An 

immobilized enzyme is an enzyme attached to an inert,

insoluble material—such as calcium alginate (produced by
reacting a mixture of sodium alginate solution
and enzyme solution with calcium chloride). This can provide
increased resistance to changes in conditions such as pH or
temperature.

Enzymes immobilised in beads of alginate gel

It also lets enzymes be held in place throughout the reaction,
following which they are easily separated from the products and
may be used again. This is widely used in industry
for enzyme catalysed reactions.
Immobilized enzymes are very important for commercial uses as
they possess many benefits to the expenses and processes of the
reaction of which include:
● Convenience: Minuscule amounts of protein dissolve in the
reaction, so workup can be much easier. Upon completion,
reaction mixtures typically contain only solvent and reaction
products.
● Economy: The immobilized enzyme is easily removed from
the reaction making it easy to recycle the biocatalyst. This is
particularly useful in processes such as the production of
Lactose Free Milk, as the milk can be drained from a
container leaving the enzyme (Lactase) inside ready for the
next batch.
● Stability: Immobilized enzymes typically have
greater thermal and operational stability than the soluble form
of the enzyme.
In the past, biological washing powders and detergents
contained many proteases and lipases that broke down dirt.
However, when the cleaning products contacted human skin,
they created allergic reactions. This is why immobilization of
enzymes are important, not just economically.
There are various ways by which one can immobilize
an enzyme:
● Affinity-tag binding: Enzymes may be immobilized to a
surface, e.g. in a porous material, using non-covalent or
covalent Protein tags. This technology has been established
for protein purification purposes.
● Adsorption on glass, alginate beads or matrix: Enzyme is
attached to the outside of an inert material. As adsorption is
not a chemical reaction, the active site of the immobilized
enzyme may be blocked by the matrix or bead, greatly
reducing the activity of the enzyme.
● Entrapment: The enzyme is trapped in insoluble beads or
microspheres, such as calcium alginate beads. However, this
insoluble substance hinders the arrival of the substrate, and
the exit of products.
● Cross-linkage: Enzyme molecules are covalently bonded to
each other to create a matrix consisting of almost only
enzyme. The reaction ensures that the binding site does not
cover the enzyme's active site, the activity of the enzyme is
only affected by immobility. Use of a spacer molecule like
polyethylene glycol helps reduce the steric hindrance by the
substrate in this case.
● Covalent bond: The enzyme is bound covalently to an
insoluble support (such as silica gel). This approach provides
the strongest enzyme/support interaction, and so the lowest
protein leakage during catalysis.