Effects of In Vitro Proteolysis on the Allergenicity of Major Whey Proteins
J. Asselin, J. Hébert, Jean Amiot
Abstract
J. Asselin, J. Hébert, Jean Amiot
Abstract
ABSTRACT The effects of in vitro proteolysis on the allergenicity of major whey proteins (α‐lactalbumin and β‐lactoglobulin) by simulating the human gastrointestinal conditions were evaluated. The proteolysis of demineralized whey with pepsin (pH 2.0 for 30 min) and/or various pancreatic enzymes (pH 7.5 for 60 and 240 min) was performed by the pH‐stat technique at 37°C. The enzyme inactivation was performed by heating at 80°C for 20 min. Allergenicity of the hydrolyzates was evaluated by RAST inhibition using sera obtained from children allergic to whey proteins. Selective proteolysis of whey by pepsin and α‐chymotrypsin was the most efficient combination of enzymes to reduce the allergenicity of both α‐lactalbumin and β‐lactoglobulin. The above hydrolyzate could be used to develop an ingredient for infant milk formula with a lower allergenicity.
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ABSTRACT The effects of in vitro proteolysis on the allergenicity of major whey proteins (α‐lactalbumin and β‐lactoglobulin) by simulating the human gastrointestinal conditions were evaluated. The proteolysis of demineralized whey with pepsin (pH 2.0 for 30 min) and/or various pancreatic enzymes (pH 7.5 for 60 and 240 min) was performed by the pH‐stat technique at 37°C. The enzyme inactivation was performed by heating at 80°C for 20 min. Allergenicity of the hydrolyzates was evaluated by RAST inhibition using sera obtained from children allergic to whey proteins. Selective proteolysis of whey by pepsin and α‐chymotrypsin was the most efficient combination of enzymes to reduce the allergenicity of both α‐lactalbumin and β‐lactoglobulin. The above hydrolyzate could be used to develop an ingredient for infant milk formula with a lower allergenicity.
Key concepts: Proteolysis, Pepsin, Lactalbumin, Chemistry, Whey protein, Beta-lactoglobulin, Trypsin, Enzyme