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No.30 (1983/11) >

 
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)
Title alternative :Purification and properties of α-L-arabinofuranosidase I from Bacillus sp. (Department of Agricultural Chemistry)
Authors :安田, 正昭
徳里, 政丈
瀬底, 正康
Authors alternative :Yasuda, Masaaki
Tokuzato, Masatake
Sesoko, Masayasu
Issue Date :19-Nov-1983
Abstract :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.
Type Local :紀要論文
ISSN :0370-4246
Publisher :琉球大学農学部
URI :http://hdl.handle.net/20.500.12000/3993
Citation :琉球大学農学部学術報告 = The Science Bulletin of the Faculty of Agriculture. University of the Ryukyus no.30 p.201 -209
Appears in Collections:No.30 (1983/11)

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