Purification and Characterization of New Trehalose-producing Enzymes Isolated from the Hyperthermophilic Archae,<i>Sulfolobus solfataricus</i>KM1

• KATO Masaru

• MIURA Yutaka

• KETTOKU Masako

• SHINDO Kazutoshi

• IWAMATSU Akihiro

• KOBAYASHI Kazuo

書誌事項

タイトル別名

• Purification and Characterization of New Trehalose-producing Enzymes Isolated from the Hyperthermophilic Archae, Sulfolobus solfataricus KM1.

抄録

Amylolytic activity that converts soluble starch to α, α-trehalose (trehalose), was found in the cell homogenate of the hyperthermophilic acidophilic archae, Sulfolobus solfataricus KM1. DEAE chromatography of the homogenate as well as other new reliable assay methods showed two enzymes to be essential for this activity. These enzymes, a glycosyltransferase and an amylase, were purified to homogeneity and characterized. Their molecular masses were 76 kDa and 61 kDa and activities were maximal at 70-80°C and 70-85°C, respectively. High thermostability was noted for each. The reaction products by the two enzymes on maltooligosaccharides were identified by ¹H- and ¹³C-NMR spectra and HPLC analysis. The cooperative mechanism of the two enzymes was used in a new enzymatic pathway for trehalose synthesis from starch.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 60 (3), 546-550, 1996

  公益社団法人 日本農芸化学会

キーワード

• trehalose
• Sulfolobus solfataricus
• glycosyltrehalose

詳細情報

• CRID: 1390001206475814784
• NII論文ID: 110002678064
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.60.546
• COI: 1:CAS:528:DyaK28XhvFygur4%3D
• ISSN: 13476947
• ISSN: 09168451
• PubMed: 8901122
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.60.546
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可