ABSTRACT
Most enzymes have been condition adapted by developing lab strains of industrial enzyme-producing fungi and bacteria. To overcome the limitations of naturally occurring enzymes, scientists and engineers have used multiple approaches to develop economically viable biocatalysts with desirable characteristics. However, only a small subset of microorganisms can be readily cultivated in a laboratory setting. Thus, scientists began to place more emphasis on bioprospecting and metagenomic approach. Two general approaches in protein engineering have been employed with varying levels of success: rational design and directed evolution. An example of rational design application is the enhancement of enzyme thermostability without reducing catalytic activity. Rational design can be applied to other biomolecular interactions such as pharmaceutical design, enhancement of molecular docking systems, biosynthesis, and development of nanotechnology. The semirational approach builds on the strengths of both rational and random variant design to produce smaller but more focused libraries that facilitate efficiency in directed evolution.
