Purification and some properties of Ichoimo .BETA.-amylase.

• ARAI Teiko

  Toyokogakuen Women's Junior College

• KAWABATA Akiko

  Tokyo University of Agriculture

• TANIGUCHI Hajime

  National Food Research Institute

抄録

An amylase was purified from tubers of ichoimo, a cultivar of yam (Dioscorea batatas), and its basic properties were investigated. The enzyme was purified by acid treatment of crude extracts at pH 4.5, DEAE-Toyopearl 650S ion-exchange chromatography, and hydrophobic chromatography using Butyl-Toyopearl 650S to a state showing a single band on SDS polyacrylamide gel electrophoresis (PAGE). The purified enzyme had a specific activity of 161 U/mg protein. It has a molecular mass of 60, 000 Da on SDS-PAGE, optimum pH of 6.0, optimum temperature of 55°C, and a stable pH range of 4.3 to 8.5. On isoelectric focusing PAGE it gave two protein bands with pi's of 5.0 and 5.2. It produced maltose as a sole low molecular weight product from soluble starch and did not act on cyclodextrins. The anomeric form of the maltose was identified as the β-form. These results confirmed that the purified enzyme is a β-amylase.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 55 (2), 399-405, 1991

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390001206463014016
• NII論文ID: 110006325369
• NII書誌ID: AA00515312
• DOI: 10.1271/bbb1961.55.399
• COI: 1:CAS:528:DyaK3MXhtlyls78%3D
• ISSN: 18811280
• ISSN: 00021369
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可