Allergenicity evaluation of five types of commercial food-derived oligopeptide products

Che, Huilian; Zhang, Qiuyu; Wang, Junjuan; Hao, Mengzhen; Zeng, Binghui; Che, Huilian

doi:10.1039/d2fo02825e

Cited by 4 publications

(3 citation statements)

References 42 publications

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“…Food allergy is a worldwide food safety and public health problem, and food allergens, mostly proteins, are capable of inducing allergic reactions mediated by immunological mechanisms in the body after exposure. , Currently, the World Health Organization (WHO) has recognized more than about 390 food allergens . And the relevant statistics show that the number of food allergy sufferers is increasing, with a prevalence rate of up to 10% .…”

Section: Introductionmentioning

confidence: 99%

Conformation-Activity Mechanism of Alcalase Hydrolysis for Reducing In Vitro Allergenicity of Instant Soy Milk Powder

Ding,

Qi,

Zhong

et al. 2024

J. Agric. Food Chem.

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Effective reduction of the allergenicity of instant soy milk powder (ISMP) is practically valuable for expanding its applications. This study optimized the enzymolysis technology of ISMP using single-factor experiments and response surface methodology, combined serological analysis, cellular immunological models, bioinformatics tools, and multiple spectroscopy techniques to investigate the effects of alcalase hydrolysis on allergenicity, spatial conformation, and linear epitopes of ISMP. Under the optimal process, special IgE and IgG1 binding abilities and allergenic activity to induce cell degranulation of alcalase-hydrolyzed ISMP were reduced by (64.72 ± 1.76)%, (56.79 ± 3.72)%, and (73.3 ± 1.19)%, respectively (P < 0.05). Moreover, the spatial conformation of instant soy milk powder hydrolysates (ISMPH) changed, including decreased surface hydrophobicity, a weaker peak of amide II band, lower contents of α-helix and β-sheet, and an enhanced content of random coil. Furthermore, the linear epitopes of major soy allergens, 9 from glycinin and 13 from β-conglycinin, could be directionally disrupted by alcalase hydrolysis. Overall, the structure−activity mechanism of alcalase hydrolysis to reduce ISMP allergenicity in vitro was preliminarily clarified. It provided a new research direction for the breakthrough in the desensitization of ISMP and a theoretical basis for revealing the potential mechanism of alcalase enzymolysis to reduce the allergenicity of ISMP.

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Section: Introductionmentioning

confidence: 99%

Conformation-Activity Mechanism of Alcalase Hydrolysis for Reducing In Vitro Allergenicity of Instant Soy Milk Powder

Ding,

Qi,

Zhong

et al. 2024

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…Specific Antibody Levels. Serum levels of IgE were characterized as modified by Xiong et al 19 The OD values were read immediately at diluted by sealing liquid at a ratio of 1:10. 100 μL of biotin-labeled rat anti-mouse IgE (1:1000) (Abcam, Cambridge, U.K.) and HRP (1:2000) were added to each well.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Specific Antibody Levels. Serum levels of IgE were characterized as modified by Xiong et al 19 The OD values were read immediately at 450 nm. The modifications were made as follows: the serum was diluted by sealing liquid at a ratio of 1:10.…”

Section: ■ Introductionmentioning

confidence: 99%

Investigation into Potential Allergenicity and Digestion-Resistant Linear Epitopes of Fish Skin Gelatin in Cell-Cultured Meat Scaffolds

Wang,

Lin,

Liu

et al. 2024

J. Agric. Food Chem.

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As a key component of cell-cultured fish, fish skin gelatin (FSG)-based cell scaffold provides support structures for cell growth, proliferation, and differentiation. However, there are potential allergenicity risks contained in FSG-based scaffolds. In this study, 3D edible scaffolds were prepared by phase separation method and showed a contact angle of less than 90°, which indicated that the scaffolds were favorable for cell adhesion. Besides, the swelling ratio was greater than 200%, implying a great potential to support cell growth. The sequence homology analysis indicated that FSG was prone to cross-reaction with collagen analogues. Additionally, a food allergic model was constructed and represented that mice gavaged with cod FSG exhibited higher levels of specific antibodies, mast cell degranulation, vascular permeability, and intestinal barrier impairment than those gavaged with pangasius and tilapias FSG. Its higher allergenicity might be attributed to a higher number of digestion-resistant linear epitopes. Moreover, the higher hydrolysis degree linked to the exposure of linear epitopes to promote the combination with IgE, which was also responsible for maintaining the higher allergenicity of cod FSG. This study clarifies allergenic risks in cell-cultured fish and further study will focus on the allergenicity reduction of FSG-based cell scaffolds.

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Identification and molecular docking of novel antioxidant peptides from Candida utilis

Wei,

Wang,

et al. 2024

Food Chemistry

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Allergenicity evaluation of five types of commercial food-derived oligopeptide products

Abstract: Though derived from allergic food, oligopeptide products have low allergenicity and may be exempted from allergen labeling if the industrial production conditions are well controlled.

Cited by 4 publications

References 42 publications

Conformation-Activity Mechanism of Alcalase Hydrolysis for Reducing In Vitro Allergenicity of Instant Soy Milk Powder

Conformation-Activity Mechanism of Alcalase Hydrolysis for Reducing In Vitro Allergenicity of Instant Soy Milk Powder

Investigation into Potential Allergenicity and Digestion-Resistant Linear Epitopes of Fish Skin Gelatin in Cell-Cultured Meat Scaffolds

Identification and molecular docking of novel antioxidant peptides from Candida utilis

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