ArticleBMC biotechnology2017
Constitutive expression of active microbial transglutaminase in Escherichia coli and comparative characterization to a known variant.
Article in BMC biotechnology, 2017. 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, 30 citations in OpenAlex.
- Microbial transglutaminase in food biotechnology: from biochemical mechanisms to industrial applications.Applied microbiology and biotechnology · 2026Review
- LexA, an SOS response repressor, activates TGase synthesis inFrontiers in microbiology · 2024Article
- Identification of multiple regulatory genes involved in TGase production inEngineering microbiology · 2023Article
- Screening of Yeast Display Libraries of Enzymatically Treated Peptides to Discover Macrocyclic Peptide Ligands.International journal of molecular sciences · 2021Article
- An effective combination of codon optimization, gene dosage, and process optimization for high-level production of fibrinolytic enzyme in Komagataella phaffii (Pichia pastoris).BMC biotechnology · 2020Article
- A recent update on the use of microbial transglutaminase for the generation of biotherapeutics.World journal of microbiology & biotechnology · 2020Review
- Transglutaminases: part I-origins, sources, and biotechnological characteristics.World journal of microbiology & biotechnology · 2020Review
- Improved the expression level of active transglutaminase by directional increasing copy of mtg gene in Pichia pastoris.BMC biotechnology · 2019Article
- Design of a glutamine substrate tag enabling protein labelling mediated by Bacillus subtilis transglutaminase.PloS one · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMicrobial transglutaminase (mTG) is a robust enzyme catalyzing the formation of an isopeptide bond between glutamine and lysine residues. It has found use in food applications, pharmaceuticals, textiles, and biomedicine. Overexpression of soluble and active mTG in E. coli has been limited due to improper protein folding and requirement for proteolytic cleavage of the pro-domain. Furthermore, to integrate mTG more fully industrially and academically, thermostable and solvent-stable variants may be imperative.
resultsA novel expression system constitutively producing active mTG was designed. Wild-type (WT) mTG and a S2P variant had similar expression levels, comparable to previous studies. Kinetic constants were determined by a glutamate dehydrogenase-coupled assay, and the S2P variant showed an increased affinity and a doubled enzyme efficiency towards Z-Gln-Gly. The melting temperature (T
conclusionsA constitutive expression system of active mTG in E. coli without downstream proteolytic cleavage processing was used for overexpression and characterization. High throughput techniques for testing thermostability and kinetics were useful in streamlining analysis and could be used in the future for quickly identifying beneficial mutants. Hitherto untested thermostability and stability of mTG in organic solvents was evaluated, which can pave the way for use of the enzyme in novel applications and processes.
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