Adjusting Bioactive Functions of Dairy Products via Processing

Abstract

Milk is known for its high nutrient content that helps to maintain important body functions. In this regard, bioactive peptides that are encrypted in milk proteins and get released during processing and/or digestion might play a role. These peptides are able to inhibit enzymes, influence cell growth, or target specific receptors. The peptide profile that arises after protein digestion in the jejunum before the absorption into the blood takes place includes these bioactive peptides. The composition of the peptide profile is influenced strongly via processing and a modification in processing might target specific functionalities. Thermal, chemical, biochemical, and physical treatments affect protein digestion mainly by changing the protein structure for example via denaturation or protease actions. Parameters influencing this are external ones, like the matrix of the product, and internal ones, like specific enzyme deficiencies. However, considering all the important aspects that are involved, there might be the possibility in the future to adjust a bioactive function via processing.

Food-Derived Opioids: Production and the Effects of Opioids on Human Health

“…On the purpose of improving protein digestion and peptide formation, acid hydrolysis is applied to food protein-rich substrate. For cheeses (e.g., Mozzarella), the profile of produced bioactive peptide might be affected from the type of acid used for hydrolysis [52]. Conventional conditions for acid hydrolysis (6 M HCl treatment at 110° C for more than 24 h) can cause the destruction of amino acids (e.g., tryptophan) [53].…”

“…Conventional conditions for acid hydrolysis (6 M HCl treatment at 110° C for more than 24 h) can cause the destruction of amino acids (e.g., tryptophan) [53]. On the other hand, in the food industry, alkali treatment is quite rarely applied for protein hydrolysis because of the loss of protein digestibility [52] and it can reduce arginine, cystine, serine, threonine, lysine, and/or isoleucine content and form unexpected amino acid residual forms such as lanthionine or lysinoalanine. Because of the difficulty of controlling chemical processes and yielding products with modified amino acids, the other treatment methods (enzymatic, fermentation) are preferred in bioactive peptide productions [53].…”