Fusion tags to enhance heterologous protein expression
- Authors
- Ki, Mi-Ran; Pack, Seung Pil
- Issue Date
- 3월-2020
- Publisher
- SPRINGER
- Keywords
- Escherichia coli; Heterologous protein expression; Expression-enhancing tag; Fusion tag; Protein tag; Peptide tag; Solubility tag; Aggregation-prone tag; Inclusion body
- Citation
- APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, v.104, no.6, pp.2411 - 2425
- Indexed
- SCIE
SCOPUS
- Journal Title
- APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 104
- Number
- 6
- Start Page
- 2411
- End Page
- 2425
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/57430
- DOI
- 10.1007/s00253-020-10402-8
- ISSN
- 0175-7598
- Abstract
- Escherichia coli is the most widely used heterologous protein expression system. However, this system remains a challenge due to the low solubility of proteins, insufficient yield, and inclusion body formation. Numerous approaches have sought to address these issues. The use of a fusion tag is one of the most powerful strategies for obtaining large amounts of heterologous protein in E. coli expression system. Here, recent advances in fusion tags that increase the expression of proteins are reviewed. In addition, proposed concepts for designing peptide tags to increase protein expression are discussed.
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Collections - Graduate School > Department of Biotechnology and Bioinformatics > 1. Journal Articles
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