Self Introduction
I’m Masato Kakuma. Family name is Kakuma. Currently, I’m attending university and studying enzymes. My hobby is scuba diving and I got a license two years ago. I did scuba diving in Bali this March. I do scuba diving once a year, but I can’t do many times because it costs money. When I will become a working member of society and earn money, I will do scuba diving many times a year. Scuba diving is a hobby that started since I became a university student, but I also experienced various good things while I attended university. I went abroad for the first time when I was a university student. Iwent with my friends in Taiwa and Bali. Also, I went to study abroad in Malaysia. I touched a different culture from Japan, and I was surprised many times, but it was a good learning experience. Also, because international students come to our laboratory every year, I discuss with foreign people every year. This experience was a good English study for me. Besides, I experienced various things such as paragliding and mountain climbing. Because I’m a university student, I was able to experience these things and I think that these experiences have made me a lot of growth
My Experiment Theme
Thermophile is a microorganism that lives in the hot springs and volcano of undersea. Thermophile can grow even under high temperature environment. Most of thermophile belong to archaea neither eukaryote nor bacteria. From here onwards, it is expected that special properties of only thermophilic archaea. It is said that there is a high possibility of having the property closest to the origine of life, Because thermophile are located near the origine of life in evolutionary tree. Therefore, it is expected that studying of thermophile can elucidate the mystery of life creation.
It is reported that enzymes derived from thermophile have higher thermal stability than enzymes derived from normal bacteria. In addition, enzymes derived from thermophile are stable for a long time even at room temperature. Furthermore, enzymes derived from thermophile have resistance in a wide range of pH and resistance against organic solvents, denaturing agents. Therefore, enzymes derived from thermophile are also expected to be applied to industrial aspects.
Currently, enzymes derived from thermophile are produced by bacteria such as Escherichia coli. However the archaeal expression system is more like the expression system of eukaryote rather than bacteria. Therefore, it is reported that many enzymes are produced without function as enzymes, if an enzyme derived from thermophilic archaea is expressed in Escherichia coli. Therefore, expression of enzymes derived from thermophilic archaea was performed in the thermophilic archaeal sulfolobus acidocaldarius by gene recombination opreration.
I am studying D-lactate dehydrogenase derived from thermophilic archaeal sulfolobus tokodaii. Two D-lactate dehydrogenase are found in sulfolobus tokodai, and it is interesting whether there is a difference in the physiological role of these two enzymes. Therefore, I am studying two D-lactate dehydrogenase derived from sulfolobus tokodaii.
Many D-lactate is contained in the blood of diabetic patients. Also, D-lactate is contained in wine and beer. From here onwards, D-lactate dehydrogenase is expected to be applied as a device for diagnosis of diabetes and quality control of alcoholic drinks.
By 2016, I succeeded in expressing the D-lactate dehydrogenase and purifying the enzyme single. Also, a wide pH range and thermal stability of the enzyme could be confirmed. Currently, I am analyzing the D-lactate dehydrogenase in more detail.
It is reported that enzymes derived from thermophile have higher thermal stability than enzymes derived from normal bacteria. In addition, enzymes derived from thermophile are stable for a long time even at room temperature. Furthermore, enzymes derived from thermophile have resistance in a wide range of pH and resistance against organic solvents, denaturing agents. Therefore, enzymes derived from thermophile are also expected to be applied to industrial aspects.
Currently, enzymes derived from thermophile are produced by bacteria such as Escherichia coli. However the archaeal expression system is more like the expression system of eukaryote rather than bacteria. Therefore, it is reported that many enzymes are produced without function as enzymes, if an enzyme derived from thermophilic archaea is expressed in Escherichia coli. Therefore, expression of enzymes derived from thermophilic archaea was performed in the thermophilic archaeal sulfolobus acidocaldarius by gene recombination opreration.
I am studying D-lactate dehydrogenase derived from thermophilic archaeal sulfolobus tokodaii. Two D-lactate dehydrogenase are found in sulfolobus tokodai, and it is interesting whether there is a difference in the physiological role of these two enzymes. Therefore, I am studying two D-lactate dehydrogenase derived from sulfolobus tokodaii.
Many D-lactate is contained in the blood of diabetic patients. Also, D-lactate is contained in wine and beer. From here onwards, D-lactate dehydrogenase is expected to be applied as a device for diagnosis of diabetes and quality control of alcoholic drinks.
By 2016, I succeeded in expressing the D-lactate dehydrogenase and purifying the enzyme single. Also, a wide pH range and thermal stability of the enzyme could be confirmed. Currently, I am analyzing the D-lactate dehydrogenase in more detail.