Expression of Bacillus amyloliquefaciens transglutaminase in recombinant E. coli under the control of a bicistronic plasmid system in DO-stat fed-batch bioreactor cultivations

Duarte, Lovaine Silva; Matte, Carla Roberta; Cortivo, Paulo Roberto Dall; Nunes, J.; Barsé, Laísa Quadros; Bizarro, Cristiano Valim; Ayub, Marco Antônio Záchia

doi:10.1007/s42770-021-00521-3

Cited by 5 publications

(2 citation statements)

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“…During a batch bioreactor culture, the concentration of Cas9 protein that heterologously was expressed in E. coli was approximately 420.1 mg/L, obtained 6 h after the induction time (Carmignotto and Azzoni 2019 ). In another study, the produced recombinant TGase enzyme in bioreactor cultivation was 17.5 g/L (Duarte et al 2021 ). One of the problems in the high-volume production of recombinant proteins is the risk of bioreactor contamination.…”

Section: Essential Components Of E Coli -Based Exp...mentioning

confidence: 99%

Factors involved in heterologous expression of proteins in E. coli host

Pouresmaeil

Azizi-Dargahlou

2023

Arch Microbiol

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The production of recombinant proteins is one of the most significant achievements of biotechnology in the last century. These proteins are produced in the eukaryotic or prokaryotic heterologous hosts. By increasing the omics data especially related to different heterologous hosts as well as the presence of new amenable genetic engineering tools, we can artificially engineer heterologous hosts to produce recombinant proteins in sufficient quantities. Numerous recombinant proteins have been produced and applied in various industries, and the global recombinant proteins market size is expected to be cast to reach USD 2.4 billion by 2027. Therefore, identifying the weakness and strengths of heterologous hosts is critical to optimize the large-scale biosynthesis of recombinant proteins. E. coli is one of the popular hosts to produce recombinant proteins. Scientists reported some bottlenecks in this host, and due to the increasing demand for the production of recombinant proteins, there is an urgent need to improve this host. In this review, we first provide general information about the E. coli host and compare it with other hosts. In the next step, we describe the factors involved in the expression of the recombinant proteins in E. coli . Successful expression of recombinant proteins in E. coli requires a complete elucidation of these factors. Here, the characteristics of each factor will be fully described, and this information can help to improve the heterologous expression of recombinant proteins in E. coli .

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Section: Essential Components Of E Coli -Based Exp...mentioning

confidence: 99%

Factors involved in heterologous expression of proteins in E. coli host

Pouresmaeil

Azizi-Dargahlou

2023

Arch Microbiol

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“…Gene transfer technology provided many possible TGM productions, where the expression of genes in E. coli has increased the production of TGMs and their efficiency immensely. Such enzymes are consumer-friendly and biodegradable, which offers a great advantage over many other chemical substances [45][46][47]. TGM is well-known for intra-molecular and inter-molecular formations of covalent bonds of glutamine and lysine, which initiate high-MW peptides, such as monomers, dimers, trimers, and oligomers.…”

Section: Origins Of Tgmsmentioning

confidence: 99%

Transglutaminase in Foods and Biotechnology

Vasić

Knez

Leitgeb

2023

IJMS

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Stabilization and reusability of enzyme transglutaminase (TGM) are important goals for the enzymatic process since immobilizing TGM plays an important role in different technologies and industries. TGM can be used in many applications. In the food industry, it plays a role as a protein-modifying enzyme, while, in biotechnology and pharmaceutical applications, it is used in mediated bioconjugation due to its extraordinary crosslinking ability. TGMs (EC 2.3.2.13) are enzymes that catalyze the formation of a covalent bond between a free amino group of protein-bound or peptide-bound lysine, which acts as an acyl acceptor, and the γ-carboxamide group of protein-bound or peptide-bound glutamine, which acts as an acyl donor. This results in the modification of proteins through either intramolecular or intermolecular crosslinking, which improves the use of the respective proteins significantly.

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