Simple Amino Acid Tags Improve Both Expression and Secretion of Candida antarctica Lipase B in Recombinant Escherichia coli
- Authors
- Kim, Sun-Ki; Park, Yong-Cheol; Lee, Hyung Ho; Jeon, Seung Taeg; Min, Won-Ki; Seo, Jin-Ho
- Issue Date
- Feb-2015
- Publisher
- WILEY
- Keywords
- Candida antarctica lipase B; Escherichia coli; extracellular secretion; polyanionic amino acid tag; quaternary structure change
- Citation
- BIOTECHNOLOGY AND BIOENGINEERING, v.112, no.2, pp 346 - 355
- Pages
- 10
- Journal Title
- BIOTECHNOLOGY AND BIOENGINEERING
- Volume
- 112
- Number
- 2
- Start Page
- 346
- End Page
- 355
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/68507
- DOI
- 10.1002/bit.25361
- ISSN
- 0006-3592
1097-0290
- Abstract
- Escherichia coli is the best-established microbial host strain for production of proteins and chemicals, but has a weakness for not secreting high amounts of active heterologous proteins to the extracellular culture medium, of which origins belong to whether prokaryotes or eukaryotes. In this study, Candida antarctica lipase B (CalB), a popular eukaryotic enzyme which catalyzes a number of biochemical reactions and barely secreted extracellularly, was expressed functionally at a gram scale in culture medium by using a simple amino acid-tag system of E. coli. New fusion tag systems consisting of a pelB signal sequence and various anion amino acid tags facilitated both intracellular expression and extracellular secretion of CalB. Among them, the Nterminal five aspartate tag changed the quaternary structure of the dimeric CalB and allowed production of 1.9 g/L active CalB with 65 U/mL activity in culture medium, which exhibited the same enzymatic properties as the commercial CalB. This PelB-anion amino acid tag-based expression system for CalB can be extended to production of other industrial proteins hardly expressed and exported from E. coli, thereby increasing target protein concentrations and minimizing purification steps. (C) 2014 Wiley Periodicals, Inc.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - ETC > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/68507)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.