Related Experiment Video
Updated: May 23, 2026
11:25
Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
[Progress in expression and molecular modification of microbial transglutaminase]
Song Liu1, Dongxu Zhang, Guocheng Du
1Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China.
Summary
Microbial transglutaminase (MTG) production has advanced through recombinant strain development, enhancing enzyme yield and enabling molecular modifications for improved activity and stability.
Area of Science:
- Biochemistry
- Protein Engineering
- Industrial Microbiology
Context:
- Microbial transglutaminase (MTG) catalyzes protein cross-linking, finding applications in food, pharmaceuticals, and textiles.
- Recombinant DNA technology has been employed since the 1990s to improve MTG production.
- Various expression systems have been utilized for successful MTG enzyme expression.
Purpose:
- To review strategies for enhancing microbial transglutaminase yield and molecular modification.
- To analyze recent advancements in improving MTG activity, thermo-stability, and specificity.
- To identify future trends in MTG research and development.
Summary:
- Recombinant strain construction has significantly increased microbial transglutaminase (MTG) yield compared to wild strains.
- Molecular modification of MTG has led to improved enzyme activity, thermal stability, and specificity.
- Successful expression of MTG has been achieved across diverse expression systems.
Impact:
- Enhanced MTG production facilitates wider industrial applications.
- Improved enzyme properties open new avenues for MTG utilization in various sectors.
- Advancements in MTG research pave the way for novel biotechnological solutions.
Related Concept Videos
01:24Tagging and Fusion Proteins
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
01:30Production of Pharmaceuticals
Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...