Industrial Enzymes

2.2.7

They are powerful catalysts

Features that make enzymes so useful in industrial processes are: Specifity - enzymes can catalyse reactions between specific chemicals, even in mixtures of many different chemicals. This means that fewer byproducts are formed and less purification of products is necessary. Temp of enzyme action - most function well at low temps, much lower than those needed for many industrial chemical processes. This saves money on fuel costs. However, enzymes from thermophillic bacteria have been extracted and used in reactions that need a higher temperature. In biotechnological processes whole organisms are cultured on a large scale to generate particular products. In clinical research, diagnosis and industrical processes the product of a single chemical reaction is required. It is often more efficient to use isolated enzymes to carry out the reaction rather than growing the whole organism or using an inorganic catalyst. Isolated enzymes can be produced in large quantities in commercial biotechnological processes. The extraction of enzyme from the fermentation mixture is known as downstream processes.

Immobilising Enzymes
For the product of an enzyme reaction to be generated an enzyme-substrate complex must be formed. This is more easily acheived by mixing quantities of substrate and isolated enzyme together under suitable conditions for the enzyme to work. The product generated then needs to be extracted from the mixture, this can be expensive. It is possible to immobilise the enzymes so that they can continue to catalyse the enzyme controlled reaction but do not mix freely with the substrate as they would normally in a cell or isolated system.

Advantages and Disadvantages of immobilising

Advantages Enzymes are not present with products so purifications/downstream processing costs are low. Enzymes are immediately available for reuse. This is particuarly useful in allowing for continuous processes. Immobilised enzymes are more stable because the immobilising matrix protects the enzyme molecules. Disadvantages Immobilisation requires additional time, equipment and materials and so is more expensive to set up. Immobilised enzymes can be less active because they do not mix freely with substrate. Any contamination is costly to deal with because the whole system would need to be stopped.

Methods for immobilising enzymes

Absorption Enzyme molecules are mixed with the immobilising support and bind to it due to a combination of hydrophobic interactions and ionic links. Absorbing agents used include porous carbon, glass beads, clays and resins. Because the bonding forces are not particuarly strong, enzymes can become detatched. Covalent Bonding Molecules are covalently bonded to a support, often by covalently linking enzymes together and to an insoluble material, using a cross-linking agent. This method does not immobilise a large quantity of enzyme but binding is very strong so there is less leakage of enzyme from the support. Entrapment The enzymes are trapped in their natural state, however reactions can be reduced because substrate molecules need to get through the trapping barrier, this means the active site is less easily available than with absorbed or covalently bonded enzymes.