ArticleWorld journal of microbiology & biotechnology2013
Expression of soluble recombinant transglutaminase from Zea mays in Pichia pastoris.
Article in World journal of microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 30 citations in OpenAlex.
- Microbial transglutaminase in food biotechnology: from biochemical mechanisms to industrial applications.Applied microbiology and biotechnology · 2026Review
- Microbiological transglutaminase: Biotechnological application in the food industry.Open life sciences · 2023Review
- Review
- 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
- Optimization of recombinantFood science and biotechnology · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transglutaminases (TGases) catalyze post-translational protein modifications by ε-(γ-glutamyl) links and covalent amide bonds. In plant, this enzyme is poorly studied and only the Zea mays TGase gene (tgz) has been cloned. The tgz had been expressed in Escherichia coli, but the recombinant protein was mainly present in inclusion bodies. Therefore, to obtain active, soluble protein, we optimized its coding sequence according to the codon bias of Pichia pastoris and synthesized the sequence with SOEing-PCR. The optimized fragment was successfully transformed into P. pastoris GS115 by electroporation. The optimal conditions for expression were under a final concentration of 0.5 % methanol and a time-course of 96 h. The synthesized recombinant Zea mays transglutaminase (TGZs) was purified by affinity method, its production was 4.4 mg/L, and the specific activity was 0.889 U/mg under optimal expression condition. Optimal activity for TGZs was observed at 37 °C and a pH of 8.0, respectively. The cross-linking reaction of TGZs to the casein was studied, and the result was same as the reaction of casein by microbial transglutaminase. These results indicated that an effective procedure for expressing and purifying TGZs in P. pastoris GS115 was established.
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