2014 Fiscal Year Final Research Report
Establishment of a guideline to improve the low-temperature activity of thermophilic enzymes
| Project/Area Number |
24560966
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biofunction/Bioprocess
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| Research Institution | Tokyo University of Pharmacy and Life Science |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Keywords | 酵素工学 / 好熱菌酵素 / 酵素利用 |
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| Outline of Final Research Achievements |
Thermophilic enzymes are generally stable and potentially useful for industrial processes. However, a crucial drawback for their use is that they are often nearly inactive at moderate and low temperatures. I previously reported that a small change in side-chain volume of a non-polar residue that interacts with the adenine moiety of the coenzyme NAD enhances the catalytic efficiency of the thermostable 3-isopropylmalate dehydrogenase and lactate dehydrogenase from the extreme thermophile Thermus thermophiles. In this study, I produced mutants of the glucose-1-dehydrogenase from the hyperthermophile Sulfolobus tokodaii in which one of the coenzyme-binding, non-polar residues was replaced by another non-polar residue. Because the mutant showed the improved low-temperature activity, I conclude that a small volume change of a non-polar residue’s side chain that interacts with the adenine of NAD(P) in a dehydrogenase will provide a general method to improve its low temperature activity.
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| Free Research Field |
生体触媒工学
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