論文 - 詳細
| RRC ID | 71286 |
|---|---|
| 著者 | Wang S, Meng K, Su X, Hakulinen N, Wang Y, Zhang J, Luo H, Yao B, Huang H, Tu T. |
| タイトル | Cysteine Engineering of an Endo-polygalacturonase from Talaromyces leycettanus JCM 12802 to Improve Its Thermostability. |
| ジャーナル | J Agric Food Chem |
| Abstract |
Thermostable enzymes have many advantages for industrial applications. Therefore, in this study, computer-aided design technology was used to improve the thermostability of a highly active endo-polygalacturonase from Talaromyces leycettanus JCM12802 at an optimal temperature of 70 °C. The melting temperature and specific activity of the obtained mutant T316C/G344C were increased by 10 °C and 36.5%, respectively, compared with the wild-type enzyme. The crystal structure of the T316C/G344C mutant showed no formation of a disulfide bond between the introduced cysteines, indicating a different mechanism than the conventional mechanism underlying improved enzyme thermostability. The cysteine substitutions directly formed a new alkyl hydrophobic interaction and caused conformational changes in the side chains of the adjacent residues Asn315 and Thr343, which in turn caused a local reconstruction of hydrogen bonds. This method greatly improved the thermostability of the enzyme without affecting its activity; thus, our findings are of great significance for both theoretical research and practical applications. |
| 巻・号 | 69(22) |
| ページ | 6351-6359 |
| 公開日 | 2021-6-9 |
| DOI | 10.1021/acs.jafc.1c01618 |
| PMID | 34043362 |
| MeSH | Cysteine Enzyme Stability Polygalacturonase* / genetics Polygalacturonase* / metabolism Talaromyces* / genetics Talaromyces* / metabolism Temperature |
| 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 | X(Twitter) |
| 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 | JCM12802 |