Industrial enzymes

Due to advancements in recent years, biocatalysis through isolated enzymes is considered more economical than use of whole cells.

Industrial biological catalysis through enzymes has experienced rapid growth in recent years due to their ability to operate at mild conditions, and exceptional chiral and positional specificity, things that traditional chemical processes lack.

Some aspects of enzymes that must be improved prior to implementation are stability, activity, inhibition by reaction products, and selectivity towards non-natural substrates.

Enzyme adsorption onto carriers functions based on chemical and physical phenomena such as van der Waals forces, ionic interactions, and hydrogen bonding.

Selection of a carrier is dependent upon the surface area, particle size, pore structure, and type of functional group.

These immobilization techniques occur at ambient temperatures in mild conditions, which have limited potential to modify the structure and function of the enzyme.

The complex is introduced into a support matrix for which the ligand has high binding affinity, and the enzyme is immobilized through ligand-support interactions.

Ongoing research is performed to develop in situ separation techniques, where product is removed from the batch during the conversion process.

The selected enzyme defines the required operational properties, such as pH, temperature, activity, and substrate affinity.

Most enzymes are produced under aerobic conditions, and as a result, require constant oxygen input, impacting fermenter design.

Due to variations in the distribution of dissolved oxygen, as well as temperature, pH, and nutrients, the transport phenomena associated with these parameters must be considered.