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Cited 6 time in webofscience Cited 7 time in scopus
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Enhanced Production of a Thermostable Carbonic Anhydrase in Escherichia coli by Using a Modified NEXT Tagopen access

Authors
Hwang, In SeongKim, Joo HyeonJo, Byung Hoon
Issue Date
Oct-2021
Publisher
MDPI
Keywords
recombinant protein; solubility enhancer; NEXT tag; carbonic anhydrase; Thermovibrio ammonificans; CO2 capture
Citation
MOLECULES, v.26, no.19
Indexed
SCIE
SCOPUS
Journal Title
MOLECULES
Volume
26
Number
19
URI
https://scholarworks.gnu.ac.kr/handle/sw.gnu/3203
DOI
10.3390/molecules26195830
ISSN
1420-3049
1420-3049
Abstract
Carbonic anhydrase (CA) is an ultrafast enzyme that catalyzes the reversible conversion of carbon dioxide (CO2) to bicarbonate. CA is considered to be a green catalyst for enzyme-based CO2 capture and utilization. In particular, the CA of Thermovibrio ammonificans (taCA) has attracted increasing attention as a highly stable enzyme. However, the poor solubility and the low expression level in Escherichia coli have hampered further utilization of taCA. In a recent study, these limitations were partly resolved by using a small solubility-enhancing fusion tag named NEXT, which originates from the N-terminal extension of Hydrogenovibrio marinus CA. In this study, the NEXT tag was engineered by adding small peptides to the N terminus to further increase the production yield of NEXT-tagged taCA. The addition of ng3 peptide (His-Gly-Asn) originating from the N-terminal sequence of Neisseria gonorrhoeae CA improved the expression of NEXT-taCA, while the previously developed translation-enhancing element (TEE) and Ser-Lys-Ile-Lys (SKIK) tag were not effective. The expression test with all 16 codon combinations for the ng3 sequence revealed that the change in translation initiation rate brought about by the change in nucleotide sequence was not the primary determinant for the change in expression level. The modified ng3-NEXT tag may be applied to increase the production yields of various recombinant proteins.</p>
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