ArticleScientific reports2018
Tailoring recombinant lipases: keeping the His-tag favors esterification reactions, removing it favors hydrolysis reactions.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- EngineeredSynthetic and systems biotechnology · 2026Article
- Gene Cloning, Expression, and Purification of Kunitz Trypsin Inhibitor from Glycine max Using Halo Tag.Molecular biotechnology · 2026Article
- Terminator: A Software Package for Fast and Local Optimization of His-Tag Placement for Protein Affinity Purification.ACS bio & med chem Au · 2025Article
- Increasing thermostability of the key photorespiratory enzyme glycerate 3-kinase by structure-based recombination.Plant biotechnology journal · 2025Article
- Location Is Everything: Influence of His-Tag Fusion Site on Properties of Adenylosuccinate Synthetase fromInternational journal of molecular sciences · 2024Article
- Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.International journal of molecular sciences · 2022Review
- Development of alkaline phosphatase-scFv and its use for one-step enzyme-linked immunosorbent assay for His-tagged protein detection.Open life sciences · 2022Article
- Identification and Heterologous Production of a Lipase from Geobacillus kaustophilus DSM 7263The protein journal · 2021Article
- Low-resolution molecular shape, biochemical characterization and emulsification properties of a halotolerant esterase from Bacillus licheniformis.European biophysics journal : EBJ · 2020Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We determined the effect of the His-tag on the structure, activity, stability and immobilization of LipC12, a highly active lipase from a metagenomic library. We purified LipC12 with a N-terminal His-tag and then removed the tag using tobacco etch virus (TEV) protease. Circular dichroism analysis showed that the overall structure of LipC12 was largely unaffected by His-tag removal. The specific hydrolytic activities against natural and artificial substrates were significantly increased by the removal of the His-tag. On the other hand, His-tagged LipC12 was significantly more active and stable in the presence of polar organic solvents than untagged LipC12. The immobilization efficiency on Immobead 150 was 100% for both forms of LipC12 and protein desorption studies confirmed that the His-tag does not participate in the covalent binding of the enzyme. In the case of immobilized LipC12, the His-tag negatively influenced the hydrolytic activity, as it had for the free lipase, however, it positively influenced the esterification activity. These results raise the possibility of tailoring recombinant lipases for different applications, where the His-tag may be retained or removed, as appropriate for the desired activity.
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