Rational protein design for enhancing thermal stability of industrial enzymes

Abstract

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