Difference in Allergenicity between β-Lactoglobulin in Bovine Milk and Caprine Milk is Related to Their Respective Digestive Stability.

Abstract

The underlying cause of differences in sensitization between bovine and caprine milk β-lactoglobulin (β-LG) remains unclear. In this study, denatured forms of bovine and caprine milk β-LG were obtained through reductive alkylation and evaluated for allergenicity and digestibility in Balb/c mice. Results indicated weaker sensitization to nondenatured caprine milk β-LG compared to nondenatured bovine milk β-LG, with no significant difference in sensitization observed between denatured β-LG from both sources. The nondenatured β-LG of caprine milk and two types of denatured β-LG were degraded more rapidly than nondenatured bovine milk β-LG in the small intestine of mice. In terms of undenatured proteins, mouse intestinal tissues absorbed more bovine milk β-LG than caprine milk β-LG. Overall, structural disparities in β-LG between bovine and caprine milk resulted in varying digestion rates. Moreover, the slower-degraded bovine milk β-LG and its enzymatic fragments facilitated easier absorption by the intestine, disrupting the Th1/Th2 balance and increasing susceptibility to severe allergic reactions in mice.