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CGTase

Cyclodextrin glucanotransferase (CGTase) is an enzyme that catalyzes the conversion of starch and related glucans into cyclodextrins through transglycosylation and hydrolysis. In a starch medium, CGTase cleaves α-1,4-glycosidic bonds and facilitates the formation of cyclic glucan molecules consisting of 6, 7, or 8 glucose units, known as α-, β-, and γ-cyclodextrins. The distribution of these products depends on the enzyme source, substrate, and reaction conditions.

CGTase is produced by several bacteria, with Bacillus circulans historically the most prominent source. Additional thermostable

Applications of CGTase center on cyclodextrin production. Cyclodextrins are widely used as inclusion complexes to improve

variants
have
been
described
in
Bacillus
stearothermophilus
and
related
species.
These
enzymes
are
active
at
moderate
to
high
temperatures
and
neutral
to
mildly
acidic
pH,
often
displaying
optimal
activity
in
the
range
of
roughly
50–70°C
and
pH
around
4.5–6.0.
Some
CGTases
require
chloride
ions
to
enhance
cyclization
over
hydrolysis
and
to
influence
product
distribution.
the
solubility,
stability,
and
delivery
of
pharmaceuticals,
flavors,
and
fragrances,
as
well
as
in
food,
cosmetics,
and
agricultural
products.
β-Cyclodextrin
is
particularly
valuable
for
many
industrial
uses
due
to
its
cavity
properties.
Industrial
processes
generally
convert
starch
to
a
mixture
of
cyclodextrins,
followed
by
downstream
purification
using
precipitation,
adsorption,
and
chromatographic
methods.
Protein
engineering
and
process
optimization
are
employed
to
favor
the
production
of
specific
cyclodextrin
types
and
to
improve
enzyme
performance
and
recyclability.