Catalysts increase the rate of otherwise slow or imperceptible reactions without undergoing any net change in their structure. The early development of the concept of catalysis in the 19th century went hand in hand with the discovery of powerful catalysts from biological sources. These were called enzymes and were later found to be proteins. They mediate all synthetic and degradative reactions carried out by living organisms. They are very efficient catalysts, often far superior to conventional chemical catalysts, for which reason they are being employed increasingly in today's high-technological society, as a highly significant part of biotechnological expansion. Their utilization has created a billion dollar business including a wide diversity of industrial processes, consumer products, and the burgeoning field of biosensors. Further applications are being discovered constantly.
Enzymes have a number of distinct advantages over conventional chemical catalysts. Foremost amongst these are their specificity and selectivity not only for particular reactions but also in their discrimination between similar parts of molecules (regiospecificity) or optical isomers (stereospecificity). They catalyse only the reactions of very narrow ranges of reactants (substrates), which may consist of a small number of closely related classes of compounds (e.g. trypsin catalyses the hydrolysis of some peptides and esters in addition to most proteins), a single class of compounds (e.g. hexokinase catalyses the transfer of a phosphate group from ATP to several hexoses), or a single compound (e.g. glucose oxidase oxidises only glucose amongst the naturally occurring sugars). This means that the chosen reaction can be catalysed to the exclusion of side-reactions, eliminating undesirable by-products. Thus, higher productivities may be achieved, reducing material costs. As a bonus, the product is generated in an uncontaminated state so reducing purification costs and the downstream environmental burden. Often a smaller number of steps may be required to produce the desired end-product. In addition, certain stereospecific reactions (e.g. the conversion of glucose into fructose) cannot be achieved by classical chemical methods without a large expenditure of time and effort. Enzymes work under generally mild processing conditions of temperature, pressure and pH. This decreases the energy requirements, reduces the capital costs due to corrosion-resistant process equipment and further reduces unwanted side-reactions. The high reaction velocities and straightforward catalytic regulation achieved in enzyme-catalysed reactions allow an increase in productivity with reduced manufacturing costs due to wages and overheads.
There are some disadvantages in the use of enzymes which cannot be ignored but which are currently being addressed and overcome. In particular, the high cost of enzyme isolation and purification still discourages their use, especially in areas which currently have an established alternative procedure. The generally unstable nature of enzymes, when removed from their natural environment, is also a major drawback to their more extensive use.