During the transition from milk to solid feed, the digestive system of young pigs is not yet fully developed. At this stage, the provision of highly digestible protein sources is critical, as inadequate protein digestion can disturb gastrointestinal function. Eggs contain high-quality protein, but raw eggs contain natural trypsin inhibitors that interfere with protein digestion. Heat treatments such as pasteurization are often applied to reduce microbial load as well as reduce these antinutritional factors to improve amino acid (AA) digestibility. In this experiment, four egg products were tested: raw egg powder, dry-pasteurized egg powder, liquid-pasteurized egg powder, and trypsin inhibitor-free egg powder. Casein, a milk-derived protein characterized by its high digestibility, was also used. Results demonstrated that all egg products had high digestibility for most AA. However, trypsin inhibitor-free egg had protein and AA digestibility values that were not different from values obtained for casein, whereas other pasteurized egg powders had slightly lower values. These observations demonstrate that targeted removal of trypsin inhibitors is more effective in enhancing AA digestibility than mild thermal processing alone.

Read the full article in the Journal of Animal Science.