High-efficiency expression of the thermophilic lipase from Geobacillus thermocatenulatus in Escherichia coli and its application in the enzymatic hydrolysis of rapeseed oil
文献类型:期刊论文
作者 | Zhang, Jun1,3; Tian, Miao1,3; Lv, Pengmei3![]() ![]() ![]() ![]() |
刊名 | 3 BIOTECH
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出版日期 | 2020-11-10 |
卷号 | 10期号:12页码:9 |
关键词 | Thermophilic lipase Escherichia coli Enzymatic hydrolysis Rapeseed oil |
ISSN号 | 2190-572X |
DOI | 10.1007/s13205-020-02517-6 |
通讯作者 | Lv, Pengmei(lvpm@ms.giec.ac.cn) ; Xu, Jingliang(xujl@zzu.edu.cn) |
英文摘要 | Long-chain fatty acids are widely used in food and chemical industries, and the enzymatic preparation of fatty acids is considered an environmentally friendly process. In the present study, long-chain fatty acids were prepared by the enzymatic hydrolysis of rapeseed oil with a genetically engineered lipase. Because thermophilic lipase has strong stability at higher temperatures, it was more suitable for the industrial production of long-chain fatty acids. Therefore, the thermophilic lipase BTL2 from Geobacillus thermocatenulatus was efficiently expressed in E. coli BL21(DE3) cells with an enzyme activity of 39.50 U/mg followed by gene codon optimisation. Experimental results showed that the recombinant lipase BTL2 exhibited excellent resistance to certain organic solvents (n-hexane, benzene, ethanol, and butanol). The metal cation Ca2+ and the non-ionic surfactant Triton-100X enhanced enzyme activity by 7.36% and 56.21% respectively. Moreover, the acid value of the liberated long-chain fatty acids by hydrolysing rapeseed oil was approximately 161.64 mg KOH/g at 50 degrees C in 24 h, the hydrolytic conversion rate was 91.45%, and the productivity was approximately 6.735 mg KOH/g h. These results suggested that the recombinant lipase BTL2 has excellent hydrolytic performance for rapeseed oil and showed great potential for the enzymatic preparation of long-chain fatty acids. |
WOS关键词 | METAL-ORGANIC FRAMEWORKS ; BACILLUS ; IMMOBILIZATION ; PURIFICATION ; AMYLASE ; PROTEIN ; BTL2 |
资助项目 | Guangdong Special Support Program[2017TX04Z109] ; National Natural Science Foundation of China[51606201] ; National Natural Science Foundation of China[51903236] ; 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研究方向 | Biotechnology & Applied Microbiology |
语种 | 英语 |
WOS记录号 | WOS:000593779200005 |
出版者 | SPRINGER HEIDELBERG |
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 |
源URL | [http://ir.giec.ac.cn/handle/344007/34828] ![]() |
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.Univ China Acad Sci, Beijing 100049, Peoples R China 2.Zhengzhou Univ, Sch Chem Engn, Zhengzhou 450001, Peoples R China 3.Chinese Acad Sci, CAS Key Lab Renewable Energy, Guangdong Prov Key Lab New & Renewable Energy Res, Guangzhou Inst Energy Convers, Guangzhou 510640, Peoples R China |
推荐引用方式 GB/T 7714 | Zhang, Jun,Tian, Miao,Lv, Pengmei,et al. High-efficiency expression of the thermophilic lipase from Geobacillus thermocatenulatus in Escherichia coli and its application in the enzymatic hydrolysis of rapeseed oil[J]. 3 BIOTECH,2020,10(12):9. |
APA | Zhang, Jun.,Tian, Miao.,Lv, Pengmei.,Luo, Wen.,Wang, Zhiyuan.,...&Wang, Zhongming.(2020).High-efficiency expression of the thermophilic lipase from Geobacillus thermocatenulatus in Escherichia coli and its application in the enzymatic hydrolysis of rapeseed oil.3 BIOTECH,10(12),9. |
MLA | Zhang, Jun,et al."High-efficiency expression of the thermophilic lipase from Geobacillus thermocatenulatus in Escherichia coli and its application in the enzymatic hydrolysis of rapeseed oil".3 BIOTECH 10.12(2020):9. |
入库方式: OAI收割
来源:广州能源研究所
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