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- Mori Toshiaki
- Department of Biomolecular Engineering and Frontier Collaborative Research Center, Tokyo Institute of Technology
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- Okahata Yoshio
- Department of Biomolecular Engineering and Frontier Collaborative Research Center, Tokyo Institute of Technology
書誌事項
- タイトル別名
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- Gravimetric Analyses of Enzymatic Glucan Hydrolysis and Phosphorolysis on a 27MHz Quartz-Crystal Microbalance
- 27MHz スイショウ ハッシンシ マイクロバランス ジョウ デ ノ グルカン ノ カスイ ブンカイ カリンサン ブンカイ ハンノウ オ オモサ デ ハカル ガン エイブン
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説明
Catalytic cleavage reactions by glucoamylase or phosphorylase b were monitored directly on an amylopectin-immobilized 27MHz quartz-crystal microbalance (QCM). As a first example, we could follow kinetically the enzyme binding to the substrate binding (kon) and dissociation rate constants (koff) and intramolecular hydrolysis rate constant (kcat) of glucan hydrolysis by glucoamylase by detecting directly the formation and decomposition of the enzyme-substrate (ES) complex as mass changes. Secondly, glucan phosphorolysis by phosphorylase b was directly observed by two methods through reactions on a QCM. All kinetic parameters for the enzyme binding to the substrate kon and koff, and dissociation constant, Kd, the AMP binding to the enzyme as activator (KAMP), and the catalytic rate constant (kcat) were obtained from curve fittings of time-courses of frequency (mass) changes. The obtained kinetic parameters were compared with those from Michaelis-Menten kinetics in the bulk solution.
収録刊行物
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- Ｔｒｅｎｄｓ ｉｎ Ｇｌｙｃｏｓｃｉｅｎｃｅ ａｎｄ Ｇｌｙｃｏｔｅｃｈｎｏｌｏｇｙ
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Ｔｒｅｎｄｓ ｉｎ Ｇｌｙｃｏｓｃｉｅｎｃｅ ａｎｄ Ｇｌｙｃｏｔｅｃｈｎｏｌｏｇｙ 17 (94), 71-83, 2005
FCCA(Forum: Carbohydrates Coming of Age)
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詳細情報 詳細情報について
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- CRID
- 1390282679345146752
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- NII論文ID
- 10015466864
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- NII書誌ID
- AA10995236
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- ISSN
- 18832113
- 09157352
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- NDL書誌ID
- 7318354
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- 本文言語コード
- ja
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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
- NDLサーチ
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- 抄録ライセンスフラグ
- 使用不可
