Aspergillus aculeatus由来β-キシロシダーゼの精製と諸性質 Purification and Some Properties of Aspergillus aculeatus β-Xylosidase

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Author(s)

    • 大井 俊彦 [他] OOI Toshihiko
    • 大阪府立大学農学部応用生物化学科 Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
    • 藤本 啓明 FUJIMOTO Hiroaki
    • 大阪府立大学農学部応用生物化学科 Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
    • 王 三郎 WANG Sang-lang
    • 大阪府立大学農学部応用生物化学科 Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
    • 小倉 セイ OGURA Sei
    • 大阪府立大学農学部応用生物化学科 Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
    • 村尾 澤夫 MURAO Sawao
    • 大阪府立大学農学部応用生物化学科 Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
    • 荒井 基夫 ARAI Motoo
    • 大阪府立大学農学部応用生物化学科 Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture

Abstract

A.aculeatusの生産するβ-キシロシダーゼをフスマを炭素源とした培養i上清より硫安沈澱DEAE-Sephadex A-50,Sephacryl S-200,DEAF-Toyopearl650Mおよび等電点電気泳動の各カラムクロマトにより精製を行った結果,電気泳動的に単一な精製酵素を27%の回収率で得た.本酵素の分子量はSDS-PAGEで105,000と算出され,等電点はpH 4.3であった.酵素はpH 3~7の範囲で安定であり,50℃ 以下で安定であった.また至適pHおよび至適温度はpH 2および70℃ であった.本酵素の活性はCu<SUP>2+</SUP>, Mn<SUP>2+</SUP>,Hg<SUP>2+</SUP>の存在によって阻害された.一方,本酵素はキシロオリゴ糖およびLarchwoodキシランからキシロースのみを生成し,他のオリゴ糖はまったく検出されなかった.

Extracellular β-xylosidase ([EC 3.2.1.37]: xylan 1, 4-β-xylosidase) was purified from a culture filtrate of Aspergillus aculeatus No. F-50 by column chromatography using DEAE-Sephadex A-50, Sephacry 5-200, and DEAE-Toyopearl 650M columns, and preparative isoelectric focusing. The purified enzyme was homogeneous on SDS-polyacrylamide gel electrophoresis . The molecular weight was about 105, 000 by SDS-PAGE and its p1 value was 4.3. The optimum pH and temperature for the /3 -xylosidase activities were 2.0 and 70°C, respectively. The β-xylosidase was stable for 30 min at 50°C and stable between pH 3 and 7. The enzyme activity was strongly inhibited by Cu<SUP>2+</SUP>, Mn<SUP>2+</SUP>, and Hg<SUP>2+</SUP>. The enzyme hydrolyzed xylooligosaccharides, xylobiose through xylopentaose, to form xylose. The β-xylosidase showed potent activity towards larchwood xylan .

Journal

  • Journal of Applied Glycoscience

    Journal of Applied Glycoscience 42(1), 45-48, 1995-03-31

    The Japanese Society of Applied Glycoscience

References:  16

Cited by:  1

Codes

  • NII Article ID (NAID)
    10008253971
  • NII NACSIS-CAT ID (NCID)
    AN10453916
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    13403494
  • NDL Article ID
    3616893
  • NDL Source Classification
    RA14(生理・生化学・生物物理--核酸・蛋白質・酵素)
  • NDL Source Classification
    ZP24(科学技術--化学・化学工業--糖・澱粉)
  • NDL Call No.
    Z17-15
  • Data Source
    CJP  CJPref  NDL  J-STAGE 
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