@article{oai:u-ryukyu.repo.nii.ac.jp:02003022,
 author = {安田, 正昭 and 徳里, 政丈 and 瀬底, 正康 and Yasuda, Masaaki and Tokuzato, Masatake and Sesoko, Masayasu},
 issue = {30},
 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 = {Nov},
 note = {土壌から分離した細菌のアラビナン分解酵素の精製を行ない, その性質を検討した。酵素の精製は, Bacillus sp. No. 430の培養ろ液から硫酸アンモニウム分画, DEAE-セルロース, QAE-セファデックスA-50,DEAE-トーヨーパール650S, ヒドロキシアパタイト及びセファデックスG-75などのカラムクロマトグラフィーを組み合わせて行なった。精製酵素はディスク電気泳動的に高度に精製されていた。精製酵素の反応至適pHは6.5,反応至適温度は40℃であった。精製酵素はビートアラビナン, アラビノガラクタン, アラビノキシランやp-nitrophenyl α-L-arabinofuranosideに作用した。反応生成物はL-アラビノースのみが検出された。本精製標品はα-L-arabinofuranosidaseであると考えられた。, This study was carried out for a purpose of effective utilization of agricultural wastes by microbial enzymes. In order to liberate arabinose from arabinose-containing polysaccharides such as arabinan, arabinoxylan and arabinogalactan, an α-L-arabinofuranosidase was investigated. An α-L-arabinofuranosidase I was purified from the culture fluid of Bacillus sp. No. 430,which was isolated from the soil of sugar-cane fields. The process was as follows; salting out by ammonium sulfate, DEAE-cellulose, QAE-Sephadex A-50,DEAE-Toyopearl 650 S, hydroxyapatite and Sephadex G-75 column chromatography. The enzyme was highly purified by the method of discelectrophoresis. The purified enzyme had the maximum reactivity at pH 6.5 and 40℃. The highly purified enzyme was confirmed to be able to liberate L-arabinose from beet arabinan, arabinogalactan, arabinoxylan and p-nitrophenyl α-L-arabinofuranoside. The reaction product was paper chromatographically demonstrated to be only L-arabinose. The purified enzyme was inactive for p-nitrophenyl β-D-galctopyranoside., 紀要論文},
 pages = {201--209},
 title = {細菌のアラビナン分解酵素の精製とその性質(農芸化学科)},
 year = {1983}
}