Biocatalysis enzyme mutation

Finally, another critical aspect for rapid and predictive design is the lack of information available about the dynamics of these enzymatic systems. Prediction of the effect of a mutation on the enzyme structure and dynamics remains a difficult task. Molecular dynamics and simulations of protein and substrate motions combined with the use of biophysical techniques enabling conformational changes to be trapped have to be developed. Multidisciplinary approaches will undoubtedly lead to major advances in this field and help to promote the key role that computational methods must play for efficient re-engineering of enzymes. These new ways to accelerate the evolution process and identify mutation sites important for optimizing enzyme characteristics will help to provide rapidly a well-expressed, efficient, stable, and specific enzyme, in other words the ideal glucansucrase for biocatalysis. 

Of greater immediate relevance for this industrial biocatalysis is the use of genetic engineering to incorporate new proteins into a cell. The commercial products of this technology, such as insulin and chymosin, do not affect the metabolism of the producing cell they are end-products of their own right. If, on the other hand, the cell is altered to produce a new enzyme which is metabolically active in the cell itself, it becomes possible to extend a metabolic pathway by one or two desirable steps, an action which cannot be achieved through the normal process of mutation and selection, which can only act on the complement of enzymes which the cell already contains. This concept has been applied to a number of commercial processes, one of which is the manufacture of ascorbic acid. 

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