Development of a liquid chromatography-tandem mass spectrometry method for simultaneous quantification of hen’s egg white allergens Gal d 1–4 in fresh and processed eggs

Kiyota, Kyohei; Yoshimitsu, Masato; Uchida, Kôtarô; Kajimura, K.

doi:10.1016/j.foodchem.2020.128022

Cited by 12 publications

(3 citation statements)

References 28 publications

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“…Through our systematic comparison, it became evident that the peptide VLPVPQK derived from β-casein exhibited the best sensitivity and accuracy, thus becoming the chosen quantitative peptide for milk. As for egg allergen analysis, ovalbumin (Gal d 2) constitutes over 50% of the total egg protein, making it a frequent target for quantitative analysis in most reported methods . However, we observed that ovalbumin exhibits poor thermal stability, leading to lower accuracy in quantitative analysis results.…”

Section: Resultsmentioning

confidence: 83%

“…As for egg allergen analysis, ovalbumin (Gal d 2) constitutes over 50% of the total egg protein, making it a frequent target for quantitative analysis in most reported methods. 41 However, we observed that ovalbumin exhibits poor thermal stability, leading to lower accuracy in quantitative analysis results. Consequently, we explored an alternative, and the peptide VMVLC[+57]NR derived from ovomucoid (Gal d 1) showed superior sensitivity and accuracy in our study, becoming the selected quantitative peptide for egg allergen analysis.…”

Section: Theoretical Basis Of Osccmentioning

confidence: 78%

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Advancing High-Throughput MS-Based Protein Quantification: A Case Study on Quantifying 10 Major Food Allergens by LC-MS/MS Using a One-Sample Multipoint External Calibration Curve

Yang,

Lin,

Yang

et al. 2024

J. Agric. Food Chem.

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The LC-MS-based method has emerged as the preferred approach for quantifying food allergens. However, the preparation of a traditional calibration curve (MSCC) is labor-intensive and error-prone. Here, a sensitive and robust LC-MS/MS method for quantifying 10 major food allergens was developed and validated, where the one-sample multipoint external calibration curve (OSCC) was employed instead of MSCC. By employing the multiple isotopologue reaction monitoring (MIRM) technique with only one spiked level in the blank, OSCC can be effectively established. Results demonstrate that the proposed method exhibits excellent performance in selectivity, sensitivity, accuracy, and precision, comparable to that of the traditional MSCC. Additionally, this strategy allows for isotope sample dilution by monitoring the less abundant MIRM channel. Moreover, the developed method was successfully applied to investigate the contamination of 10 food allergens in commercial food products. With its high throughput and robustness, the MIRM-OSCC-LC-MS/MS methodology has many potential applications, especially in the MS-based protein quantification analysis.

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Section: Resultsmentioning

confidence: 83%

Section: Theoretical Basis Of Osccmentioning

confidence: 78%

Advancing High-Throughput MS-Based Protein Quantification: A Case Study on Quantifying 10 Major Food Allergens by LC-MS/MS Using a One-Sample Multipoint External Calibration Curve

Yang,

Lin,

Yang

et al. 2024

J. Agric. Food Chem.

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“…The plant protein beverages were prepared according to the previous reports with minor modification [17][18][19][20]. Shelled plant protein materials were separately ground in 70 mL water for 3 min by a grinder, followed by heating at 85 ℃ for 15 min to inactivate enzymes.…”

Section: Preparation Of the Plant Protein Beveragesmentioning

confidence: 99%

Adulteration detection of plant protein beverages by UPLC-MS/MS based on signature peptide of allergen

Ning,

Liu,

Yang

et al. 2024

Food Science and Human Wellness

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Plant protein beverage adulteration occurs frequently, which may cause health problems for consumers due to the hidden allergens. Hence, a novel method was developed for authentication by UPLC-MS/MS. Almond, peanut, walnut and soybean were hydrolyzed, followed by separation by NanoLC-Triple TOF MS. The obtained fingerprints were identified by ProteinPilot TM combined with Uniprot, and 16 signature peptides were selected. Afterwards, plant protein beverages treated by trypsin hydrolysis were analyzed with UPLC-MS/MS. This method showed a good linear relationship with R 2 > 0.99403. The LOQs were 0.015, 0.01, 0.5 and 0.05 g/L for almond, peanut, walnut and soybean, respectively. Mean recoveries ranged from 84.77% to 110.44% with RSDs < 15%. The developed method was successfully applied to the adulteration detection of 31 plant protein beverages to reveal adulteration and false labeling. Conclusively, this method could provide technical support for authentication of plant protein beverages to protect the rights and health of consumers.

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Determination of degradation degree of ovalbumin in hen’s egg enzymatic hydrolysates using liquid chromatography–tandem mass spectrometry

Kiyota

Yoshimitsu²,

Matsui³

2022

Food Measure

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Development of a liquid chromatography-tandem mass spectrometry method for simultaneous quantification of hen’s egg white allergens Gal d 1–4 in fresh and processed eggs

Cited by 12 publications

References 28 publications

Advancing High-Throughput MS-Based Protein Quantification: A Case Study on Quantifying 10 Major Food Allergens by LC-MS/MS Using a One-Sample Multipoint External Calibration Curve

Advancing High-Throughput MS-Based Protein Quantification: A Case Study on Quantifying 10 Major Food Allergens by LC-MS/MS Using a One-Sample Multipoint External Calibration Curve

Adulteration detection of plant protein beverages by UPLC-MS/MS based on signature peptide of allergen

Determination of degradation degree of ovalbumin in hen’s egg enzymatic hydrolysates using liquid chromatography–tandem mass spectrometry

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