A novel thermostable keratinase from Deinococcus geothermalis with potential application in feather degradation
文献类型: 外文期刊
作者: Tang Yin;Guo Leizhou;Zhao Mingming;Gui Yuan;Han Jiahui;Lu Wei;Dai Qilin;Jiang Shijie;Lin Min;Zhou Zhengfu;Wang Jin
作者机构:
关键词: C-terminal extension; Deinococcus geothermalis; Feather degradation; Keratinase; Thermostability
期刊名称: Applied Sciences (Switzerland)
ISSN: 2076-3417
年卷期: 2021 年 11 卷 7 期
页码:
收录情况: JCR(2021版)
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 °C and pH 9-The thermal stability assay (60 °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 °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. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
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