Purification and Characterization of Extracellular Alginate Lyase from<i>Enterobacter cloacae</i>M-1
書誌事項
- タイトル別名
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- Purification and Characterization of Extracellular Alginate Lyase from Enterobacter cloacae M-1.
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説明
An alginate lyase from the culture supernatant of Enterobacter cloacae M-1 was purified by ammonium sulfate precipitation, cation-exchange chromatography (SP-Toyopearl), and gel filtration (Ultrogel AcA44). The final preparation thus obtained showed a single band on SDS-PAGE. The purified enzyme had the molecular weight of 38, 000 and 32, 000 by SDS-PAGE and gel filtration, respectively. The pI of the enzyme was 8. 9. The optimum pH and temperature for the enzyme reaction were around 7. 8 and 30°C, respectively. The enzyme was unstable on heating. EDTA completely inhibited the enzyme activity, but the activity was completely restored by the treatment with CaCl2. The enzyme was specific for poly-guluronate and produced several kinds of unsaturated oligomers from the gluluronate. This suggested that the enzyme could be classified as an endo poly-guluronate lyase.
収録刊行物
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- Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ
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Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ 59 (4), 632-637, 1995
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206474662016
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- NII論文ID
- 110002677516
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- NII書誌ID
- AA10824164
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- COI
- 1:CAS:528:DyaK2MXlsVSmtL0%3D
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- ISSN
- 13476947
- 09168451
- http://id.crossref.org/issn/09168451
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- PubMed
- 7772828
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- JaLC
- Crossref
- PubMed
- CiNii Articles
- OpenAIRE
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- 抄録ライセンスフラグ
- 使用不可
