Effect of heat treatment and enzymatic digestion on the B cell epitopes of cow's milk proteins

Morisawa, Yutaka; Kitamura, Akihide; Ujihara, Takako; Zushi, N; Kuzume, Kazuyo; Shimanouchi, Yasuhiro; Tamura, Sakiko; Wakiguchi, Hiroshi; Saito, Hirohisa; Matsumoto, Kenji

doi:10.1111/j.1365-2222.2009.03203.x

Cited by 48 publications

(36 citation statements)

References 52 publications

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“…Untreated and heat treated b-Lg samples were partially resistant to pepsin, as shown in their electrophoretic and chromatographic patterns, confirming the results of previous studies (Herman et al, 2007;Mandalari et al, 2009;Morisawa et al, 2009). According to Morisawa et al (2009), b-Lg is partially resistant to pepsin when heat treated at up to 80 C and is almost totally digested when treated at temperatures above 100 C. The polymerization with TG modified the resistance to pepsin: the heat treated and polymerized samples were partially resistant to the enzyme, whereas the samples treated with 0.25 mol L À1 Cys polymerized with 10 U TG g À1 , was digested by pepsin.…”

Section: Discussionsupporting

confidence: 91%

“…According to Morisawa et al (2009), b-Lg is partially resistant to pepsin when heat treated at up to 80 C and is almost totally digested when treated at temperatures above 100 C. The polymerization with TG modified the resistance to pepsin: the heat treated and polymerized samples were partially resistant to the enzyme, whereas the samples treated with 0.25 mol L À1 Cys polymerized with 10 U TG g À1 , was digested by pepsin. Such results confirmed that these treatments modified the protein structure, since the access of pepsin to the cleavage sites was modified.…”

Section: Discussionmentioning

confidence: 98%

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Effect of polymerization with transglutaminase on in vitro digestion and antigenicity of β-lactoglobulin

Villas-Boas

Fernandes

Zollner

et al. 2012

International Dairy Journal

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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 98%

Effect of polymerization with transglutaminase on in vitro digestion and antigenicity of β-lactoglobulin

Villas-Boas

Fernandes

Zollner

et al. 2012

International Dairy Journal

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“…In fact, most of the studies aiming at analyzing the relationship between structure and allergenicity, and particularly the effect of processing on allergenicity of food proteins, generally use very few individual sera from allergic patients [18], [23], [30], [31], even sometimes only one pool of such sera is available [11], [19], [32], [33]. In the present study, a large population of peanut allergic patients from various European countries was involved leading to significant conclusions.…”

Section: Discussionmentioning

confidence: 80%

Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut

Vissers

Blanc

Skov³

et al. 2011

PLoS ONE

110

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BackgroundPeanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from peanut.Methodology/Principal FindingsNative Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in the presence or absence of glucose. Ara h 2 and 6 were also purified from roasted peanut. Using PBMC and sera from peanut-allergic patients, the cellular proliferative potency and IgE reactivity (reverse EAST inhibition) and functionality (basophil degranulation capacity) of allergens were assessed. Heating Ara h 2/6 at 110°C resulted in extensive denaturation, hydrolysis and aggregation of the protein, whilst Ara h 2 and 6 isolated from roasted peanut retained its native conformation. Allergen stimulation of PBMC induced proliferation and Th2 cytokine secretion which was unaffected by thermal processing. Conversely, IgE reactivity and functionality of Ara h 2/6 was decreased by heating. Whilst heating-glycation further reduced the IgE binding capacity of the proteins, it moderated their loss of histamine releasing capacity. Ara h 2 and 6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6.Conclusions/SignificanceAlthough no effect of processing on T-cell reactivity was observed, heat induced denaturation reduced the IgE reactivity and subsequent functionality of Ara h 2/6. Conversely, Ara h 2 and 6 purified from roasted peanut retained the structure and IgE reactivity/functionality of the native protein which may explain the allergenic potency of this protein. Through detailed molecular study and allergenicity assessment approaches, this work then gives new insights into the effect of thermal processing on structure/allergenicity of peanut proteins.

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“…11−13 However, while pepsin stability as a part of an allergenicity assessment would still seem reasonable for the purpose of safety evaluation of most food proteins, we now know that for some allergenic proteins, this approach would be misleading. The milk allergen β-casein (Bos d 8) 7,14,15 as well as the peanut allergen Ara h 1 9,10 have several times been shown to be easily digestible food allergens.…”

Section: ■ Introductionmentioning

confidence: 99%

Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions

Bøgh

Barkholt²,

Rigby

et al. 2012

J. Agric. Food Chem.

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The major peanut allergen Ara h 1 is an easily digestible protein under physiological conditions. The present study revealed that pepsin digestion products of Ara h 1 retained the sensitizing potential in a Brown Norway rat model, while this sensitizing capacity was lost by separating the digest into fractions by gel permeation chromatography. Protein chemical analysis showed that the peptide composition as well as the aggregation profiles of the fractions of Ara h 1 digest differed from that of the whole pool. These results indicate that the sensitizing capacity of digested Ara h 1 is a consequence of the peptides being in an aggregated state resembling the intact molecule or that most peptides of the digests need to be present in the same solution, having a synergistic or adjuvant effect and thereby augmenting the immune response against other peptides.

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Effect of heat treatment and enzymatic digestion on the B cell epitopes of cow's milk proteins

Abstract: Heat treatment reduced the allergenicity of beta-lactoglobulin by inducing conformational changes and by increasing its susceptibility to enzymatic digestion, both of which disrupted B cell epitopes, whereas heat treatment alone did not alter the allergenicity of alpha-casein.

Cited by 48 publications

References 52 publications

Effect of polymerization with transglutaminase on in vitro digestion and antigenicity of β-lactoglobulin

Effect of polymerization with transglutaminase on in vitro digestion and antigenicity of β-lactoglobulin

Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut

Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions

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