Using the catalytic power of enzymes to perform highly stereo selective organic transformations has been the basis of the ever-expanding field of biocatalysis. Enzymes have evolved over millions of years to be some of the best catalysts available to chemists. Now, through advances in molecular and synthetic biology, chemists are able to redesign the active sights of many enzymes to fit their synthetic needs. Biocatalysis has been around for a long time. In fact, it was probably the first type of multi-step chemical reaction humans ever carried out, over 9000 years ago. But seeing as the product of that particular reaction was beer, that’s hardly surprising. Lab coat or mammoth hide, scientists never change. What does change is how the pharmaceutical industry uses biocatalysis. While fermentation technology was used in key drug developments in the past, such as the production of penicillin in 1941, for most of the 20th century the industry favoured transition metal catalysts and the profitable mining that uncovered them. It’s only in the last 20 years or so that synthetic labs have come around to the B-word. Using the DNA sequence of known enzymes, it is possible to search for sequences which are similar. If these same sequences are found, it can then be placed into a different organism and then made to see if the sequence does in fact code for an enzyme.  Articles from difference backgrounds will be received, and renowned, and highly qualified, expert reviewers.  Main of the Open access policies are highly appreciable, accepted and adaptable to the criteria that have been prescribed by the international agencies.