論文 - 詳細
| RRC ID | 55116 |
|---|---|
| 著者 | Li X, Xia W, Bai Y, Ma R, Yang H, Luo H, Shi P. |
| タイトル | A Novel Thermostable GH3 β-Glucosidase from Talaromyce leycettanus with Broad Substrate Specificity and Significant Soybean Isoflavone Glycosides-Hydrolyzing Capability. |
| ジャーナル | Biomed Res Int |
| Abstract |
A novel β-glucosidase gene (Bgl3B) of glycoside hydrolase (GH) family 3 was cloned from the thermophilic fungus Talaromyce leycettanus JM12802 and successfully expressed in Pichia pastoris. The deduced Bgl3B contains 860 amino acid residues with a calculated molecular mass of 91.2 kDa. The purified recombinant Bgl3B exhibited maximum activities at pH 4.5 and 65°C and remained stable at temperatures up to 60°C and pH 3.0-9.0, respectively. The enzyme exhibited broad substrate specificities, showing β-glucosidase, glucanase, cellobiase, xylanase, and isoflavone glycoside hydrolase activities, and its activities were stimulated by short-chain alcohols. The catalytic efficiencies of Bgl3B were 693 and 104/mM/s towards pNPG and cellobiose, respectively. Moreover, Bgl3B was highly effective in converting isoflavone glycosides to aglycones at 37°C within 10 min, with the hydrolysis rates of 95.1%, 76.0%, and 75.3% for daidzin, genistin, and glycitin, respectively. These superior properties make Bgl3B potential for applications in the food, animal feed, and biofuel industries. |
| 巻・号 | 2018 |
| ページ | 4794690 |
| 公開日 | 2018-10-23 |
| DOI | 10.1155/2018/4794690 |
| PMID | 30426008 |
| PMC | PMC6218797 |
| MeSH | Amino Acids / chemistry Cellobiose / chemistry Enzyme Stability Glycine max / chemistry* Glycosides / chemistry* Hydrolysis Isoflavones / chemical synthesis Isoflavones / chemistry* Pichia / chemistry Substrate Specificity Talaromyces / chemistry* beta-Glucosidase / chemistry* |
| IF | 2.197 |
| 引用数 | 2 |
| 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 | 2 |
| 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 |