layers of the protein [18-19, 21-22]. The molecular weight of potential partners with
the protein is important in this relationship.
Among the molecules of di-, monosaccharides and dipoles of water, the fastest
contact occurs with water molecules; larger sugars molecules are generally excluded
from the space around the protein molecule (due to the excluded volume [20]). As a
result, this space is also enriched by water molecules, since any contact of the protein
with sugar molecules in the solvent volume is thermodynamically disadvantageous and
contributes to the energy expenditure in the system necessary for the restructuring of
the solvent structure.
In this way, the protein will try to minimize the area of its surface that contacts
with a solvent such as sugar and water. At the same time, the difference in molecular
weight will provide monosaccharides molecules with greater access to albumin and, as
a consequence, more reliable interrelationships between them compared to
disaccharides. Perhaps this is why most disaccharide molecules will be located in the
water around the protein molecule, having less contact with the protein globe than
monosaccharides. Therefore, the molecules of disaccharides are more dehydrating
substances relative to the protein than the monosaccharides molecules, and their
hydration ability tends to increase. In molecules of monosaccharides, the potential to
form complexes with a protein molecule is higher, which can reduce the amount of
hydrophilic bonds of sugars oriented to water dipoles. As a result, there is a
deterioration of their hydration ability in the system with ovalbumin.
Thus, the effect of sugars on the process of foaming of ovalbumin with sugars is
determined by two main factors. First of all, foaming depends on the solubility of
sugars, which determines the coefficient of surface tension and the kinematic viscosity
of their solutions. Secondly, the ability of the protein to develop foam will depend on
the interaction of hydroxyl groups of sugars with polar amino acid groups of protein in
the monomolecular layer, which significantly influences the hydration of ovalbumin.
Thus, it has been established that high solubility of lactulose at temperatures of
foam formation of ovalbumin and its significant dehydration ability due to to the latter,
has a negative effect on foam formation and the FFA index for its systems is the least.
Monosaccharide molecules are more involved in the formation of the adsorption layer
of the protein, due to which their hydration capacity is lower and the process of foam
development occurs more compared to disaccharides. At the same time, high solubility
of fructose increases the coefficient of surface tension of its solutions and increases
their viscosity, which does not provide high rates of FFA.
The obtained data will be taken into account when creating confectionery
products. For example, the addition of lactulose to systems with saccharose or glucose
will reduce FFA, but will increase the stability of the system to stratification;
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