2003年5月
An exotype alginate lyase in Sphingomonas sp Al: overexpression in Escherichia coli, purification, and characterization of alginate lyase IV (A1-IV)
PROTEIN EXPRESSION AND PURIFICATION
- ,
- ,
- 巻
- 29
- 号
- 1
- 開始ページ
- 33
- 終了ページ
- 41
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/S1046-5928(03)00018-4
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
Sphingomonas sp. Al (strain Al) cells contain three kinds of endotype alginate lyases [Al-I, Al-II, and Al-III], all of which are formed from a common precursor through posttranslational processing. In addition to these lyases, another type of lyase (Al-IV) that acts on oligoalginates exists in the bacterium. Al-IV was overexpressed in Escherichia coli cells through control of its gene under the T7 promoter. The expression level of the enzyme in E coli cells was 8.6 U/L-culture, which was about 270-fold higher than that in strain A I cells. The enzyme was purified to homogeneity through three steps with an activity yield of 10.9%. The optimal pH and temperature, thermal stability, and mode of action of the purified enzyme were similar to those of the native enzyme from strain Al cells. Al-IV exolytically degraded oligoalginates, which were produced from alginate through the reaction of Al-I, Al-II, or Al-III, into monosaccharides, indicating that the cooperative actions of these four enzymes cause the complete depolymerization of alginate in strain Al cells. (C) 2003 Elsevier Science (USA). All rights reserved.
- リンク情報
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- DOI
- https://doi.org/10.1016/S1046-5928(03)00018-4
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902248266747911
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/12729723
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000182863800005&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1016/S1046-5928(03)00018-4
- ISSN : 1046-5928
- J-Global ID : 200902248266747911
- PubMed ID : 12729723
- Web of Science ID : WOS:000182863800005