tokunaga M,Arakawa T,Tokunaga Y,Sugimoto Y,Ishibashi M

doi

10.1016/j.pep.2019.01.001

subject

Has Abstract

pub_date

2019-04-01 00:00:00

pages

50-57

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(18)30641-7

journal_volume

156

pub_type

杂志文章

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