The effect of the length of polysaccharide chains on the functional
properties of Maillard-type
protein−polysaccharide conjugates was investigated using the lysozyme
as a model protein, various
sizes of galactomannan as a polysaccharide, and xyloglucan as an
oligosaccharide. The emulsifying
properties of the lysozyme−galactomannan conjugates increased in
proportion to the length of
polysaccharide chains. On the other hand, the heat stability of
the lysozyme−galactomannan
conjugates greatly increased in the range of 3.5−24 kDa
galactomannan, regardless of its molecular
mass. In addition, the effects of the binding number of
polysaccharide to lysozyme on the emulsifying
properties of the lysozyme−galactomannan conjugates were further
investigated using 1 and 2 mol
of the galactomannan (24 kDa)-attached lysozyme. The 2 mol of the
polysaccharide-attached
lysozyme showed better emulsifying properties than 1 mol of the
polysaccharide-attached protein.
The residue most sensitive to the Maillard reaction in a lysozyme
was identified as the 97-lysine
using the lysozyme−xyloglucan conjugate.
Keywords: Lysozyme; Maillard-type protein−polysaccharide conjugate;
galactomannan; xyloglucan
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