Microbiosci is a leading company offering the best microbial gene expression service. Backed by years of development and research experience, our talented scientists will help you achieve your research goals quickly and efficiently. They would research closely with you to offer your one stop service in microbial gene expression system. All you need to do is simply provide the gene sequences.
Microbial enzymes have been used in a large number of fields, such as chemical, agricultural and biopharmaceutical industries1. Some commodity chemicals or enzymes benefit major sectors of the biopharmaceutical, agricultural and chemical industries2. As chemical synthesis undergo inherent constraints that limit regular large-scale production, recombinant DNA technologies have rapidly become a choice for commodity chemicals or enzymes production. There is a wide and growing spectrum of expression systems that are becoming available, such as Escherichia coli, Bacilli (e.g., Bacillus subtilis), lactic acid bacteria (e.g., Lactobacillus lactis), filamentous fungi (e.g., Aspergillus) and yeasts (e.g., Pichia pastoris) and so on. Microbial expression systems remain very attractive due to their ability to grow rapidly and at high density on inexpensive substrates, their well-characterized genetics and the availability of an increasingly large number of cloning vectors and mutant host strains1.
Fig.1 Systems-level engineering strategies of microbial expression system (Liu, et al. 2017)1
As a leader in microbial gene expression service, Microbiosci provides a "one-stop shop" tailored to your research needs. Our services range from codon optimization to gene synthesis, clonal selection and purify. It's entirely customizable and flexible to fit how you run projects. At the theoretical level, the steps are pretty straightforward.
Rapid growth rate
Capacity for continuous fermentation
Does not possess necessary machinery for removing in-trons from transcripts
Foreign gene might contain sequences that act as termina-tion signals resulting in premature termination and loss of gene expression
Lack of post translational modifications
Glycosylation is extremely uncommon in bacteria
Production of proteins in the insoluble form or in the form of inclusion bodies
Degradation of proteins
Accumulation of endotoxins
Rapid growth in low cost medium
Appropriate post-translational modifications
Safety of the system is guaranteed
No endotoxins production
Hyperglycosylation of proteins
Inefficient in secreting the proteins into growth medium leading to intracellular retention
Does not produce LPS/endotoxins
Can be transformed readily with many bacteri-ophages and plasmids
Capable of secreting functional extracellular proteins directly into the culture medium
Production of extracellular proteases which can recognize and degrade heterologous proteins
Instability of plasmids
Reduced or non expression of the protein of interest
Not producing endotoxins;
Minimal protease activities;
Secreting properly folded and functional protein to the culture
Much lower transformation efficiency
Few expression vectors being available
|Filamentous fungus||High-level of expression|
Lack of knowledge on physiology
• Easy to Culture
• Grow Fast
• High Titer
• Vaccine Seed Development
• Gene Therapies
Microbiosci is the premier institution to provide professional and comprehensive gene expression services. Microbiosci is dedicated to providing complete solutions for gene expression to meet your specific project needs. Simply let us know the sequences you want to express. We will propose the best strategy for you.
1. Liu, L., Yang, H., Shin, H. D., Chen, R. R., Li, J., & Du, G., et al. (2013). How to achieve high-level expression of microbial enzymes. Bioengineered Bugs, 4(4), 12.
2. Sanchezgarcia, L., Lucas Martín, Mangues, R., Ferrermiralles, N., Esther Vázquez, & Villaverde, A., (2016). Recombinant pharmaceuticals from microbial cells: a 2015 update. Microbial Cell Factories, 15(1), 1-7.
3. Gomes, Amitha Reena, et al. “An Overview of Heterologous Expression Host Systems for the Production of Recombinant Proteins.” Advances in Animal and Veterinary Sciences, vol. 4, no. 7, 2016, pp. 346–356.
4. Lambertz, Camilla, et al. “Challenges and Advances in the Heterologous Expression of Cellulolytic Enzymes: A Review.” Biotechnology for Biofuels, vol. 7, no. 1, 2014, pp. 135–135.