Regulation of action sites for reducing the allergenicity of pea protein based on enzymatic hydrolysis with Alcalase

Ding, Jie; Liu, Dong; Jiang, Pengfei; Tang, Yue; Lin, Songyi

doi:10.1016/j.foodchem.2022.133930

Cited by 13 publications

(12 citation statements)

References 34 publications

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“…Meinlschmidt et al found that high-pressure processing promoted the hydrolysis of the soy protein isolate by flavor protease and destroyed the linear epitopes of the allergen β-conglycinin, thereby reducing its allergenicity . Ding et al reported that alcalase hydrolysis significantly reduced the allergenicity of pea protein by destroying its allergic epitopes, l -vicilin hydrolysates and H-vicilin hydrolysates …”

Section: Resultsmentioning

confidence: 99%

“…16 Ding et al reported that alcalase hydrolysis significantly reduced the allergenicity of pea protein by destroying its allergic epitopes, L-vicilin hydrolysates and Hvicilin hydrolysates. 40 In summary, we studied the effects of spatial conformation changes and antigenic epitopes on the binding levels of OVM…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…The specific IgE and IgG1 binding levels of OVM and its hydrolysates were determined by ELISA. As per the method described by Li et al 17 and Ding et al, 23 the samples of OVM, HOVM, HOVM-P, HOVM-P′, and HOVM-PP′ were diluted to a concentration of 0.1 mg/mL and then coated on 96-well plates overnight to detect the binding levels of IgE and IgG1. Briefly, overnight samples were incubated with a phosphate-buffered saline (PBS)/1% BSA solution at 37 °C for 60 min.…”

Section: Materials Andmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Section: Materials Andmentioning

confidence: 99%

See 1 more Smart Citation

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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“…It indicated that enzymatic hydrolysis treatment could decrease total IgE and IgG1 secretion levels caused by allergic reactions. Specific IgE and IgG1 were frequently used as diagnostic methods because they had specific binding receptors that triggered clinical reactions to food allergies. , As displayed in Figure C,D, the binding capacities of specific IgE and IgG1 in the serum of mice in the ISP, ISPH, and CASP groups were significantly strengthened compared to the BC group ( P < 0.05), which increased by 129.71 and 226.89%, 75.64 and 183.62%, 78.88 and 180.26%, respectively. Compared to the ISP group, the ISPH and CASP groups showed significantly weak binding abilities to specific IgE and IgG1 in the serum of mice ( P < 0.05), which were reduced by 28.00 and 25.73%, 24.46 and 20.60%, respectively, and there was no significant difference between the two groups ( P > 0.05).…”

Section: Resultsmentioning

confidence: 96%

“…According to previous reports, the allergenicity of allergenic proteins treated with enzymatic hydrolysis (e.g., pea proteins, cow’s milk proteins, egg white proteins, wheat gluten proteins, soy proteins, sea bream albumin, Antarctic krill proteins, blue whiting proteins, etc.) was reduced . Among them, Alcalase is more effective in reducing the allergenicity of proteins. − Enzymatic hydrolysis, as a biological desensitization technology to reduce allergen sensitization, is advantageous because of its high efficiency, mild conditions, easy control, no side effects, energy savings, etc.…”

Section: Introductionmentioning

confidence: 99%

Dual Action of Reduced Allergenicity and Improved Memory of Instant Soybean Powder Hydrolysates

Ding,

Huang,

Yang

et al. 2023

J. Agric. Food Chem.

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Debittering and antioxidant improvement of soy protein hydrolysates using curcumin as hydrophobic core

Chen,

Wei,

Hou

et al. 2024

J Sci Food Agric

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BACKGROUNDProtein hydrolysates possess various bioactive functions (e.g. antioxidant), but their bitter taste is unacceptable to most consumers. In the present study, a novel approach for debittering was introduced, which involved the utilization of a hydrophobic compound, curcumin (Cur). Soy protein hydrolysates (SPH), prepared through alcalase hydrolysis, served as the research model for this investigation.RESULTSIt was found that bitter intensity of SPH was dominated by the hydrophobic amino acid residues, and the addition of Cur could remarkably reduce bitterness. The debittering mechanism is attributed to the direct binding of Cur to the exposed hydrophobic amino acid residues of SPH via hydrophobic interaction, thereby shielding the hydrophobic bitter groups and hindering their interaction with the bitter taste receptors. Moreover, this debittering strategy leads to the generation of stable nanoparticles with a Cur‐core/SPH‐shell architecture, which can significantly improve the antioxidant capacity of SPH compared to those using biomacromolecules for encapsulation.CONCLUSIONUsing curcumin as a hydrophobic core is a facile and feasible strategy with bifunction of debittering as well as improving bioactive effect of SPH, which may extend its application in foods. © 2024 Society of Chemical Industry.

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Regulation of action sites for reducing the allergenicity of pea protein based on enzymatic hydrolysis with Alcalase

Cited by 13 publications

References 34 publications

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

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

Dual Action of Reduced Allergenicity and Improved Memory of Instant Soybean Powder Hydrolysates

Debittering and antioxidant improvement of soy protein hydrolysates using curcumin as hydrophobic core

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