@article{oai:u-ryukyu.repo.nii.ac.jp:02003162,
 author = {当山, 清善 and 与那覇, 和雄 and 石原, 昌信 and 儀間, 勝 and Toyama, Seizen and Yonaha, Kazuo and Ishihara, Masanobu and Gima, Masaru},
 issue = {26},
 journal = {琉球大学農学部学術報告, The Science Bulletin of the Faculty of Agriculture. University of the Ryukyus},
 month = {Dec},
 note = {酵母のL-ロイシン : α-ケトグルタル酸トランスアミナーゼ活性を調べた結果, 本酵素活性が各種の醸造用酵母に存在することがわかった。高い活性が泡盛醪から分離された泡盛酵母AY-634菌株で得られたので, 本菌株を用いて酵素の性質を調べた。本菌株をペプトンーグルコース培地で振とう培養してえた菌体の無細胞抽出液はL-ロイシンとα-ケトグルタル酸からL-グルタミン酸とα-ケトイソカプロン酸を生成するアミノ基転移反応を触媒した。培地にL-ロイシンを加えても活性の増加はみられなかったが, 本菌株を麹抽出液培地で培養すると高い活性が得られた。本酵素はL-イソロイシン, L-バリン, L-スレオニンおよびL-フェニールアラニンのアミノ基転移反応も触媒した。本酵素の反応至適pHは8.0で, 至適温度は40℃であった。本酵素はピリドキサールー5'-リン酸の存在下で熱に安定であった。, The activity of L-leucine : α-ketoglutarate transaminase was distributed in various strains of brewer's yeasts. A high activity of the enzyme was found in the strain AW-634 of awamori yeast isolated from awamori mash, and the strain was chosen for characterization of the enzyme. The cell-free extract of the strain grown on peptone-glucose medium with shaking catalyzed the transamination reaction between L-leucine and α-ketoglutarate to produce L-glutamate and α-ketoisocaproate. The enzyme activity was not enhanced by addition of L-leucine to the medium. When the strain was grown on koji-extract medium with stationary culture, the strong activity was obtained. The enzyme also catalyzed the transamination of L-isoleucine, L-valine, L-threonine and L-phenylalanine to α-ketoglutarate. The pH and temperature optima for the activity were 8.0 and 45℃, respectively. The enzyme was heat stable at pH 8.0 in the presence of pyridoxal 5'-phosphate., 紀要論文},
 pages = {125--133},
 title = {泡盛酵母の L-ロイシン : α-ケトグルタル酸トランスアミナーゼ(農芸化学科)},
 year = {1979}
}