The roles of sulfhydryl/disulfide interactions and acid/pepsin hydrolysis on β-lactoglobulin (β-lg) thermal aggregation at acidic pH 3.35 and 2 were studied using rheology, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transmission electron microscopy (TEM), and Western blotting. Pepsin promoted additional hydrolysis compared to the acid-hydrolyzed control sample based on a 12% increase in free amino groups.
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