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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Su, Erzheng Xu, Jingjing Wu, Xiangping |
| Description | Author Affiliation: Su E ( Enzyme and Fermentation Technology Laboratory, College of Light Industry Science and Engineering, Nanjing Forestry University, Nanjing, People's Republic of China.) |
| Abstract | Serratia marcescens lipase (SmL) is an important biocatalyst used to enantioselectively hydrolyze (±)-trans-3-(4-methoxyphynyl) glycidic acid methyl ester. However, the economically justified level recombinant soluble expression of SmL in Escherichia coli has not been established. Thus, fusion genes of lipase from S. marcescens H30 with different fusion tags were constructed and expressed in E. coli. The effects of fusion tags were revealed. A significant increase in recombinant lipase solubility showed that E. coli BL21 (DE3)/pET32a-SmL was a suitable choice for SmL production. To optimize the performance of recombinant SmL production, changes in culture medium compositions and induction conditions were systematically tested. Finally, the recombinant SmL activity and productivity reached approximately 23,000 U/L and 1,278 U/L/H in shake flasks, respectively. This value is the highest SmL activity attained by heterogeneous recombinant expression in E. coli. Lipase activity and productivity reached 19,650 U/L and 1,228 U/L/H, respectively, by scaling up SmL production in a 7.0 L fermenter. The existence of the Trx tag did not influence the chiral selectivity of recombinant SmL. These findings indicate a possibility for soluble and economical SmL expression in E. coli to meet industrial needs. |
| File Format | HTM / HTML |
| ISSN | 08854513 |
| Issue Number | 1 |
| Volume Number | 62 |
| e-ISSN | 14708744 |
| Journal | Biotechnology and Applied Biochemistry |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 2015-01-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Discipline Biotechnology Biotechnology Methods Escherichia Coli Genetics Lipase Chemistry Serratia Marcescens Enzymology Bioreactors Microbiology Carbon Pharmacology Cloning, Molecular Culture Media Culture Techniques Drug Effects Growth & Development Feasibility Studies Gene Expression Lactose Biosynthesis Metabolism Nitrogen Phosphates Recombinant Proteins Solubility Stereoisomerism Substrate Specificity Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Drug Discovery Molecular Medicine Bioengineering Biomedical Engineering Applied Microbiology and Biotechnology Biotechnology Process Chemistry and Technology |
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