Insoluble expression of highly soluble halophilic metal binding protein for metal ion biosorption: Application of aggregation-prone peptide from hen egg white lysozyme
| Autor: | Matsujiro Ishibashi, Yasushi Sugimoto, Masao Tokunaga, Tsutomu Arakawa, Yuhei Tokunaga |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0106 biological sciences
Metal ions in aqueous solution Peptide 01 natural sciences Inclusion bodies Metal 03 medical and health sciences chemistry.chemical_compound Egg White 010608 biotechnology Escherichia coli Histidine 030304 developmental biology chemistry.chemical_classification 0303 health sciences Biosorption Phosphate Halophile Recombinant Proteins chemistry Biochemistry Metals visual_art visual_art.visual_art_medium Muramidase Lysozyme Biotechnology Protein Binding |
| Zdroj: | Protein expression and purification. 156 |
| ISSN: | 1096-0279 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect