Rational protein design for enhancing thermal stability of industrial enzymes

Authors

DOI:

https://doi.org/10.46223/HCMCOUJS.tech.en.8.1.340.2018

Keywords:

industrial enzymes; introduction of disulfide bonds; introduction of proline; rational proteindesign; thermostability

Abstract

Enzymes possessing many excellent properties such as high selectivity, consuming less energy, and producing less side products or waste have been widely applied as biocatalysts in pharmaceutical production and many industries such as biofuel, biomaterials, biosensor, food, and environmental treatment. Although enzymes have shown its potential as biocatalysts for many industrial applications, natural enzymes were not originated for manufacturing process which requires harsh reaction conditions such as high temperature, alkaline pH, and organics solvents. It was reported that reduction of final conversion of several enzymatic reactions was declined at high temperature. Protein engineering to improve the enzymes’ thermostability is crucial to extend the use of the industrial enzymes and maximize effectiveness of the enzyme-based procesess. Various industrial enzymes with improved thermostability were produced through rational protein engineering using different strategies. This review is not aimed to cover all successful rational protein engineering studies. The review focuses on some effective strategies which have widely used to increase the thermostability of several industrial enzymes through introduction of disulfide bonds and introduction of proline.

Downloads

Download data is not yet available.

References

Akoh, C. C., Chang, S. W., Lee, G. C., & Shaw, J. F. (2007). Enzymatic approach to biodiesel production. Journal of Agricultural and Food Chemistry, 55, 8995-9005.

Anbar, M., Gul, O., Lamed, R., Sezerman, U. O., & Bayer, E. A. (2012). Improved thermostability of clostridium thermocellum endoglucanase Cel8A by using consensus-guided mutagenesis. Applied and Environmental Microbiology, 78(9), 3458-3464.

Anfinsen, C., & Scheraga, H. (1975). Experimental and theoretical aspects of protein folding. Advances in Protein Chemistry, 29, 205-300.

Arnold, F. H. (2001). Combinatorial and computational challenges for biocatalyst design. Nature, 409, 253-257.

Badieyan, S., Bevan, R. D., & Zhang, C. (2012). Study and design of stability in GH5 Cellulases. Biotechnology and Bioengineering, 109, 31-44.

Downloads

Received: 03-06-2020
Accepted: 03-06-2020
Published: 17-08-2018

Statistics Views

Abstract: 410
PDF: 336

How to Cite

Tuan, L. Q. A. (2018). Rational protein design for enhancing thermal stability of industrial enzymes. HO CHI MINH CITY OPEN UNIVERSITY JOURNAL OF SCIENCE - ENGINEERING AND TECHNOLOGY, 8(1), 3–17. https://doi.org/10.46223/HCMCOUJS.tech.en.8.1.340.2018