Sucrase Sucrase
is a yeast-derived enzyme. Sucrase splits sucrose into glucose and fructose (invert
syrup) and can be applied for any inversion of sucrose especially liquefied cherry
centers, creams, mints, truffles, marshmallow, invert syrup and other fondants.
Sucrase is used to improve shelf life of confections. It is available in single,
double and triple strengths and is packaged in one, ten and 44 pound containers
for ease of use, storage and cost efficiency.
The official name for Sucrase
is beta-fructofuranosidase (EC3.2.1.26), which implies that the reaction catalyzed
by this enzyme is the hydrolysis of the terminal nonreducing beta-fructofuranoside
residues in beta-fructofuranosides. Note that alpha-D-glucosidase, which splits
off a terminal glucose unit, can also catalyze this reaction. Note that sucrose
can be hydrolyzed relatively easily; the reaction proceeds in an acidic environment
without the aid of Sucrase.
Sucrase is mainly used in the food (confectionery)
industry where fructose is preferred over sucrose because it is sweeter and does
not crystallize as easily. However, the use of Sucrase is rather limited because
another enzyme, glucose isomerase, can be used to convert glucose to fructose
more inexpensively. For health and taste reasons, its use in food industry requires
that Sucrase be highly purified.
A wide range of microorganisms produce
Sucrase and can, thus, utilize sucrose as a nutrient. Commercially, Sucrase is
biosynthesized chiefly by yeast strains of Saccharomyces cerevisiae or Saccharomyces
carlsbergensis. Even within the same yeast culture, Sucrase exists in more than
one form. For example, the intracellular Sucrase has a molecular weight of 135,000
Daltons, whereas the extracellular variety has a molecular weight of 270,000 Daltons.
In
contrary to most other enzymes, Sucrase exhibits relatively high activity over
a broad range of pH (3.5--5.5), with the optimum near pH=4.5. The enzyme activity
reaches a maximum at about 55ºC. The Michaelis-Menten values of various enzymes
vary widely, but for most enzymes Km is between 2 mM and 5 mM. The Michaelis-Menten
value for the free enzyme is typically approx. 30 mm.
Enzyme inhibition
is an extremely important area of research in the medical field. For example,
lead, mercury, other heavy metals, and nerve gases are extremely poisonous to
humans because they are inhibitory to enzymes. For example, Pb^++ can easily react
with the sulfhydryl (-SH) groups in a protein.
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