Advances in the Production of Recombinant Protease through Expression Systems: An Updated Review

Enzymes are proteins that act as biocatalysts and have been revolutionized in several fields and industries owing to their unique properties. Proteases are enzymes that hydrolyze peptide bonds in proteins. They are widely employed in the food, biotechnology, and pharmaceutical industries. As the demand for proteases increases, there is a growing focus on enhancing the expression and synthesis of protease enzymes in microorganisms using recombinant DNA technology, which has attracted attention due to its high potential in biotechnology. Several expression systems, such as Bacillus, E. coli, and Saccharomyces cerevisiae, are commonly employed for the synthesis of proteases. The accurate selection of an expression system for a microorganism depends greatly on the protease in terms of functional modifications and activity. However, the native protease host does not show increased expression. As a result, the production of recombinant proteases has emerged as a crucial target that provides a high yield of protease and is cost-effective. Despite this advancement, there are still some challenges, such as the specificity and stability of the expression systems. This review presents an overview of the primary factors that enhance protein expression, as well as several strategies that increase the production of recombinant proteases, such as improving signal peptidases, promoter regions, and fermentation conditions. The applications of protease enzymes are also discussed, with the aim of presenting diverse sources and approaches for producing recombinant proteases using various expression systems. Furthermore, protease production from expression systems is still evolving, offering a wide range of applications in diverse industries.