H
Hiroto Chaen
Researcher at Kyushu University
Publications - 150
Citations - 2430
Hiroto Chaen is an academic researcher from Kyushu University. The author has contributed to research in topics: Trehalose & Maltose. The author has an hindex of 25, co-authored 150 publications receiving 2318 citations.
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Journal ArticleDOI
Formation of trehalose from maltooligosaccharides by a novel enzymatic system.
Kazuhiko Maruta,Tetsuya Nakada,Michio Kubota,Hiroto Chaen,Toshiyuki Sugimoto,Masashi Kurimoto,Yoshio Tsujisaka +6 more
TL;DR: A trehalose-producing bacterium, Arthrobacter sp.
Journal ArticleDOI
Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius.
Kazuhiko Maruta,Hitoshi Mitsuzumi,Tetsuya Nakada,Michio Kubota,Hiroto Chaen,Shigeharu Fukuda,Toshiyuki Sugimoto,Masashi Kurimoto +7 more
TL;DR: It is proposed that the biosynthesis of trehalose in Sulfolobus occurs via the actions of the three enzymes encoded by treZXY, which are 33-40% homologous to the corresponding enzymes from Arthrobacter sp.
Journal ArticleDOI
Bioavailability of Glucosyl Hesperidin in Rats
Mika Yamada,Fujimi Tanabe,Norie Arai,Hitoshi Mitsuzumi,Yoshikatsu Miwa,Michio Kubota,Hiroto Chaen,Masayoshi Kibata +7 more
TL;DR: It was concluded that G-hesperidin is absorbed more rapidly and efficiently than hes peridin, because of its high water solubility.
Journal ArticleDOI
Purification and properties of a novel enzyme, trehalose synthase, from Pimelobacter sp. R48.
Tomoyuki Nishimoto,Masayuki Nakano,Tetsuya Nakada,Hiroto Chaen,Shigeharu Fukuda,Toshiyuki Sugimoto,Masashi Kurimoto,Yoshio Tsujisaka +7 more
TL;DR: A novel enzyme, trehalose synthase, was purified from a cell-free extract of Pimelobacter sp.
Journal ArticleDOI
Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36.
Tetsuya Nakada,Kazuhiko Maruta,Keiji Tsusaki,Michio Kubota,Hiroto Chaen,Toshiyuki Sugimoto,Masashi Kurimoto,Yoshio Tsujisaka +7 more
TL;DR: The enzyme showed the highest activity at pH 7.0 and 40 degrees C, and was stable from pH 6.0 to 9.5 and up to 40 degreesC, and the enzyme activity was inhibited by Hg2+ and Cu2+.