Product Description
APPLICATION
- Production of heat-stable trypsin dispersion solution;
- Production of biologics..
FEATURES
- Expressed in Recombinant Yeast;
- Highly heat-stable.
- Specific activity ≥ 2500 USP units/mg.
AI Product Description
*The following content is generated by AI and is for reference only.
Recombinant Heat-stable Trypsin represents a significant advancement in proteolytic enzyme technology, offering superior performance compared to traditional bovine or porcine trypsin. Produced via recombinant DNA technology, typically using *Escherichia coli* expression systems, this engineered enzyme possesses a unique amino acid sequence that confers exceptional thermal stability. Unlike native trypsin, which denatures rapidly at temperatures above 37°C, the recombinant variant maintains full catalytic activity even at elevated temperatures up to 50-60°C and across a broad pH range of 7.0 to 9.0. This robustness makes it ideal for industrial processes requiring harsh conditions without the risk of enzyme degradation.
The molecular formula is not applicable in the traditional sense as it is a protein polymer; however, its specific primary structure consists of approximately 240 amino acids with a molecular weight of roughly 24 kDa. It lacks a defined CAS number because it is a genetically modified biological product rather than a small chemical molecule, often identified by manufacturer-specific catalog numbers or accession codes in biobanks. The core mechanism involves cleaving peptide bonds on the carboxyl side of basic amino acids, arginine and lysine, facilitating efficient protein digestion.
Key applications span diverse sectors including peptide mapping, mass spectrometry sample preparation, and large-scale protein hydrolysis in the food industry. In pharmaceutical manufacturing, its high purity and low endotoxin levels are crucial for producing therapeutic peptides and vaccines. Furthermore, the heat stability allows for simplified process workflows where sterilization steps can be integrated directly into the reaction vessel, reducing contamination risks and operational costs. Its consistency ensures reproducible results in research settings, making it a preferred choice for genomic sequencing, antibody fragment generation, and diagnostic assays. By eliminating animal-derived components, it also addresses ethical concerns and reduces the risk of viral transmission associated with tissue-sourced enzymes. Overall, Recombinant Heat-stable Trypsin stands as a versatile, reliable tool driving efficiency and innovation in modern biotechnology and industrial enzymology.