Creative BioMart is a well-known expert who committed to developing a variety of methods to explore enzyme sequences and create new high-efficiency biocatalysts. With years of experience, we provide customized enhancement of enzyme stability service to precisely meet customer requirements.

Introduction of Enzyme Stability

Enzyme stability is an important issue in enzyme engineering research. The total annual cost of enzyme-catalyzed chemical processes is about 20%, so studying enzyme stability is a key factor in determining the commercial success of biocatalytic applications. Studies have revealed that enzymes maintain their structural stability through various kinds of non-covalent interactions, including hydrogen bonds, salt bridges, hydrophobic interactions, and van der Waals forces. Several strategies have been proposed to improve enzyme stability: use soluble Additives, immobilization, protein engineering and chemical modification. In addition, many researchers try to improve enzyme stability and enhance enzyme activity through rational design and in vitro evolution of enzymes. Stability is one of the most desirable properties of the enzyme to be improved, and its enhancement has been widely used in clinical, industrial and environmental applications.

Fig 1. Effect of immobilization on enzyme stability. (Mateo C, et al., 2007)

Services

In the past, stable biocatalysts were produced through amino acid substitutions to increase structural rigidity, limit conformational flexibility, and increase the interaction between unstable domains. However, insufficient understanding of the structure-function relationship hinders the identification of suitable mutation targets. As a leading service provider of protein engineering, Creative BioMart has established a powerful platform for enhancing enzyme stability to explore new stabilization mechanisms and strategies to guide enzyme design. We can rationally design protein by considering various factors (hydrophobicity, hydrogen bond, solvent, protease, metal ion, temperature and pH value) to help you improve protein stability. In addition, we measure protein stability through Tm, the midpoint temperature of the thermal denaturation curve, and turnover in vivo of a number of enzymes correlates with Tm.

Our scientists are committed to developing a variety of strategies to improve the stability and half-life of enzymes, including but not limited to:

1. Directed evolution with canonical amino acids.
2. Screening for enzymes from extremophiles and their isolation. The protein is attached to the matrix material.
3. Production of stable enzymes in genetically manipulated mesophilic organisms.
4. Stabilize unstable enzymes by methods like protein engineering, chemical modification, immobilization and medium engineering by using/employing additives.

Enhancing stability while maintaining enzyme activity is an arduous task of protein engineering. We will work with you to develop the most appropriate strategy and provide the most meaningful data for your research for accelerating the research of life sciences. If you are interested in our services, please do not hesitate to contact us for more information.

References

1. Iyer P V, Ananthanarayan L. (2008) Enzyme stability and stabilization—aqueous and non-aqueous environment. Process biochemistry. 43(10): 1019-1032.
2. Mateo C, Palomo J M, Fernandez-Lorente G, et al.. (2007) Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme and microbial technology. 40(6): 1451-1463.

• Enzyme Activity Analysis Service
• Protease Substrate Screening Service
• Protease Substrate Specificity Profiling Service