Industrial enzymes

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Industrial enzymes are enzymes that are commercially used in a variety of

industries such as pharmaceuticals, chemical production, biofuels, food & beverage,
and consumer products. Due to advancements in recent years, biocatalysis through
isolated enzymes is considered more economical than use of whole cells. Enzymes
may be used as a unit operation within a process to generate a desired product, or
may be the product of interest. 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.[1] Isolated enzymes are typically used
in hydrolytic and isomerization reactions. Whole cells are typically used when a
reaction requires a co-factor. Although co-factors may be generated in vitro, it is
typically more cost-effective to use metabolically active cells. [1]

Contents

 1Enzymes as a unit of operation

o 1.1Immobilization
 1.1.1Adsorption
 1.1.2Covalent binding
 1.1.3Affinity
 1.1.4Entrapment
o 1.2Recovery
 2Enzymes as a desired product
o 2.1Upstream
 2.1.1Selection of a suitable enzyme
 2.1.2Identification and selection of a suitable source for the selected enzyme
 2.1.3Process development
 2.1.4Large scale production
o 2.2Downstream
 2.2.1Removal of insoluble materials and recovery of enzymes from the
source
 2.2.2Concentration and primary purification of enzymes
 3See also
 4References

Enzymes as a unit of operation[edit]

Immobilization[edit]
Despite their excellent catalytic capabilities, enzymes and their properties must be
improved prior to industrial implementation in many cases. Some aspects of
enzymes that must be improved prior to implementation are stability, activity,
inhibition by reaction products, and selectivity towards non-natural substrates. This
may be accomplished through immobilization of enzymes on a solid material, such
as a porous support.[2] Immobilization of enzymes greatly simplifies the recovery
process, enhances process control, and reduces operational costs. Many
immobilization techniques exist, such as adsorption, covalent binding, affinity, and
entrapment.[3] Ideal immobilization processes should not use highly toxic reagents in
the immobilization technique to ensure stability of the enzymes. [4] After immobilization
is complete, the enzymes are introduced into a reaction vessel for biocatalysis.
Adsorption[edit]
Enzyme adsorption onto carriers functions based on chemical and physical
phenomena such as van der Waals forces, ionic interactions, and hydrogen bonding.
These forces are weak, and as a result, do not affect the structure of the enzyme. A
wide variety of enzyme carriers may be used. Selection of a carrier is dependent
upon the surface area, particle size, pore structure, and type of functional group. [5]
Covalent binding[edit]

Example of Enzyme Immobilization through Covalent Binding

Many binding chemistries may be used to adhere an enzyme to a surface to varying

degrees of success. The most successful covalent binding techniques include
binding via glutaraldehyde to amino groups and N-hydroxysuccinide esters. These
immobilization techniques occur at ambient temperatures in mild conditions, which
have limited potential to modify the structure and function of the enzyme. [6]
Affinity[edit]
Immobilization using affinity relies on the specificity of an enzyme to couple an
affinity ligand to an enzyme to form a covalently bound enzyme-ligand complex. 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. [3]
Entrapment[edit]
Immobilization using entrapment relies on trapping enzymes within gels or fibers,
using non-covalent interactions. Characteristics that define a successful entrapping
material include high surface area, uniform pore distribution, tunable pore size, and
high adsorption capacity