Breaking cells and extracting high-purity, highly active proteins or peptides is a key goal for researchers and biotech professionals. Among the various methods available, ultrasonic disruption has long been a popular choice. It works by using the cavitation effect of sound waves in liquid to break down cell structures. While it's easy to use, ultrasonic methods can be costly and often lead to significant temperature increases, which may denature sensitive biological molecules. In larger-scale operations, free radicals can form, potentially inactivating certain active substances. The effectiveness of sonication varies depending on the microorganism: bacilli are generally easier to break than cocci, and Gram-negative bacteria are more susceptible than Gram-positive ones. Yeast, however, tends to be more resistant. As research advances and demand for high-activity proteins grows, traditional ultrasonic methods are no longer sufficient.
High-pressure cell disruption offers an alternative approach. Instead of relying on sound waves, this method uses extreme pressure to force the sample through a narrow chamber at high speed—often hundreds of meters per second. The resulting shear forces, collisions, and cavitation within the system cause the cells to rupture. This technique is especially effective when applied at pressures above 100 MPa, known as ultra-high pressure. Under these conditions, non-covalent bonds in the cell structure are disrupted, leading to membrane damage and the release of intracellular components. This makes the process ideal for destroying microbial cells without the need for chemicals.
The development of low-temperature ultra-high pressure continuous flow cell disruptors has addressed many of the limitations of traditional methods. These systems operate under controlled, low-temperature conditions (typically 4–6°C), ensuring that heat generated during the process is efficiently removed. This helps preserve the integrity and activity of proteins and peptides. Through extensive design and testing, engineers have optimized the balance between shear, collision, and cavitation to maximize cell disruption while minimizing damage to sensitive biomolecules.
In a comparative study, we tested both a conventional ultrasonic cell disruptor and a low-temperature ultra-high pressure continuous flow cell disruptor on the same amount of *E. coli*. The results showed that the polypeptide activity obtained using the low-temperature system was significantly higher—155 U/mg compared to 110 U/mg from ultrasonication. This represents a 40% improvement in activity, demonstrating the superior performance of the new technology.
Reference: Expression and purification and identification of recombinant glucagon-like peptide-1 derived polypeptide, Chinese Journal of Biotechnology, 2009, 29(6): 1–6.
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