Construction of squalene producing cell factories and screening, cloning and expression of key genes.

Ning LI; Bo LIU; Mengxue DIAO; Jian LU; Weifeng LIU; Yong TONG

Return

Construction of squalene producing cell factories and screening, cloning and expression of key genes.

Author: Ning LI ¹ ; Bo LIU ² ; Mengxue DIAO ³ ; Jian LU ¹ ; Weifeng LIU ² ; Yong TONG ²
Author Information

1. College of Life Science and Technology, Guangxi University, Nanning 530004, Guangxi, China.
2. Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
3. National Engineering Research Center for Non-food Biorefinery, State Key Laboratory of Non-food Biomass Energy and Enzyme Technology, and Guangxi Key Laboratory of Biorefinery, Guangxi Academy of Sciences, Nanning 530007, Guangxi, China.
Publication Type:Journal Article
Keywords: Escherichia coli; biosynthesis; prokaryotic gene screening; squalene
MeSH: Cloning, Molecular; Escherichia coli/genetics*; Humans; Phylogeny; Squalene; Synechococcus
From: Chinese Journal of Biotechnology 2021;37(8):2813-2824
CountryChina
Language:Chinese
Abstract: Squalene is widely used in pharmaceutical, nutraceutical, cosmetics and other fields because of its strong antioxidative, antibacterial and anti-tumor activities. In order to produce squalene, a gene ispA encoding farnesyl pyrophosphate synthase was overexpressed in a previously engineered Escherichia coli strain capable of efficiently producing terpenoids, resulting in a chassis strain that efficiently synthesizes triterpenoids. Through phylogenetic analysis, screening, cloning and expression of squalene synthase derived from different prokaryotes, engineered E. coli strains capable of efficiently producing squalene were obtained. Among them, squalene produced by strains harboring squalene synthase derived from Thermosynechococcus elongatus and Synechococcus lividus reached (16.5±1.4) mg/g DCW ((167.1±14.3) mg/L broth) and (12.0±1.9) mg/g DCW ((121.8±19.5) mg/L broth), respectively. Compared with the first-generation strains harboring the human-derived squalene synthase, the squalene synthase derived from T. elongatus and S. lividus remarkably increased the squalene production by 3.3 times and 2.4 times, respectively, making progress toward the cost-effective heterologous production of squalene.