Protein modification for health benefits
Proteins can be modified by the covalent attachment of polysaccharides utilizing the Maillard reaction. Recently, a novel method was developed at University of Wisconsin where conjugation was achieved in (liquid) batch processed mixtures. Protein denaturation/aggregation was inhibited by conducting the process in the presence of a crowding agent (such as dextran). A food-grade chromatography method was developed to purify these conjugates. Conjugated proteins produced by this method had excellent solubility and heat stability and did not exhibit browning or off-flavors. Using an in vitro infant digestion model (i.e., physiological amounts of enzymes that matched in vivo infant digestion rate of β-lactoglobulin), we also demonstrated that conjugated proteins were digested more slowly than unmodified proteins, which could help avoid the high titers of immunoreactive proteins for sensitive infants. We obtained blood sera from patients that had cow’s milk protein allergy. The IgE binding capacity of conjugates was tested using the ImmunoCap method. Conjugation of allergenic protein significantly reduced IgE binding but we observed large individual (patient) differences for the level of reduction in IgE binding. Conjugation may be helpful in reducing the allergenicity of food proteins.
Maillard, digestion, allergenicity