Enhanced activity of Rhizomucor miehei lipase by directed saturation mutation of the propeptide
文献类型：期刊论文
| 作者 | Tian, Miao3,4; Huang, Shaowei2; Wang, Zhiyuan4; Fu, Junying4; Lv, Pengmei4 ; Miao, Changlin4; Liu, Tao1; Yang, Lingmei4; Luo, Wen4
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| 刊名 | ENZYME AND MICROBIAL TECHNOLOGY
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| 出版日期 | 2021-10-01 |
| 卷号 | 150页码:8 |
| 关键词 | Propeptide RML Enzyme activity Directed saturation mutation |
| ISSN号 | 0141-0229 |
| DOI | 10.1016/j.enzmictec.2021.109870 |
| 通讯作者 | Lv, Pengmei(lvpm@ms.giec.ac.cn) ; Luo, Wen(luowen@ms.giec.ac.cn) |
| 英文摘要 | The propeptide is a short sequence that facilitates protein folding. In this study, four highly active Rhizomucor miehei lipase (RML) mutants were obtained through saturation mutagenesis at three propeptide positions: Ser8, Pro35, and Pro47. The enzyme activities of mutants P35 N, P47 G, P47 N, and S8E/P35S/P47A observed at 40 degrees C, and pH 8.0 were 10.19, 7.53, 6.15, and 8.24 times of that wild-type RML, respectively. The S8E/P35S/ P47A mutant showed good thermostability. After incubation at 40 degrees C for 1 h, 98.98 % of its initial activity remained, whereas wild-type RML retained only 78.76 %. This result indicated that the enhancement of hydrophilicity of 35- and 47- amino-acid residues could promote the interaction between the propeptide and the mature peptide and the enzyme activity and expression level. Highly conserved sites had a more significant impact on enzyme performance than did other sites, similar to the Pro35 and Pro47 mutants showed in this study. This study provides a new idea for protein modification: enzyme performance can be improved through propeptide regulation. |
| WOS关键词 | INDUSTRIAL-PRODUCTION ; BIODIESEL PRODUCTION ; PICHIA-PASTORIS ; EXPRESSION ; EVOLUTION ; OPTIMIZATION ; MUTAGENESIS ; SUBTILISIN |
| 资助项目 | National Natural Science Foundation of China[51903236] ; National Natural Science Foundation of China[51806225] ; National Natural Science Foundation of China[51861145103] ; National Key Research and Development Projects[2019YFB1504003] |
| WOS研究方向 | Biotechnology & Applied Microbiology |
| 语种 | 英语 |
| WOS记录号 | WOS:000703947600007 |
| 出版者 | ELSEVIER SCIENCE INC |
| 资助机构 | National Natural Science Foundation of China ; National Key Research and Development Projects |
| 源URL | [http://ir.giec.ac.cn/handle/344007/34822]  |
| 专题 | 中国科学院广州能源研究所 |
| 通讯作者 | Lv, Pengmei; Luo, Wen |
| 作者单位 | 1.Guangdong Pharmaceut Univ, Guangdong Prov Key Lab Pharmaceut Bioact Subst, Guangzhou 510006, Peoples R China 2.South China Agr Univ, Guangzhou 510642, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 4.Chinese Acad Sci, Guangzhou Inst Energy Convers, Key Lab Renewable Energy, Guangzhou 510640, Peoples R China |
| 推荐引用方式 GB/T 7714 | Tian, Miao,Huang, Shaowei,Wang, Zhiyuan,et al. Enhanced activity of Rhizomucor miehei lipase by directed saturation mutation of the propeptide[J]. ENZYME AND MICROBIAL TECHNOLOGY,2021,150:8. |
| APA | Tian, Miao.,Huang, Shaowei.,Wang, Zhiyuan.,Fu, Junying.,Lv, Pengmei.,...&Luo, Wen.(2021).Enhanced activity of Rhizomucor miehei lipase by directed saturation mutation of the propeptide.ENZYME AND MICROBIAL TECHNOLOGY,150,8. |
| MLA | Tian, Miao,et al."Enhanced activity of Rhizomucor miehei lipase by directed saturation mutation of the propeptide".ENZYME AND MICROBIAL TECHNOLOGY 150(2021):8. |
入库方式： OAI收割
来源：广州能源研究所
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