キシロース残基を含む合成オリゴ糖(三糖,四糖)に対するα-およびβ-アミラーゼの作用

• NITTA Yasunori

  Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University

• SUZUKI Akihiro

  Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University

• TAKEO Kenichi

  Department of Agricultural Chemistry, Kyoto Prefectural University

書誌事項

タイトル別名

• Actions of α- and β-Amylases to Tri-and Tetra-Saccharides Containing Xylose
• Actions of アルファ and ベータ Amylases to Tri

抄録

The actions of a-amylases (Taka-amylase A and porcine pancreatic α-amylase) and soybean β-amylase for four synthetic oligosaccharides, which are contained one or two D-xylose residues linked via α-1, 4 glycosidic bond, were investigated. A synthetic analogue of maltotetraose, Ο-α-Dglucopyranosyl-(14) -Ο-α-D-xylopyranosyl- (1→4) -Ο-α-D-xylopyranosyl- (1→4) -D-glucopyranose (GXXG) was not hydrolyzed by a- and β-amylases and was a competitive inhibitor only for both aamylases. GXXG had almost the same binding affinities as maltotetraose. An analogue of maltotriose, Ο-α-D-glucopyranosyl- (1→4) -Ο-α-D-glucopyranosyl- (1→4) -D-xylopyranose (GGX) was αcompetitive inhibitor (K, = 7.8 mM) only for soybean β-amylase. From the result, it was found that the CHZOH group at C-5 of the glucose residue of substrate plays a very important role in the catalytic action or in the productive binding of substrate for α-and β-amylases, and that GXXG and GGX arevery useful for the X-ray crystallographic study on the productive binding mode of substrate for α-and fl-amylases, respectively.

収録刊行物

• 応用糖質科学

  応用糖質科学 43 (2), 167-172, 1996

  日本応用糖質科学会

詳細情報

• CRID: 1390282680148514432
• NII論文ID: 10008255325
• NII書誌ID: AN10453916
• DOI: 10.11541/jag1994.43.167
• COI: 1:CAS:528:DyaK28XkvVGnu7g%3D
• ISSN: 18844898
• ISSN: 13403494
• NDL書誌ID: 3995011
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I3995011
• データソース種別:
  • JaLC
  • NDL
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可