2019
DOI: 10.1016/j.foodchem.2018.08.138
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Matrix effect on food allergen detection – A case study of fish parvalbumin

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Cited by 23 publications
(20 citation statements)
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“…From the dot blot ( Figure 1 ), three major findings were obtained. First, salmon parvalbumin immunoreactivity increased when 10 mM EDTA or 10 mM EGTA was incubated with purified salmon parvalbumin ( Figure 1 A), which matched our previous findings [ 23 ]. Additionally, Gajewski and Hsieh [ 79 ] reported an increase in mAb PARV19 immunoreactivity with calcium-depleted fish protein extracts.…”
Section: Fish Allergy and Allergenssupporting
confidence: 91%
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“…From the dot blot ( Figure 1 ), three major findings were obtained. First, salmon parvalbumin immunoreactivity increased when 10 mM EDTA or 10 mM EGTA was incubated with purified salmon parvalbumin ( Figure 1 A), which matched our previous findings [ 23 ]. Additionally, Gajewski and Hsieh [ 79 ] reported an increase in mAb PARV19 immunoreactivity with calcium-depleted fish protein extracts.…”
Section: Fish Allergy and Allergenssupporting
confidence: 91%
“…Griesmeier et al [ 88 ] reported IgE binding to heated (100 °C/10 min) whiff proteins even after in vitro pepsin digestion for 120 min while the IgE binding to heated whiff parvalbumin monomer disappeared after a 5 s digestion. Keshavarz et al [ 23 ] noticed parvalbumin was almost undetectable in heated (100 °C/8 min) salmon protein extracts, while purified salmon parvalbumin was thermostable and soluble after the same heat treatment.…”
Section: Effect Of Processing On Fish Allergensmentioning
confidence: 99%
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