P-53 セルラーゼのプロセッシビティを中心とした機能解析
書誌事項
- タイトル別名
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- P-53 Processive movement observation of GH6 cellulases
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説明
<p>Recently, our research group visualized the linear movement of Glycosyl Hydrolase family 7 (GH7) cellulase TrCel7A on crystalline cellulose to use High-Speed Atomic Force Microscopy (HS-AFM). In this study, we observed the processive movement of four GH6 cellulases (CfCel6A, CfCel6B, SaCel6B and TrCel6A). HS-AFM observation analysis revealed that CfCel6B and SaCel6B molecules sliding on crystalline cellulose. These two cellulases showed opposite direction movement with TrCel7A. Prediction 3D structure of CfCel6B and SaCel6B showed more loop regions covering the subsite cleft than CfCel6A and TrCel6A, which may imply higher binding affinity with cellulose chain. Protein 3D structure could be affected for strength of processivity. In biochemical analysis, we studied for synergistic degradation activity for crystalline cellulose by TrCel7A and GH6 exo-cellulase or combination of two GH6 exo-cellulases. Exo-exo synergy was clearly seen between TrCel7A and GH6 exo-cellulases. However, there was no synergism between two GH6 exo-cellulases combination, the activities were lower than sum of individual activities. These differences could be caused by the direction of processivity of cellulases. Two GH6 exo-cellulases show same direction movements on the crystalline cellulose, it could be cause traffic jams then degradation activity is lower.</p>
収録刊行物
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- バイオマス科学会議発表論文集
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バイオマス科学会議発表論文集 12 (0), 155-156, 2017
一般社団法人 日本エネルギー学会
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詳細情報 詳細情報について
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- CRID
- 1390282680763723008
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- NII論文ID
- 130005296163
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- ISSN
- 24238341
- 24238333
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可