Abstract #438

# 438
Relationships between structures of dairy-based matrices and digestibility within the gastrointestinal tract.
A. Brodkorb*1, 1Teagasc Food Research Centre Moorepark, Fermoy, Co. Cork, Ireland.

Milk proteins are the main structural components of dairy and dairy-containing foods. Their molecular structure and aggregation behavior can be tuned by targeted, “smart” processing. Whey proteins, previously considered a low-value by-product from cheese production, exhibit a globular molecular structure, and are prone to unfolding and self-aggregation or association with caseins or casein micelles. This can be either detrimental or advantageous for food processing. In this talk, several examples are given on how to understand, control and modify the structure of milk proteins, thereby adding value. Rapid pilot scale, pre-heat treatments of whey proteins can improve the standard processability and/or efficiency of the enzymatic hydrolysis of protein products. This will benefit down-stream production of nutritional products such as infant formula, sports nutrition, and nutrition for the elderly. Changes in processing conditions can also affect the gastro-intestinal transit of dairy proteins and accelerate or delay the bioaccessibility of nutrients, as demonstrated by static (Brodkorb et al., Nature Protocols 2019) or semi-dynamic in vitro digestion methods (Mulet-Cabero et al., Food Hydrocolloids, 2018). In particular, heat treatment and homogenization can have a profound effect on the mechanism and kinetics of in vitro and in vivo gastro-intestinal digestion of dairy proteins, due to gastric restructuring. Dairy proteins can also act as carriers for labile, bioactive components of food to protect or encapsulate them during food production, storage or the harsh environment of the gastrointestinal tract (in vivo and in vitro, Doherty et al., International Dairy Journal 2012).