Preparation and some properties of active monomer of sweet potato β-amylase

• ANN Yong-Geun

  Faculty of Science, Osaka City University

• IIZUKA Masaru

  Faculty of Science, Osaka City University

• YAMAMOTO Takehiko

  Faculty of Engineering, Fukuyama University

• MINAMIURA Noshi

  Faculty of Science, Osaka City University

書誌事項

タイトル別名

• Preparation and some properties of active monomer of sweet potato .BETA.-amylase.

抄録

Sweet potato β-amylase was divided into two active fractions (named F-A and F-B) by modification with periodate-oxidized maltohexaose at pH 9.7. F-A and F-B isolated by exclusion chromatography using Sephadex G-200 corresponded to a pentamer of the enzyme with molecular weight of 31.5 × 10⁴ and a monomer with molecular weight of 6.4 × 10⁴, respectively. The contents of carbohydrate of the modified enzymes were 9.7% for F-A and 9.3% for F-B. The specific activities of F-A and F-B were 2, 059 and 1, 129 units/mg of protein and were reduced to 82% and 45% of that of the original enzyme, respectively. The modification of the enzyme with the oxidized maltohexaose was due to formation of a Schiff base between ε-NH2 groups of lysines of the enzyme protein and CHO groups of the oxidized maltohexaose.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 54 (3), 769-774, 1990

  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: 1390282681441507200
• NII論文ID: 110006324838
• NII書誌ID: AA00515312
• DOI: 10.1271/bbb1961.54.769
• COI: 1:CAS:528:DyaK3cXitFaru7c%3D
• ISSN: 18811280
• ISSN: 00021369
• 本文言語コード: en
• データソース種別:
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  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可