hydrolysaten

Hydrolysaten, commonly termed hydrolysates in English, are products formed by hydrolysis, a process that cleaves chemical bonds in molecules with the addition of water. In food science and nutrition, the term often refers to protein hydrolysates—proteins that have been partially or fully broken down into shorter peptides and free amino acids. Carbohydrate hydrolysates, produced by breaking down starches or other carbohydrates, yield mixtures of sugars and oligosaccharides. Hydrolysaten are valued for improved digestibility, altered functional properties, and specific nutritional or flavor characteristics.

Production methods vary. Enzymatic hydrolysis uses proteases or carbohydrases under controlled pH and temperature to target specific bonds. Chemical hydrolysis employs acid or base at high temperature. After hydrolysis, purification steps such as filtration, ultrafiltration, chromatography, and drying remove enzymes, salts, and unwanted components and help achieve a desired degree of hydrolysis and peptide profile. The degree of hydrolysis (DH) indicates the extent of bond cleavage and strongly affects solubility, viscosity, taste, and allergenicity.

Protein hydrolysates are widely used in infant formulas, clinical and medical nutrition for patients with malabsorption or special dietary needs, and in sports nutrition as easily digestible protein sources. They also serve as flavor enhancers or texture modifiers in various foods. High-DH hydrolysates tend to be rich in free amino acids, while low-DH products contain more peptides; taste can range from mild to bitter depending on DH and peptide composition.

Safety and regulation: hydrolysaten derived from common dietary proteins are generally considered safe when produced under good manufacturing practices. Allergen labeling remains important, as some hydrolysates may still contain allergenic epitopes or cross-reactive peptides. Manufacturers often specify intended use, DH, and peptide profile on labeling.