Recovery of heavy metal ions from brine-damaged area with denaturation-resistant halophilic proteins and halophiles.

2015 Fiscal Year Final Research Report

• Project/Area Number: 15K14922
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Applied molecular and cellular biology
• Research Institution: Kagoshima University
• Principal Investigator: TOKUNAGA MASAO 鹿児島大学, 農学部, プロジェクト研究員 (20112782)
• Project Period (FY): 2015-04-01 – 2016-03-31
• Keywords: 応用微生物 / 好塩性タンパク質 / 極限環境微生物 / バイオテクノロジー / バイオロジクス

Outline of Final Research Achievements

Halophilic proteins are highly water soluble and resistant to aggregation under even strong salting-out conditions, resulting in exhibiting denaturation-resistant characteristics under harsh conditions. Halophilic histidine-rich metal binding protein (HP) has been found to have high binding capacity to several heavy metal ions and to be expressed in Escherichia coli cytoplasm as soluble form in large amount. We attempted to employ this HP protein and its High-His region to recover heavy metal ions from brine-damaged area. HP was found to bind high amount of Ni ion, and fixed Escherichia coli cells, expressing His-HP protein, from 1 liter culture was found to bind ~9.6 mg Ni ion.

Free Research Field

応用分子細胞生物学・応用微生物学