β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose.
Sugar can be inverted by sulfuric acid but this is not suitable for food-grade products and enzymic hydrolysis is preferred.
[3] Invertase is produced by various organisms such as yeast, fungi, bacteria, higher plants, and animals.
[4] Urea acts as a pure non-competitive inhibitor of invertase, presumably by breaking the intramolecular hydrogen bonds contributing to the tertiary structure of the enzyme.
Finally, the nucleophilic oxygen atom from alcohol or water will attack the C-2 cation which will leave behind a fructose molecule.
Dimerization is an important aspect of protein folding due to it increasing the affinity of substrate binding.
The “‘closed’ arrangement” dimers have fourteen out of the 32 hydrogen bonds made between the catalytic domain which creates a tighter pocket for the ligand; in turn, this makes it more stable.
In contrast, the “‘open’ assembly” dimers only have a few hydrogen bonds in the catalytic domain, and the interactions that strengthen the pocket come from the salt bridges between Asp-45 and Lys-385.