糸状菌によるゲンチオビオースの分解(第1報)

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書誌事項

タイトル別名
  • Fungal Enzymes Active in Degrading Gentiobiose Part I
  • Aspergillus japonicus SAITO ベータ-グルコシダーゼ ノ セイセイ ト セイシツ
  • Purification and Some Properties of β-Glucosidase of <i>Aspergillus japonicus</i> SAITO
  • <i>Aspergillus japonicus</i> SAITO β-グルコシダーゼの精製と性質
公開日
1969
DOI
  • 10.1271/nogeikagaku1924.43.224
公開者
公益社団法人 日本農芸化学会

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説明

Enzymatic degradation of gentiobiose, a bitter component in the residual mother liquor in the production of D-glucose by acid hydrolysis of starch (hydrol), was studied.<br> Gentiobiase-producing mould, identified as Aspergillus japonicus SAITO, has been isolated from many wild moulds by using the synthetic medium containing gentiobiose as a sole carbon source. This mould has also been able to grow well in solid bran medium and induce strong gentiobiase activity. Enzyme was purified about 100-fold with a yield of 20% from the extract of bran culture by tannic acid precipitation, ammonium sulfate fractionation, DEAE-Sephadex chromatography, Sephadex G-75 gel filtration and starch block electrophoresis.<br> Analyses by free boundary electrophoresis and sedimentation showed the presence of almost single component with the mobility of -1.26×10-5cm2.V-1. sec-1 (pH 6.0, μ 0.1) and s20, w of 5.5 (pH 6.0, μ 0.1, _??_ 0.75).<br> Optimal pH and temperature of the enzyme reaction were 4.0 to 4.5 and 55 to 60°C, respectively. The enzyme was stable at pH 2 to 6 (40°C, 24 hr) and inactivated when heated for 15 min over 50 to 55°C at pH 4.5.<br> The enzyme was found to be able to hydrolyze gentiobiose, cellobiose, laminaribiose, salicin and p-nitrophenyl β-glucoside with Km, of 1.4, 1.5, 2.3, 5.4 and 1.35×10-3M, respectively.

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