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| Content Provider | Springer Nature Link |
|---|---|
| Author | Kuroda, Kouichi Nishitani, Takashi Ueda, Mitsuyoshi |
| Copyright Year | 2012 |
| Abstract | By cell surface display of ModE protein that is a transcriptional regulator of operons involved in the molybdenum metabolism in Escherichia coli, we have constructed a molybdate-binding yeast (Nishitani et al., Appl Microbiol Biotechnol 86:641–648, 2010). In this study, the binding specificity of the molybdate-binding domain of the ModE protein displayed on yeast cell surface was improved by substituting the amino acids involved in oxyanion binding with other amino acids. Although the displayed S126T, R128E, and T163S mutant proteins adsorbed neither molybdate nor tungstate, the displayed ModE mutant protein (T163Y) abolished only molybdate adsorption, exhibiting the specific adsorption of tungstate. The specificity of the displayed ModE mutant protein (T163Y) for tungstate was increased by approximately 9.31-fold compared to the displayed wild-type ModE protein at pH 5.4. Therefore, the strategy of protein design and its cell surface display is effective for the molecular breeding of bioadsorbents with metal-specific adsorption ability based on a single species of microorganism without isolation from nature. |
| Starting Page | 153 |
| Ending Page | 159 |
| Page Count | 7 |
| File Format | |
| ISSN | 01757598 |
| Journal | Applied Microbiology and Biotechnology |
| Volume Number | 96 |
| Issue Number | 1 |
| e-ISSN | 14320614 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2012-05-01 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | Subscribed |
| Subject Keyword | Binding selectivity Molybdate Tungstate ModE Rare metals Yeast cell surface engineering Microbiology Biotechnology Microbial Genetics and Genomics |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Applied Microbiology and Biotechnology Biotechnology |
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