論文 - 詳細
| RRC ID | 50868 |
|---|---|
| 著者 | Zhang D, Tu T, Wang Y, Li Y, Luo X, Zheng F, Wang X, Bai Y, Huang H, Su X, Yao B, Zhang T, Luo H. |
| タイトル | Improving the Catalytic Performance of a Talaromyces leycettanus α-Amylase by Changing the Linker Length. |
| ジャーナル | J Agric Food Chem |
| Abstract |
A novel α-amylase, Amy13A, that consists of these domains was identified in Talaromyces leycettanus JCM12802: catalytic TIM-barrel fold, domain B, domain C, Thr/Ser-rich linker region, and C-terminal CBM20 domain. The wild type and three mutant enzymes were then expressed in Pichia pastoris GS115 to identify the roles of linker length (Amy13A21 and Amy13A33) and CBM20 (Amy13A-CBM) in catalysis. All enzymes had similar enzymatic properties, exhibiting optimal activities at pH 4.5-5.0 and 55-60 °C, but varied in catalytic performance. When using soluble starch as the substrate, Amy13A21 and Amy13A33 showed specific activities (926.3 and 537.8 units/mg, respectively, vs 252.1 units/mg) and catalytic efficiencies (kcat/Km, 25.7 and 22.0 mL s-1 mg-1, respectively, vs 15.4 mL s-1 mg-1) higher than those of the wild type, while Amy13A-CBM performed worse during catalysis. This study reveals the key roles of the CBM and linker length in the catalysis of GH13 α-amylase. |
| 巻・号 | 65(24) |
| ページ | 5041-5048 |
| 公開日 | 2017-6-21 |
| DOI | 10.1021/acs.jafc.7b00838 |
| PMID | 28573852 |
| MeSH | Amino Acid Sequence Catalysis Cloning, Molecular Enzyme Stability Fungal Proteins / chemistry* Fungal Proteins / genetics Fungal Proteins / metabolism Molecular Sequence Data Sequence Alignment Substrate Specificity Talaromyces / chemistry Talaromyces / enzymology* Talaromyces / genetics Temperature alpha-Amylases / chemistry* alpha-Amylases / genetics alpha-Amylases / metabolism |
| IF | 3.571 |
| 引用数 | 4 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | Patent(IFI CLAIMS) |
| 各媒体での言及数の合計 | 1 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 一般微生物 | JCM 12802 |