| Literature DB >> 19894045 |
Takashi Nishitani1, Mariko Shimada, Kouichi Kuroda, Mitsuyoshi Ueda.
Abstract
In modern industrial society, molybdenum is one of the important metals for development of the industry of rare metals. It is important to recycle the rare metals from wastes because they are technically and economically difficult to be dug and be purified, and they exist in only a few regions in the world. In this study, ModE protein derived from Escherichia coli, which is a molybdate-dependent transcriptional regulator with the ability to bind molybdate as a form of soluble molybdenum, was displayed on the yeast cell surface by alpha-agglutinin-based cell surface display system for the adsorption and recovery of molybdate. Displayed ModE, confirmed by immunofluorescence labeling, caught molybdate more preferably at pH 3.0 than at basic pH. Yeast cells displaying C-terminal domain of ModE, which lacks N-terminal DNA binding domain, more effectively adsorbed molybdate than those displaying full-length ModE, suggesting that the deletion of the domain unrelated to metal binding enhanced the binding ability. Our results indicated that the adsorption system on cell surface of yeast cells displaying ModE is effective not only for adsorption of molybdate as a rare metal bioadsorbent but also for the easy recovery of molybdate located on the cell surface.Entities:
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Year: 2009 PMID: 19894045 DOI: 10.1007/s00253-009-2304-1
Source DB: PubMed Journal: Appl Microbiol Biotechnol ISSN: 0175-7598 Impact factor: 4.813