The mechanism of the reduction in allergenic reactivity of bovine α-lactalbumin induced by glycation, phosphorylation and acetylation

Improved antitumor activity and IgE/IgG–binding ability of α‐Lactalbumin/β‐lactoglobulin induced by ultrasonication prior to binding with oleic acid

“…The increase in the IgE/IgG–binding ability was mainly due to the continuous expansion of the spatial structure of α‐La/β‐Lg caused by OA, which exposed the buried IgE/IgG‐binding epitopes, leading to the increase of IgE/IgG–binding ability. The probable epitopes of α‐La included the peptide 1–16, 7–18, 13–26, 47–58, 51–56, 93–102, and 89–108 as IgE/IgG‐binding epitopes (Liu et al., 2020). The potential β‐Lg allergenic epitopes identified are the fragments 1–8, 9–14, 25–40, 41–60, 78–83, 84–91, 92–100, 102–124, 125–135, and 149–162 of the peptide (Benedé et al., 2014).…”

“…These results showed that hydrogen bonds and hydrophobic interaction were the major driving forces taking part in the formation of α-La/β-Lg-OA. Allergenic epitopes of proteins contains the linear epitopes and conformational epitopes (Vila et al, 2001), the disruption of aller- IgG-binding epitopes (Liu et al, 2020). The potential β-Lg allergenic epitopes identified are the fragments 1-8, 9-14, 25-40, 41-60, 78-83, 84-91, 92-100, 102-124, 125-135, and 149-162 of the peptide (Benedé et al, 2014).…”

Casein Oligochitosan-Glycation by Transglutaminase Enhances the Anti-Inflammatory Potential of Casein Hydrolysates to the Lipopolysaccharide-Stimulated IEC-6 Cells

“…In referring to the protein glycation of the Maillard-type, it was evidenced that this glycation could improve solubility, rheology, emulsification, thermal stability, foaming, and gelation of the treated proteins [ 36 , 37 ], or enhance the anti-bacterial, anti-oxidant, ACE-inhibitory, and anti-inflammatory activities of the peptides [ 38 ]. Unfortunately, a previous study also found that lactose glycation of casein led to lower immune potential for the casein hydrolysates [ 4 ]. TGase can also catalyze the reaction between proteins and amino sugars, causing another reaction type of protein glycation (i.e., protein glycation of TGase-type).…”

“…In addition, chemical modifications of proteins can also impact their digestion or bioactivities. For example, the performed glycation, phosphorylation, and acetylation of bovine α-lactalbumin caused an attenuation of its allergic response [ 4 ], while the used phosphorylation of soy protein isolate (SPI) led to reduced digestion in the intestine [ 5 ]. Moreover, it was reported that the Maillard-type protein glycation could cause the loss of the essential amino acids (e.g., lysine and arginine) in proteins [ 6 ], and resulted in protein digestion in the gastrointestinal tract [ 7 ].…”

Food Allergens and Methods for Producing Hypoallergenic Foods

“…Модификация β-лактоглобулина молока путем гликозилирования галактозой в сочетании с ультразвуковой обработкой сопровождается изменением вторичной и третичной структур белка, что снижает способность связывания с иммуноглобулином Е и G [69]. Модификация α-лактальбумина путем гликозилирования, фосфорилирования и ацетилирования приводит к изменению конформационной структуры белка и снижению аллергенности молочной сыворотки [70]. Модификация аллергенных белков гречихи обыкновенной (Fagopyrum esculentum) полисахаридами арабиногалактаном и ксилоглюканом по реакции Майяра привела к снижению аллергенности этих белков [71].…”