Purification and some properties of amylomaltase from Escherichia coli IFO 3806.

• KITAHATA Sumio

  Osaka Municipal Technical Research Institute

• MURAKAMI Hiromi

  Osaka Municipal Technical Research Institute

• OKADA Shigetaka

  Osaka Municipal Technical Research Institute

抄録

The amylomaltase from Escherichia coli IFO 3806 was purified to homogeneity seen by SDSpolyacrylamide gel electrophoresis after DEAE-Sephadex, Ultrogel AcA 44, hydroxylapatite, and 1, 6-hexane-diamine-Sepharose 4B column chromatographies. The molecular weight of the purified enzyme was 93, 000 by SDS-polyacrylamide gel electrophoresis. The enzyme was most active at pH 6.5 and at 35°C, and stable up to 45°C at pH 7.0 and from pH 6.0-7.3 at 40°C on 30min incubation. The enzyme acted on maltotetraitol, maltopentaitol, and maltosylsucrose besides maltooligosaccharides, but did not act on maltitol, maltotriitol, glucosylsucrose, isomaltose, panose, isopanose, or isomaltosylmaltose. This enzyme did not catalyze hydrolytic action on maltotetraitol, maltopentaitol, or maltosylsucrose.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 53 (10), 2653-2659, 1989

  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: 1390282681444940544
• NII論文ID: 110006324038
• NII書誌ID: AA00515312
• DOI: 10.1271/bbb1961.53.2653
• 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