The evaluation of antigenic reactivity of cow's milk proteins treated with non-commercial enzyme preparations of microbial and plant origin

<p class="MsoNormal" style="text-align:justify;line-height:200%"><span style="font-size:10px"><span style="font-family:&#39;times new roman&#39; , &#39;times&#39; , serif">Allergy to cow&#39;s milk
protein (CMPA) is commonly diagnosed in 1–17.5 %
of infants
and children under age of 5 years, among 1–13.5 % of teenagers and also among
about 0.5-2.4 % of adults. Cow milk contains at least 20 potentially allergenic
proteins, among which casein (CN), serum proteins, β-lactoglobulin (BLG), and ɑ-lactalbumin
(ALA) have been identified as the main allergens recognized by human IgE. In most cases, children
with milk allergies are sensitized to more than one allergen. In the processing
of milk and manufacturing of dairy products, various methods are
applied to reduce the allergenicity of CMP, such as thermal (dry heating,
boiling, or cooking), biochemical,
and chemical processes (enzymatic digestion). To reduce allergenicity, proteins
can be broken down into smaller peptides and amino acids by enzyme hydrolysis. </span><span lang="EN-US" style="line-height:107%;font-family:&#39;times new roman&#39; , serif">The aim of the study was to investigate the use
of two different origin serine proteases isolated from </span><em style="font-size:10px"><span lang="EN-GB" style="line-height:107%;font-family:&#39;times new roman&#39; , serif">Cucurbita</span><span lang="EN-US" style="line-height:107%;font-family:&#39;times new roman&#39; , serif"> ficifolia</span></em></span><span lang="EN-US" style="line-height:107%;font-family:&#39;times new roman&#39; , serif;font-size:11pt"><span style="font-size:10px"> (Asian pumpkin) and
secreted from <em>Yarrowia lipolytica</em>
yeast for reduction the milk protein allergenicity. Analyzed enzymes were
introduced in a sequence, in both combinations, and simultaneously.  </span></span><span style="font-size:10px"><span lang="EN-US" style="letter-spacing:0px;font-family:&#39;times new roman&#39; , serif;color:rgb( 31 , 31 , 31 )">These results demonstrate the potential of enzyme combinations to
enhance the efficiency of epitope destruction in allergenic proteins, providing
valuable insights into the development of hypoallergenic </span><span lang="EN-GB" style="letter-spacing:0px;font-family:&#39;times new roman&#39; , serif"><a href="https://www.sciencedirect.com/topics/food-science/dairy-product" rel="nofollow"><span lang="EN-US" style="color:rgb( 31 , 31 , 31 )">dairy products</span></a></span></span><span lang="EN-US" style="letter-spacing:0px;font-family:&#39;times new roman&#39; , serif;color:rgb( 31 , 31 , 31 );font-size:10px">.</span></p><p class="MsoNormal" style="text-align:justify;line-height:150%"><span lang="EN-US" style="font-family:&#39;times new roman&#39; , serif"></span><br /></p><p><br /></p>