Extensively hydrolysed sodium caseinate. Part I: Selection of enzymes, molecular mass distribution, and allergy site analysis by liquid chromatography-mass spectrometry

Qin, Airong; Li, Xiaoyao; Yang, Feifei; Yang, Jingjing; Li, Hongbo; Li, Hongjuan; Yu, Jinghua

doi:10.1016/j.idairyj.2022.105501

Cited by 7 publications

(6 citation statements)

References 45 publications

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“…Therefore, both enzymes had catalytic activity at pH 8.5. This was consistent with the optimal pH of casein hydrolysate, which was also compounded by these two enzymes (Qin et al., 2023). In addition, hydrolysis at pH 7.5 and 9 showed also high reactivity to MPC, which further indicated that the complex enzyme exhibited better stability and activity under alkaline conditions (Zhang et al., 2021).…”

Section: Resultssupporting

confidence: 81%

“…The characterization of the MPC hydrolysate met the requirements of extensive hydrolysis. Although there is no direct correlation between MW and antigenicity, more studies have shown that larger MW hydrolysates (>10 kDa) are susceptible to antigenic reactions, whereas lower MWs (<1000 Da) are very unlikely to trigger allergy to cow's milk in infants and children (Qin et al., 2023). For example, α‐lactalbumin and BLG hydrolysates with MW below 4.8 kDa had low immunoreactivity, whereas the reduction in antigenicity is higher than 80% at MW less than 1.5 kDa (Wroblewska et al., 2004; Zhang et al., 2020).…”

Section: Resultsmentioning

confidence: 99%

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Extensive hydrolysis of milk protein and its peptidomic antigenicity analysis by LC–MS/MS

Zhao

Jiang

et al. 2023

Journal of Food Science

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Milk protein concentrate (MPC) is considered an ideal substitute of cow milk because of its similar protein and nutrition. In this study, MPC was hydrolyzed to peptides by alcalase and neutrase, and the properties of hydrolysate were evaluated. When MPC was hydrolyzed at the ratio of alcalase and neutrase of 1:1 and enzyme to substrate ratio of 6000 U/g MPC at 50°C, pH 8.5 for 3 h, the proportion of peptides with molecular weights <1 kDa was 85.31%, and the antigenicity reduction rates of casein and β‐lactoglobulin were 33.76% and 22.38%, respectively. Moreover, LC–MS/MS peptide identification revealed that the alcalase and neutrase disrupted a total of 65 epitopes of casein and 21 epitopes of whey protein, which further elucidated the mechanism of complex enzyme hydrolysis to reduce milk protein allergenicity.

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Section: Resultssupporting

confidence: 81%

Section: Resultsmentioning

confidence: 99%

Extensive hydrolysis of milk protein and its peptidomic antigenicity analysis by LC–MS/MS

Zhao

Jiang

et al. 2023

Journal of Food Science

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“…This indicated that the spatial conformation changes masked the binding site of OVM, which reduced its allergic reaction. Second, the destruction of epitopes was one of the key factors that reduce the binding rate of OVM. , Qin et al reported that casein in milk was hydrolyzed by alcalase and neutrase, and its main allergic sites were hydrolyzed, thereby significantly reducing its allergenicity . Based on the above results, the effects of PEF-assisted alcalase treatment on OVM epitopes were subsequently analyzed using bioinformatics and nano-HPLC MS/MS.…”

Section: Resultsmentioning

confidence: 99%

“…34,35 Qin et al reported that casein in milk was hydrolyzed by alcalase and neutrase, and its main allergic sites were hydrolyzed, thereby significantly reducing its allergenicity. 35 Based on the above results, the effects of PEF-assisted alcalase treatment on OVM epitopes were subsequently analyzed using bioinformatics and nano-HPLC MS/MS.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Pulsed Electric Field-Assisted Alcalase Treatment Reduces the Allergenicity and Eliminates the Antigenic Epitopes of Ovomucoid

