Co-Expression of a Thermally Stable and Methanol-Resistant Lipase and Its Chaperone from Burkholderia cepacia G63 in Escherichia coli | |
Zhang, Jun2,3; Tian, Miao2,3; Chen, Xiaoyan2,3; Lv, Pengmei3; Luo, Wen3; Wang, Zhiyuan3; Xu, Jingliang1,3; Wang, Zhongming3 | |
刊名 | APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY |
2020-11-12 | |
页码 | 13 |
关键词 | Lipase Lipase chaperone Co-expression Escherichia coli Biodiesel |
ISSN号 | 0273-2289 |
DOI | 10.1007/s12010-020-03453-0 |
通讯作者 | Lv, Pengmei(lvpm@ms.giec.ac.cn) ; Xu, Jingliang(xujl@zzu.edu.cn) |
英文摘要 | Biodiesel biosynthesis with enzymatic transesterification is considered green, sustainable, and environmentally friendly method. Lipase from Burkholderia cepacia G63 has excellent catalytic properties in biodiesel production. Lipase chaperones promote secretion and folding of enzymes, thereby enhancing enzymatic activity. In the current study, heterologous co-expression of lipase (lipA) and chaperone (lipB) was achieved in Escherichia coli through codon optimization. The enzymatic activity of purified and renatured lipAB was 2080.23 +/- 19.18 U/g at 50 degrees C and pH 8.0. Moreover, lipAB showed increased resistance to pH and temperature changes, and lipAB retained stable catalytic properties after treatment with metal ions, organic solvents, and surfactants, namely Mg2+, methanol, and Triton-100X. Besides, using recombinant lipase lipAB as catalysts, biodiesel was synthesized using rapeseed oil under 50 degrees C for 72 h with a yield of 90.23%. Thus, the current study confirmed that co-expression of lipase and its chaperone is an effective strategy to enhance enzyme activity and improve the biochemical profile, meanwhile, showing that lipAB is a promising biocatalyst for biodiesel production. |
资助项目 | Guangdong Special Support Program[2017TX04Z109] ; National Natural Science Foundation of China[51606201] ; Science and Technology Planning Project of Guangdong Province[2016A010104008] ; Natural Science Foundation of Guangdong Province[2017A010104010] ; National Key Research and Development Program of China[2019YFB1504003] ; Projects of International Cooperation and Exchanges NSFC[51861145103] |
WOS关键词 | CODON OPTIMIZATION ; EXPRESSION ; CLONING ; GENES ; OIL |
WOS研究方向 | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
语种 | 英语 |
出版者 | SPRINGER |
WOS记录号 | WOS:000589037100001 |
资助机构 | Guangdong Special Support Program ; National Natural Science Foundation of China ; Science and Technology Planning Project of Guangdong Province ; Natural Science Foundation of Guangdong Province ; National Key Research and Development Program of China ; Projects of International Cooperation and Exchanges NSFC |
内容类型 | 期刊论文 |
源URL | [http://ir.giec.ac.cn/handle/344007/34871] |
专题 | 中国科学院广州能源研究所 |
通讯作者 | Lv, Pengmei; Xu, Jingliang |
作者单位 | 1.Zhengzhou Univ, Sch Chem Engn, Zhengzhou 450001, Peoples R China 2.Univ China Acad Sci, Beijing 100049, Peoples R China 3.Chinese Acad Sci, Guangzhou Inst Energy Convers, CAS Key Lab Renewable Energy, Guangdong Prov Key Lab New & Renewable Energy Res, Guangzhou 510640, Peoples R China |
推荐引用方式 GB/T 7714 | Zhang, Jun,Tian, Miao,Chen, Xiaoyan,et al. Co-Expression of a Thermally Stable and Methanol-Resistant Lipase and Its Chaperone from Burkholderia cepacia G63 in Escherichia coli[J]. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY,2020:13. |
APA | Zhang, Jun.,Tian, Miao.,Chen, Xiaoyan.,Lv, Pengmei.,Luo, Wen.,...&Wang, Zhongming.(2020).Co-Expression of a Thermally Stable and Methanol-Resistant Lipase and Its Chaperone from Burkholderia cepacia G63 in Escherichia coli.APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY,13. |
MLA | Zhang, Jun,et al."Co-Expression of a Thermally Stable and Methanol-Resistant Lipase and Its Chaperone from Burkholderia cepacia G63 in Escherichia coli".APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY (2020):13. |
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