A Novel Thermostable Keratinase from Deinococcus geothermalis with Potential Application in Feather Degradation

文献类型： 外文期刊

第一作者： Tang, Yin

作者： Tang, Yin;Guo, Leizhou;Gui, Yuan;Dai, Qilin;Jiang, Shijie;Wang, Jin;Zhao, Mingming;Han, Jiahui;Lu, Wei;Lin, Min;Zhou, Zhengfu;Wang, Jin

作者机构：

关键词： Deinococcus geothermalis; keratinase; thermostability; feather degradation; C-terminal extension

期刊名称：APPLIED SCIENCES-BASEL （ 影响因子：2.474； 五年影响因子：2.458 ）

ISSN：

年卷期： 2021 年 11 卷 7 期

页码：

收录情况： SCI

摘要： Keratinase can specifically attack disulfide bridges in keratin to convert them from complex to simplified forms. Keratinase thermal stability has drawn attention to various biotechnological industries. In this study, a keratinase DgeKer was identified from a slightly thermophilic species, D. geothermalis. The in silico analysis showed that DgeKer is composed of signal peptide, N-terminal propeptide, mature domain, and C-terminal extension. DgeKer and its C-terminal extension-truncated enzyme (DgeKer-C) were cloned and expressed in E. coli. The purified DgeKer and DgeKer-C showed maximum activity at 70 degrees C and pH 9-The thermal stability assay (60 degrees C) showed that the half-life value of DgeKer and DgeKer-C were 103.45 min and 169.10 min, respectively. DgeKer and DgeKer-C were stable at the range of pH from 9 to 11 and showed good tolerance to some metal ions, surfactants and organic solvent. Furthermore, DgeKer could degrade feathers at 70 degrees C for 60 min. However, the medium became turbid with obvious softening of barbules after being treated with DgeKer-C, which might be due to C-terminal extension. In summary, a thermostable keratinase DgeKer with high efficiency degradation of feathers may have great potential in industry.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序