| Budget Amount *help |
¥17,160,000 (Direct Cost: ¥13,200,000、Indirect Cost: ¥3,960,000)
Fiscal Year 2018: ¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2017: ¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2016: ¥9,620,000 (Direct Cost: ¥7,400,000、Indirect Cost: ¥2,220,000)
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| Outline of Final Research Achievements |
Proteins and enzymes can work through their conformational changes during interaction with substrate and ligands. These conformational changes can be detected by X-ray crystal analysis. But sometimes it is difficult to study about the conformational change owing to bad packing in the crystal lattice. It is also affected by “freezing of protein crystals” and cryo-protectants that usually interact with protein active site. We have to use non-freezing structure especially to observe the effect of pH. In the present work, I have studied about the function of food-related enzymes such as beta-amylase, pullulanase and protein glutaminase by X-ray crystal analysis with freezing and non-freezing (capillary) methods. I could get the fine structure changes in the active site of beta-amylase/substrate complexes caused by pH. The functions of pullulanase and protein glutaminase were also studied using mutant and complex crystals.
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