Processing approaches to reducing allergenicity in proteins

Mills, E. N. Clare; Moreno, F. Javier; Sancho, Ana I.; Jenkins, John A.; Wichers, Harry J.

doi:10.1533/9781855738379.2.396

Cited by 5 publications

(5 citation statements)

References 102 publications

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“…It has been postulated that for an allergen sensitizing an individual via the GI tract, it must have properties which preserve its structure from degradation in the GI tract (such as resistance to low pH, bile salts and proteolysis), thus allowing enough allergen to survive in a sufficiently intact form to be taken up by the gut and sensitize the mucosal immune system [8–11]. Consequently, it has been proposed that resistance of proteins to pepsin digestion in the stomach is a marker for potential allergenicity [6].…”

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confidence: 99%

Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion

et al. 2004

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2S storage albumins occur in a diverse range of plant seeds, are members of the prolamin superfamily [1] and constitute one of the most important major plant food allergens that sensitize via the gastrointestinal (GI) tract [2]. Among the tree nuts, Brazil nut is frequently associated with immunoglobulin E (IgE)-mediated food allergy [3], the 2S albumin, known as Ber e 1, being the major allergen [4]. 2S albumins are considered to be structurally homologous, typically heterodimeric (small and large subunits of 4000 and 9000 M r , respectively) globular proteins. They have a conserved skeleton of cysteine residues (typical of members of the prolamin superfamily), which form four intermolecular disulphide bonds that hold the two subunits together and contribute to their stability and compactness [5]. This rigid The major 2S albumin allergen from Brazil nuts, Ber e 1, was subjected to gastrointestinal digestion using a physiologically relevant in vitro model system either before or after heating (100°C for 20 min). Whilst the albumin was cleaved into peptides, these were held together in a much larger structure even when digested by using a simulated phase 1 (gastric) followed by a phase 2 (duodenal) digestion system. Neither prior heating of Ber e 1 nor the presence of the physiological surfactant phosphatidylcholine affected the pattern of proteolysis. After 2 h of gastric digestion, 25% of the allergen remained intact, 50% corresponded to a large fragment of M r 6400, and the remainder comprised smaller peptides. During duodenal digestion, residual intact 2S albumin disappeared quickly, but a modified form of the 'large fragment' remained, even after 2 h of digestion, with a mass of 5000 Da. The 'large fragment' comprised several smaller peptides that were identified, by using different MS techniques, as deriving from the large subunit. In particular, sequences corresponding to the hypervariable region (Q37-M47) and to another peptide (P42-P69), spanning the main immunoglobulin E epitope region of 2S albumin allergens, were found to be largely intact following phase 1 (gastric) digestion. They also contained previously identified putative T-cell epitopes. These findings indicate that the characteristic conserved skeleton of cysteine residues of 2S albumin family and, particularly, the intrachain disulphide bond pattern of the large subunit, play a critical role in holding the core protein structure together even after extensive proteolysis, and the resulting structures still contain potentially active B-and T-cell epitopes.Abbreviations GI, gastrointestinal; IgE, immunoglobulin E; SGF, simulated gastric fluid; PtdCho, egg l-phosphatidylcholine.

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confidence: 99%

Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion

et al. 2004

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“…The resistance for pepsin digestion is used as a marker for assessing potential protein allergenicity. 36 As reported by Astwood et al . 40 the allergenic storage proteins possess digestive stability.…”

Section: Resultsmentioning

confidence: 71%

“…The resistance for pepsin digestion is used as a marker for assessing potential protein allergenicity. 36 As reported by Astwood et al 40 the allergenic storage proteins possess digestive stability. According to Fuchs and Astwood, 41 allergens that are less stable in SGF show some stability in SIF.…”

