Digestion-Resistant Linear Epitopes as Dominant Contributors to Strong Allergenicity of Tropomyosin in Antarctic Krill (<i>Euphausia superba</i>)

Wang, Shan; Lin, Songyi; Liu, Kexin; Liu, Yao; Liu, Qiaozhen; Sun, Na

doi:10.1021/acs.jafc.3c04999

Cited by 11 publications

(3 citation statements)

References 58 publications

(134 reference statements)

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“…Using bioinformatic tools to predict linear epitopes of FSG, DNAStar protean and Antheprot software used hydrophilicity, flexibility, surface accessibility, and antigenicity index as prediction criteria for candidate allergenic epitopes and the results were displayed in Table S2 and Figures S2c–10c. BepiPred 1.0 server, ABCpred server, and Immunomedicine Group tool were used to analyze potential allergenic epitopes based on amino acid secondary structure, hydrophilicity, accessibility, flexibility, and so on.…”

Section: Resultsmentioning

confidence: 99%

“…Digestion-Resistant Linear Epitopes Analysis and Mapping of the Major Allergen of FSG. Using bioinformatic tools to predict linear epitopes of FSG, DNAStar protean and Antheprot software used hydrophilicity, flexibility, surface accessibility, and antigenicity index as prediction criteria for candidate allergenic epitopes 46 and the results were displayed in Table S2 and Figures flexibility, and so on. As prediction using a single tool has limitations, overlapping epitopes predicted by more than three kinds of tools were used as linear epitopes of allergens.…”

Section: ■ Introductionmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

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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“…Determination of Surface Hydrophobicity. Surface hydrophobicity of instant soy milk powder and the enzymatic hydrolysate was carried out according to the description of Wang et al 27 The relative fluorescence intensities of the gradient-diluted test samples (0.05, 0.10, 0.15, 0.2, and 0.25 mg/mL) reacted with 8-aniline-1-naphthalene sulfonic acid were plotted on the linear curves, and the slopes of the curves were considered to be the surface hydrophobicity of the test samples (H0).…”

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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Non-Thermal Processing Technologies for Allergen Control in Alternative Protein Sources for Food Industry Applications

Dong,

Hinds,

Soro

et al. 2024

Food Eng Rev

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Sustainable food practices within the food industry are pertinent to allow efficient food supply while not negatively impacting the environment. Alternative proteins have gained the attention of the food industry and consumers. To provide safe novel food products, these protein sources need to be assessed for potential allergen risk to ensure food safety and allow effective labelling to protect the consumer. In this review, the various detection assays applied to target potential allergens in novel and alternative foods are described together with their applications, mechanisms and limitations. Additionally, the use of non-thermal technologies to mitigate the reactivity of food allergens in these new products is explored. Non-thermal techniques including cold plasma, pulsed electric field, ultrasound and gamma irradiation are discussed. This review examines the potential mechanisms by which non-thermal technologies may reduce food allergenicity, primarily through alterations in protein epitopes that could affect antibody recognition. However, it is important to note that the understanding of the precise mechanisms and outcomes in allergen mitigation through these methods remains an area requiring further research.

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Digestion-Resistant Linear Epitopes as Dominant Contributors to Strong Allergenicity of Tropomyosin in Antarctic Krill (Euphausia superba)

Cited by 11 publications

References 58 publications

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

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

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

Non-Thermal Processing Technologies for Allergen Control in Alternative Protein Sources for Food Industry Applications

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