Knowledge Management System Of Guangzhou Institute of Energy Conversion, CAS
| Enhanced activity of Rhizomucor miehei lipase by directed saturation mutation of the propeptide | |
Tian, Miao1,2; Huang, Shaowei3; Wang, Zhiyuan1; Fu, Junying1; Lv, Pengmei1 ; Miao, Changlin1; Liu, Tao4; Yang, Lingmei1; Luo, Wen1
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| 2021-10-01 | |
| Source Publication | ENZYME AND MICROBIAL TECHNOLOGY
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| ISSN | 0141-0229 |
| Volume | 150Pages:8 |
| Corresponding Author | Lv, Pengmei(lvpm@ms.giec.ac.cn) ; Luo, Wen(luowen@ms.giec.ac.cn) |
| Abstract | 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. |
| Keyword | Propeptide RML Enzyme activity Directed saturation mutation |
| DOI | 10.1016/j.enzmictec.2021.109870 |
| WOS Keyword | INDUSTRIAL-PRODUCTION ; BIODIESEL PRODUCTION ; PICHIA-PASTORIS ; EXPRESSION ; EVOLUTION ; OPTIMIZATION ; MUTAGENESIS ; SUBTILISIN |
| Indexed By | SCI |
| Language | 英语 |
| Funding Project | 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 Research Area | Biotechnology & Applied Microbiology |
| Funding Organization | National Natural Science Foundation of China ; National Key Research and Development Projects |
| WOS Subject | Biotechnology & Applied Microbiology |
| WOS ID | WOS:000703947600007 |
| Publisher | ELSEVIER SCIENCE INC |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.giec.ac.cn/handle/344007/34823 |
| Collection | 中国科学院广州能源研究所 |
| Corresponding Author | Lv, Pengmei; Luo, Wen |
| Affiliation | 1.Chinese Acad Sci, Guangzhou Inst Energy Convers, Key Lab Renewable Energy, Guangzhou 510640, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.South China Agr Univ, Guangzhou 510642, Peoples R China 4.Guangdong Pharmaceut Univ, Guangdong Prov Key Lab Pharmaceut Bioact Subst, Guangzhou 510006, Peoples R China |
| First Author Affilication | GuangZhou Institute of Energy Conversion,Chinese Academy of Sciences |
| Recommended Citation 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. |
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