Enzymes strategies have been extensively studied and immerged

Enzymes are ubiquitous natural
biocatalyst that are increasingly attractive to the field of chemical
transformation, biosensing, bioremediation and disease therapy. This attraction
is derived from some excellent features of enzymes such as, high turn-over
number, high activity, selectivity and specificity among others. In addition to
that, enzymes offer to perform most complex chemical process under the very
mild environmental and experimental conditions. However together with these
suitable properties, enzyme have others that make their implementation
difficult. Among these the storage and operational stabilities affect the
usefulness of enzymes in many instances. Major application of enzymes involves harsh
operational conditions such as high temperature, high salt concentration,
presence of surfactant/chaotropic agents, high or low pH, presence of
proteolytic enzymes, and the presence of organic solvents where organic solvent
is used to increase the solubility of hydrophobic substrate in aqueous medium.

Hence, the need to stabilize enzymes against thermo-deactivation, deactivation
in presence of organic solvent, surfactant or chaotropic agents is imperative.

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There have been many approaches to improve the enzyme stability: enzyme
immobilization, enzyme modification, protein engineering, and medium
engineering. Among these stabilization methods, immobilization strategies have
been extensively studied and immerged as a powerful tool to improve almost all
enzymes properties. It involves attachment or incorporation of enzymes onto or
into large nanostructures via simple adsorption, covalent attachment, or
encapsulation. However, this method of enzyme stabilization suffers several
disadvantages such as, mass transfer limitations, loss of enzyme activity, loss
of the enzyme due to leakage, operational restraints, requirement for
additional material and equipment, immobility of enzyme molecules inside
carriers, particle erosion and non-biological compartmentalization of enzymes
for disease therapy.

Recently we have developed an
enzyme immobilization technique capable of encapsulating enzymes inside the Qb
nanoparticles by RNA mediate noncovalent association. We have observed that
this method can improve enzyme production, isolation, performance, and lifetime
by sequestering the enzyme in a protective biocompatible shell that allows
small-molecule substrates and products to diffuse in and out. Moreover, the protective
shell able to stabilize enzymes against thermal degradation, protease attack,
and hydrophobic adsorption. Despite so many advantages in the preparation of Qb
nanoparticles encapsulated enzymes, many important aspects remain untouched and
that need to be addressed thoroughly. These understandings about VLP based
enzyme encapsulation will help such system evolve from study level to potential


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