My name is Satsuki Miyawaki.
My hobby is climbing mountains. The mountain where I climb is mostly mountains not so high. However, I have climbed Miyanoura dake (1,936 m) in Yakushima, the highest peak in Kyushu. The reason why I wanted to go to Miyanoura dake is because I wanted to see the stage of Princess Mononoke of the Ghibli movie on the way to the summit. The name of the stage is Shiratani Unsuikyo. I was impressed because Shiratani Unsuikyo was very similar to the scenery that appears in the movie Princess Mononoke. Actually, I started climbing because I thought that I would like to see the scenery like the stage of the ghibli movie. When I climbed Miyanoura dake, I was very happy that it came true. (However, its climbing was very painful physically.) There are places other than Yakushima where there was a stage for Princess Mononoke. I would like to go to the Shirakami mountain next time. Also, I currently conduct research using enzymes derived from hyperthermophilic bacteria. Hyperthermophile is a fungus that lives in a high temperature area like the source of a hot spring. I can not get a hot spring without climbing a mountain, but I am looking forward to climbing a mountain for taking samples. If you have any recommended mountain, please tell me. MY RESEARCH THEME Chiral amino acid metabolomics is to separate the optical isomers of amino acid by various methods. It has attracted attention in recent years by many chemists. Amino acids have optical isomers of L- and D-forms. Most amino acids in vivo are L-form. Therefore, it has long been considered that there is no D-Amino acid in vivo. However, recent developments in analytical methods have revealed that D-Serine (D-Ser) and D-Aspartic acid (D-Asp) are present in vivo. It was also revealed that the content of D-Amino acid is related to disease. For example, it was found that the deficiency of D-Ser leads to autonomic imbalance and a part of L-Amino acid in protein is isomerized to D-forms with aging in mammalian skin. Despite being aware of such things, quantification of D-Amino acids has not been carried out so far. This is because the content of L-Amino acid in vivo is too large (the content of D-Amino acid is too small) and interfered with the measurement of D-Amino acid. At present, there is a need for a method of higher optical isomer separation. In fact, it is possible to optically resolve the 20 kinds of amino acids that make up proteins, by the analytical method called two-dimensional HPLC analysis system. However, to do that method requires a lot of time and money. So, I thought about building an inexpensive and simple D-Amino acid detection system by combining D-Amino acid dehydrogenase derived from a thermophile capable of stable and mass culture with a cation column. To realize this, I am now purifying and identifying D-Amino acid dehydrogenase derived from thermophilic bacteria. In addition, I am also studying the conditions of buffer solution and pH to separate amino acids by cation column. (The column must be separate the enzyme at a pH at which the enzyme is not inactivated.) After enzyme purification, I will study conditions for immobilization of enzyme on glassy carbon electrode. After the immobilization of the enzyme is successful, I will examine the mediator used to support the transfer of the electrons between the enzyme and the electrode, consider the immobilization of the mediator, and finally combine the column and its electrode. I am praying for this research to be successful. Chiral amino acid metabolomics is to separate the optical isomers of amino acid by various methods. It has attracted attention in recent years by many chemists. Amino acids have optical isomers of L- and D-forms. Most amino acids in vivo are L-form. Therefore, it has long been considered that there is no D-Amino acid in vivo. However, recent developments in analytical methods have revealed that D-Serine (D-Ser) and D-Aspartic acid (D-Asp) are present in vivo. It was also revealed that the content of D-Amino acid is related to disease. For example, it was found that the deficiency of D-Ser leads to autonomic imbalance and a part of L-Amino acid in protein is isomerized to D-forms with aging in mammalian skin. Despite being aware of such things, quantification of D-Amino acids has not been carried out so far. This is because the content of L-Amino acid in vivo is too large (the content of D-Amino acid is too small) and interfered with the measurement of D-Amino acid. At present, there is a need for a method of higher optical isomer separation. In fact, it is possible to optically resolve the 20 kinds of amino acids that make up proteins, by the analytical method called two-dimensional HPLC analysis system. However, to do that method requires a lot of time and money. So, I thought about building an inexpensive and simple D-Amino acid detection system by combining D-Amino acid dehydrogenase derived from a thermophile capable of stable and mass culture with a cation column. To realize this, I am now purifying and identifying D-Amino acid dehydrogenase derived from thermophilic bacteria. In addition, I am also studying the conditions of buffer solution and pH to separate amino acids by cation column. (The column must be separate the enzyme at a pH at which the enzyme is not inactivated.) After enzyme purification, I will study conditions for immobilization of enzyme on glassy carbon electrode. After the immobilization of the enzyme is successful, I will examine the mediator used to support the transfer of the electrons between the enzyme and the electrode, consider the immobilization of the mediator, and finally combine the column and its electrode. I am praying for this research to be successful. |