Interaction between protein allergens and model gastric emulsions

Burnett, Gary R.; Wickham, Martin; Fillery-Travis, Annette; Robertson, James A.; Belton, Peter; Gilbert, Simon; Tatham, Arthur S.; Shewry, Peter R.; Mills, E.N. Clare

doi:10.1042/bst0300916

Cited by 29 publications

(17 citation statements)

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“…Although, according to Burnett et al (2002), BS exert a solubilising effect, removing proteins adsorbed to emulsions and favouring their resolubilisation in aqueous phases, our results show that it is likely that LYS precipitates in the duodenum at pH values, BS and PC concentrations representative of a fed state and, to a lesser extent, of a fasted state. In fact, when LYS is administered orally to human patients (as used for the treatment of chronic sinusitis and to promote expectoration in the case of respiratory disease), food intake negatively affects the uptake of the enzyme, with the maximum levels detected being almost 10-fold lower than those after an identical dose taken after an overnight fast (Hashida, Ishikawa, Nakamichi, & Sekino, 2002).…”

Section: Effect Of the Presence Of Bs And Pc On The Duodenal Digestiomentioning

confidence: 57%

Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests

et al. 2011

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a-LactalbuminIn-vitro gastric digestion In-vitro duodenal digestion IgE-binding a b s t r a c t This paper examines lysozyme (LYS) behaviour upon in-vitro digestion, mimicking different conditions in the stomach and intestine, and assessing the effect of natural surfactants, such as phosphatidylcholine (PC) or bile salts (BS), on hydrolysis and residual immunogenicity of the digests. The hydrolysis pattern of LYS was compared to that of a-lactalbumin (LA). Hydrolysis of LYS only occurred at low pH. PC slightly increased its resistance to pepsinolysis. A similar behaviour was found for LA. Circular dichroism revealed that the more rigid structure of LYS, as compared with that of LA, could protect it from proteolysis at acidic pH and fluorescence spectra suggested that, at acidic pH, both proteins associated to PC films. The gastric digests of LYS showed high IgE-binding capacity using sera from egg-allergic patients. On the other hand, it was found that LYS precipitated under conditions that simulated a duodenal environment, mainly due to the presence of BS.Published by Elsevier Ltd.

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Section: Effect Of the Presence Of Bs And Pc On The Duodenal Digestiomentioning

confidence: 57%

Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests

et al. 2011

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“…Burnett et al [22] published data on the behaviour of a range of protein allergens in the presence of model emulsion systems under simulated gastric and simulated duodenal conditions. A number of major allergens were found to adsorb to model stomach emulsions and subsequently desorb when duodenal conditions prevailed.…”

Section: Incorporation Of Gut Lipid Phasesmentioning

confidence: 99%

“…Decreased digestibility through adsorption would also help explain why proteins readily susceptible to pepsin digestion, like BSA, can be identified as food allergens. Furthermore, fluorescence and FTIR spectroscopy studies have shown that proteins adsorbed to oil/water interfaces can be partly denatured [22]. This is a recognised phenomenon associated with protein adsorption to oil/water interfaces [24].…”

Section: Incorporation Of Gut Lipid Phasesmentioning

confidence: 99%

In vitro digestion methods for assessing the effect of food structure on allergen breakdown

Wickham¹,

Faulks²,

Mills³

2009

Molecular Nutrition Food Res

191

136

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This article reviews the in vitro digestion models developed to assess the stability of food allergens during digestion. It is hypothesised that food allergens must exhibit sufficient gastro-intestinal stability to reach the intestinal mucosa where absorption and sensitisation (development of atopy) can occur. The investigation of stability of proteins within the gastrointestinal tract may provide prospective testing for allergenicity and could be a significant and valid parameter that distinguishes food allergens from nonallergens. Systematic evaluation of the stability of food allergens that are active via the gastrointestinal tract is currently tested in traditional pepsin digestibility models. The human gastrointestinal tract however is very complex and this article points out the importance of using physiologically relevant in vitro digestion systems for evaluating digestibility of allergens. This would involve the simulation of the stomach/small intestine environment (multi-phase models) with sequential addition of digestive enzymes, surfactants such as phospholipids and bile salts under physiological conditions, as well as the consideration of the effect of the food matrices on the allergen digestion.

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“…The demonstration of an acid-induced molten state in SKTI assumes importance because this conformation is commonly involved in translocation of proteins across membrane barriers and even in membrane insertion [34]. The ability of a food protein to be an allergen may be related to its stability in the acid environment of the digestive system by assuming a more molten structure, which is also able to cross the gastrointestinal membrane barrier and thereby initiate the IgE response [34,35].…”

Section: Discussionmentioning

confidence: 99%

Stability of the allergenic soybean Kunitz trypsin inhibitor

Roychaudhuri

Sarath

Zeece

et al. 2004

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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The soybean Kunitz trypsin inhibitor (SKTI) is a 21.5 kDa allergenic protein that belongs to the family of all antiparallel h-sheet proteins that are highly resistant to thermal and chemical denaturation. Spectroscopic and biochemical techniques such as circular dichroism (CD), ANS fluorescence and proteolysis were used to study its molecular structure under denaturing conditions such as acid and heat to which these allergens are commonly exposed during food processing. Reduction of native SKTI leads to its complete and rapid proteolysis by pepsin in simulated gastric fluid (SGF). Limited proteolysis with chymotrypsin during renaturation after heating showed that the native structure reforms at around 60 jC reversing the denaturation. CD spectra revealed that under acid denaturing conditions, SKTI shows major changes in conformation, indicating the possibility of a molten structure. The existence of this intermediate was established by ANS fluorescence studies at different concentrations of HCl. The remarkable stability of SKTI to both thermal and acid denaturation may be important for its role as a food allergen. D

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Interaction between protein allergens and model gastric emulsions

Cited by 29 publications

References 0 publications

Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests

Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests

In vitro digestion methods for assessing the effect of food structure on allergen breakdown

Stability of the allergenic soybean Kunitz trypsin inhibitor

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