Section: Simulated Gastrointestinal Digestionmentioning

confidence: 87%

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Structural stability and Sin a 1 anti-epitope antibody binding ability of yellow mustard (Sinapis alba L.) napin during industrial-scale myrosinase inactivation process

et al. 2015

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This study investigated the structural stability of yellow mustard (YM, Sinapis alba L.) napin and the changes of its Sin a 1 anti-epitope antibody-binding ability during myrosinase enzyme inactivation process. The food industry uses myrosinase-inactive non-pungent YM for uses beyond spice applications. Napin was isolated from seeds received from an industrial processor before (YM + M) and after (YM - M) myrosinase inactivation. Secondary and tertiary structural features and surface hydrophobicity parameters of napin were analyzed. The Sin a 1 content in YM seeds and the stability of Sin a 1-containing napin during simulated in vitro gastrointestinal (GI) digestion were determined by a non-competitive indirect enzyme-linked immunosorbent assay using the Sin a 1 anti-epitope antibody (AE-Ab) as the primary Ab. YM napin retained the dominant alpha-helical components of secondary and tertiary structure folds during this process. YM - M napin showed changes in hydrophobicity parameters of the molecules and binding ability of AE-Ab: 2.19 ± 0.48 g per 100 g of YM - M seeds vs. 1.49 ± 0.16 g per 100 g YM + M seeds. YM - M proteins were more susceptible for in vitro GI digestion and also showed a 30% reduction in AE-Ab binding ability upon digestion of napins. This suggests that the myrosinase inactivation process has induced the surface modification of napin, exposing Sin a 1 epitope, leading to an increase in AE-Ab binding. However, the epitope region of YM - M napin showed improved susceptibility for hydrolysis during GI digestion resulting in fewer available epitope regions, suggesting a possible reduction in napin immune reactivity.

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“…Several thermal and nonthermal techniques involving molecular‐level structural modifications of allergens via deamidation, aggregation, and hydrolysis or their interactions with other food components, such as the formation of complexes and Maillard reaction (El Mecherfi et al., 2020; Mills et al., 2004; Taheri‐Kafrani et al., 2009; Villemin et al., 2019) have been used to alleviate protein allergenicity. Moist heat (boiling, autoclaving extrusion, frying, and retorting) and dry heat (including baking, microwaving, and roasting) are the two types of thermal treatment used in the reduction of protein allergenicity (Li et al., 2016).…”

Section: Hv‐cap For Protein Modificationmentioning

confidence: 99%

Cold atmospheric plasma‐induced protein modification: Novel nonthermal processing technology to improve protein quality, functionality, and allergenicity reduction

Olatunde

Hewage

Dissanayake

et al. 2023

Comp Rev Food Sci Food Safe

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With the constant increase in protein demand globally, it is expedient to develop a strategy to effectively utilize protein, particularly those extracted from plant origin, which has been associated with low digestibility, poor techno-functional properties, and inherent allergenicity. Several thermal modification approaches have been developed to overcome these limitations and showed excellent results.Nevertheless, the excessive unfolding of the protein, aggregation of unfolded proteins, and irregular protein crosslinking have limited its application. Additionally, the increased consumer demand for natural products with no chemical additives has created a bottleneck for chemical-induced protein modification. Therefore, researchers are now directed toward other nonthermal technologies, including high-voltage cold plasma, ultrasound, high-pressure protein, etc., for protein modification. The techno-functional properties, allergenicity, and protein digestibility are greatly influenced by the applied treatment and its process parameters. Nevertheless, the application of these technologies, particularly high-voltage cold plasma, is still in its primary stage. Furthermore, the protein modification mechanism induced by high-voltage cold plasma has not been fully explained. Thus, this review meets the necessity to assemble the recent information on the process parameters and conditions for modifying proteins by high-voltage cold plasma and its impact on protein techno-functional properties, digestibility, and allergenicity.

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Processing approaches to reducing allergenicity in proteins

Cited by 5 publications

References 102 publications

Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion

Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion

Structural stability and Sin a 1 anti-epitope antibody binding ability of yellow mustard (Sinapis alba L.) napin during industrial-scale myrosinase inactivation process

Cold atmospheric plasma‐induced protein modification: Novel nonthermal processing technology to improve protein quality, functionality, and allergenicity reduction

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