Ding

Zhang

et al. 2023

J. Agric. Food Chem.

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Physically assisted chemical modifications can effectively reduce the allergenicity of ovomucoid (OVM). However, only a few studies have used pulsed electric field (PEF)-assisted alcalase hydrolysis to reduce the allergenicity of OVM. Herein, we investigated the effect of PEF-assisted alcalase treatment on the spatial conformation, allergenicity, and antigenic epitopes of OVM based on multispectroscopic analyses, bioinformatics, and mass spectrometry. The results showed that PEF-assisted alcalase treatment promoted the hydrolysis of OVM; moreover, the α-helix content and surface hydrophobicity of OVM significantly decreased, which disordered its spatial conformation and weakened its intermolecular interactions. Additionally, enzyme-linked immunosorbent assay (ELISA) results showed that the PEF-assisted alcalase treatment significantly reduced the binding levels of IgE and IgG1, which were 47.66 and 36.41%, respectively. Finally, eight epitopes of OVM were obtained by immunoinformatic tools. Nano-high performance liquid chromatography coupled to tandem mass spectrometry (nano-HPLC MS/MS) results showed that the hydrolysate of OVM and alcalase (HOVM) had nine more peptide-containing epitopes than the hydrolysate of PEF-treated OVM and PEF-treated alcalase (HOVM-PP′), indicating that PEF could promote the elimination of linear epitopes in OVM, thereby reducing OVM allergenicity.

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“…In the AT group, the allergenicity inhibition rate of CN gradually increased with the increase of hydrolysis time (from 48.14% to 68.25%); no significant differences (p > 0.05) were observed during the following 90 min. Similarly, Qin et al ( 2023) also adopted Alcalase and Neutrase hydrolyzed sodium caseinate to obtain extensive hydrolysis products and found that the allergenicity was reduced to 3.61% (Qin et al, 2023). Generally, with the increasing hydrolysis time, the allergenicity inhibition rate of CN increased gradually in the PT group, reaching a maximum reduction of 50.75%, when the hydrolysis time was 120 min.…”

Section: Ige-binding Abilitymentioning

confidence: 98%

Characterization of the potential allergenicity of enzymatically hydrolyzed casein in Balb/c mouse model

Liang,

Qu,

Gou

et al. 2024

Journal of Food Science

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Bovine casein is a major allergen present in cow milk to induce anaphylaxis. In this study, the potential allergenicity of enzymatically hydrolyzed casein (HC) was evaluated based on in vitro and in vivo. The results showed that Alcalase and Protamex treatment (AT, PT) reduced the potential allergenicity of CN, with the greatest reductions of 68.25% and 50.75%, respectively. In addition, in vivo results showed that HC effectively alleviated allergic response symptoms of Balb/c mice; a significant tendency toward decreased serum IgG1 and mast cell tryptase levels was observed, accompanied by a decrease of Th2‐associated IL‐4, IL‐5, and IL‐13 and an increase of IFN‐γ levels in spleen. Moreover, the inflammation of the lung, jejunum, and ileum was remarkably ameliorated. The findings indicated that HC induced a shift toward Th1 response and maintained the Th1/Th2 immune balance. Importantly, our results provide the basis for the production of hypoallergenic dairy products.

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Extensively hydrolysed sodium caseinate. Part I: Selection of enzymes, molecular mass distribution, and allergy site analysis by liquid chromatography-mass spectrometry

Cited by 7 publications

References 45 publications

Extensive hydrolysis of milk protein and its peptidomic antigenicity analysis by LC–MS/MS

Extensive hydrolysis of milk protein and its peptidomic antigenicity analysis by LC–MS/MS

Pulsed Electric Field-Assisted Alcalase Treatment Reduces the Allergenicity and Eliminates the Antigenic Epitopes of Ovomucoid

Characterization of the potential allergenicity of enzymatically hydrolyzed casein in Balb/c mouse model

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