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The Relationship Between The Affinity and The Kinetics of Cellulase for Its Substrate
http://hdl.handle.net/10076/11641
http://hdl.handle.net/10076/1164165104bba-78b8-49b4-a693-66f25bfb0501
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
60C15222.pdf (587.5 kB)
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| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||||||
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| 公開日 | 2011-11-04 | |||||||||
| タイトル | ||||||||||
| タイトル | The Relationship Between The Affinity and The Kinetics of Cellulase for Its Substrate | |||||||||
| 言語 | en | |||||||||
| 言語 | ||||||||||
| 言語 | eng | |||||||||
| キーワード | ||||||||||
| 主題Scheme | Other | |||||||||
| 主題 | cellulase / ITC | |||||||||
| 資源タイプ | ||||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||||
| 資源タイプ | departmental bulletin paper | |||||||||
| 著者 |
Kanie, M.
× Kanie, M.
× Karita, S.
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| 抄録 | ||||||||||
| 内容記述タイプ | Abstract | |||||||||
| 内容記述 | The recombinant endoglucanase of family 44 (Cel44A) isolated from Clostridium thermocellum F1 has activities for cellulase, xylanase, and xyloglucanase. Previous studies using mutant Cel44A (E186Q) had suggested that Trp64 play a crucial role in binding to cellooligosaccharides. This study confirmed previous findings, and provided further studies understanding the role of each subsite in the cleft of the catalytic domain. Isothermal titration calorimetry (ITC) provided a direct measure of binding enthalpy (ΔH) and allowed the determination of the association constants (Ka) of the mutated Cel44As with various degrees of cellooligosaccharides. Experimental binding studies with the mutants lacking aromatic binding residues (W64A/E186Q and W64A/Y71A/E186Q) suggest that the each amino acid residues didn’t dominate whole enzymatic affinity. However, W64A/E186Q and W64A/Y71A/E186Q showed a higher affinity for cellohexaose and cellopentaose than did E186Q. These high affinities are probably seemed to be related to the rates of hydrolysis and product pattern as demonstrated by enzyme assay and thin layer chromatography of hydrolytic products. Our result suggests that the high affinity of catalytic domain causes its products to remain in the cleft and delay the proceeding of hydrolysis. |
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| 書誌情報 |
Proceedings of the Second International Workshop on Regional Innovation Studies : (IWRIS2010) 号 2, p. 1-4, 発行日 2010-10-01 |
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| フォーマット | ||||||||||
| 内容記述タイプ | Other | |||||||||
| 内容記述 | application/pdf | |||||||||
| 著者版フラグ | ||||||||||
| 出版タイプ | VoR | |||||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||||
| 出版者 | ||||||||||
| 出版者 | Graduate School of Regional Innovation Studies, Mie University | |||||||||
| 資源タイプ（三重大） | ||||||||||
| 値 | Departmental Bulletin Paper / 紀要論文 | |||||||||
