(2015) succeeded in developing a concept for the development of solvent systems, enabling intact proteins to be analyzed by HPTLC and providing a basis for the development of specific detections . as short peptide fragments that provide epitopes. The desire to make food safer for allergy sufferers and to protect sensitized individuals from an allergenic reaction makes it clear that the detection of food antigens is mandatory; especially by considering protein interactions. plants such as broccoli, cauliflower, brussels Linagliptin (BI-1356) sprouts, and cabbage and are associated with various health-promoting properties (e.g., antibacterial, anti-inflammatory, and antidiabetogenic activity) [2,4,6,12,13,14,15,16]. Due to their functional group, isothiocyanates possess a high electrophilicity at the carbon atom, which makes a reaction with nucleophiles conceivable. The electrophilic center of ITC reacts with thiol and amino groups in the side chains of proteins to form thiocarbamates and thioureas [17,18,19]. Keppler et al. (2017) showed that covalent conjugation of allyl isothiocyanate (being a degradation of the glucosinolate sinigrin) to a whey protein isolate significantly affected the physicochemical properties such as charge, aggregation, surface hydrophobicity, and secondary structural features of the protein, depending on pH value . It was also shown that a modification of these proteins with allyl isothiocyanate had no significant effect on the antibacterial activity of this protein against different strains of and . The reason for an intensified research on whey proteins is because of their very high nutritional quality, being due to their high content of branched, sulfur-containing, and essential amino acids in an advantageous composition. Besides their high biological value, whey proteins are characterized by their extraordinary functional properties and their solubility over a wide pH value Linagliptin (BI-1356) range, making them valuable food ingredients [3,20,21,22,23]. Whey proteins include various albumins and globulins, among which -lactalbumin (-LA) TNFSF10 is the second most common protein in cows milk, accounting for 2C5% . -LA is a small, acidic protein, consisting of 123 amino acids and a molecular weight of 14.2 kDa. In addition, it is an important Ca2+-binding model protein and a classic example of the molten globule state. It is a component of lactose synthase [20,24]. For example, -LA and its hydrolysates have been found to have an antihypertensive effect in hypertension , to contribute to stress reduction , and to regulate cell growth . It further provides antimicrobial  and immunostimulatory properties . Besides to the positive properties of -LA, it is one of the main allergens in cows milk, along with -LG and casein . In general, food allergies are mostly type 1 (immediate-type) allergies that are mediated by specific IgE antibodies bound on mast cells. Binding of the antibody to the antigen activates the mast cells and stimulates them to degranulate. There is a release of histamine and a number of other mediators of allergic inflammation . Type I allergenicity of the immediate reaction is a particular immunogenicity. While immunogenicity describes the ability to induce a humoral or cellular immune response, antigenicity describes the ability to be specifically recognized by antibodies produced as a result of an immune response to the given substance or molecule . A substance that is recognized by the organism as an antigen is capable of eliciting an immune response and therefore has an immunogenic potential, the extent of which depends, among other things, on the molecular size and chemical structure. In the literature it is described that immunogenic substances usually must have a molecular weight higher than 5000 Daltons and contain antigenic regions in the secondary and tertiary structure, so-called epitopes. Generally, various proteins in food can therefore have an allergenic potential, because the epitopes can be specifically recognized by antibodies and subsequently trigger an allergic reaction. The extent of immunogenicity depends on the abundance and density of the epitopes. These epitope structures of proteins can be formed as linear (sequential and continuous) or conformational (discontinuous) epitopes [33,34,35,36,37]. The latter are formed by the folding of spatial structures such as the secondary or tertiary conformational arrangements, while sequential epitopes are short sections of the primary structure of proteins [31,38]. Despite cows milk being a valuable food source for humans and especially for infants, these food allergens can cause allergic reactions in sensitive people. However, Linagliptin (BI-1356) there is a growing desire to make food safer for allergic sufferers and to further investigate the problem of milk.