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Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure

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Akkerdaas, J, Totis, M, Barnett, B, Bell, E, Davis, T, Edrington, T, Glenn, K, Graser, G, Herman, R, Knulst, A, Ladics, G, McClain, S, Poulsen, LK, Ranjan, R, Rascle, J-B, Serrano, H, Speijer, D, Wang, R, Pereira Mouriès, L, Capt, A & van Ree, R 2018, 'Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure', Clinical and translational allergy, vol. 8, pp. 30. https://doi.org/10.1186/s13601-018-0216-9

APA

Akkerdaas, J., Totis, M., Barnett, B., Bell, E., Davis, T., Edrington, T., Glenn, K., Graser, G., Herman, R., Knulst, A., Ladics, G., McClain, S., Poulsen, L. K., Ranjan, R., Rascle, J-B., Serrano, H., Speijer, D., Wang, R., Pereira Mouriès, L., ... van Ree, R. (2018). Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure. Clinical and translational allergy, 8, 30. https://doi.org/10.1186/s13601-018-0216-9

CBE

Akkerdaas J, Totis M, Barnett B, Bell E, Davis T, Edrington T, Glenn K, Graser G, Herman R, Knulst A, Ladics G, McClain S, Poulsen LK, Ranjan R, Rascle J-B, Serrano H, Speijer D, Wang R, Pereira Mouriès L, Capt A, van Ree R. 2018. Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure. Clinical and translational allergy. 8:30. https://doi.org/10.1186/s13601-018-0216-9

MLA

Vancouver

Author

Akkerdaas, Jaap ; Totis, Muriel ; Barnett, Brian ; Bell, Erin ; Davis, Tom ; Edrington, Thomas ; Glenn, Kevin ; Graser, Gerson ; Herman, Rod ; Knulst, Andre ; Ladics, Gregory ; McClain, Scott ; Poulsen, Lars K ; Ranjan, Rakesh ; Rascle, Jean-Baptiste ; Serrano, Hector ; Speijer, Dave ; Wang, Rong ; Pereira Mouriès, Lucilia ; Capt, Annabelle ; van Ree, Ronald. / Protease resistance of food proteins : a mixed picture for predicting allergenicity but a useful tool for assessing exposure. In: Clinical and translational allergy. 2018 ; Vol. 8. pp. 30.

Bibtex

@article{3fba333fe7a341b4afb1d36ee4df0a85,
title = "Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure",
abstract = "Background: Susceptibility to pepsin digestion of candidate transgene products is regarded an important parameter in the weight-of-evidence approach for allergenicity risk assessment of genetically modified crops. It has been argued that protocols used for this assessment should better reflect physiological conditions encountered in representative food consumption scenarios.Aim: To evaluate whether inclusion of more physiological conditions, such as sub-optimal and lower pepsin concentrations, in combination with pancreatin digestion, improved the performance of digestibility protocols used in characterization of protein stability.Methods: Four pairs of established allergens and their related non/weakly-allergenic counterparts (seed albumins, muscle tropomyosins, plant lipid transfer proteins [LTP] and collagens) plus fish parvalbumin, were subjected to nine combinations of pH (1.2-2.5-4.0) and pepsin-to-protein ratio (PPR: 10-1-0.1 U/µg) for pepsin digestion, followed by pancreatin digestion in the presence of bile salts. Digestion was monitored by SDS-PAGE in conjunction with Coomassie staining and immunoblotting using rabbit antisera and human IgE.Results: At pH 4.0 and at PPR 0.1 most proteins, both allergen and non-allergen, were highly resistant to pepsin. Under conditions known to favor pepsin proteolysis, the established major allergens Ara h 2, Pru p 3 and Pen a 1 were highly resistant to proteolysis, while the allergen Cyp c 1 was not. However, this resistance to pepsin digestion only made Ara h 2 and to a lesser extent Pen a 1 and Pru p 3 stand out compared to their non-allergenic counterparts. Largely irrespective of preceding pepsin digestion conditions, pancreatin digestion was very effective for all tested proteins, allergens and non-allergens, except for Cyp c 1 and bovine collagen.Conclusions: Sub-optimal pH, low pepsin-to protein ratio, and sequential pepsin and pancreatin digestion protocols do not improve the predictive value in distinguish allergens from non-allergens. Digestion conditions facilitating such distinction differ per protein pair.",
author = "Jaap Akkerdaas and Muriel Totis and Brian Barnett and Erin Bell and Tom Davis and Thomas Edrington and Kevin Glenn and Gerson Graser and Rod Herman and Andre Knulst and Gregory Ladics and Scott McClain and Poulsen, {Lars K} and Rakesh Ranjan and Jean-Baptiste Rascle and Hector Serrano and Dave Speijer and Rong Wang and {Pereira Mouri{\`e}s}, Lucilia and Annabelle Capt and {van Ree}, Ronald",
year = "2018",
doi = "10.1186/s13601-018-0216-9",
language = "English",
volume = "8",
pages = "30",
journal = "Clinical and Translational Allergy",
issn = "2045-7022",
publisher = "BioMed Central Ltd",

}

RIS

TY - JOUR

T1 - Protease resistance of food proteins

T2 - a mixed picture for predicting allergenicity but a useful tool for assessing exposure

AU - Akkerdaas, Jaap

AU - Totis, Muriel

AU - Barnett, Brian

AU - Bell, Erin

AU - Davis, Tom

AU - Edrington, Thomas

AU - Glenn, Kevin

AU - Graser, Gerson

AU - Herman, Rod

AU - Knulst, Andre

AU - Ladics, Gregory

AU - McClain, Scott

AU - Poulsen, Lars K

AU - Ranjan, Rakesh

AU - Rascle, Jean-Baptiste

AU - Serrano, Hector

AU - Speijer, Dave

AU - Wang, Rong

AU - Pereira Mouriès, Lucilia

AU - Capt, Annabelle

AU - van Ree, Ronald

PY - 2018

Y1 - 2018

N2 - Background: Susceptibility to pepsin digestion of candidate transgene products is regarded an important parameter in the weight-of-evidence approach for allergenicity risk assessment of genetically modified crops. It has been argued that protocols used for this assessment should better reflect physiological conditions encountered in representative food consumption scenarios.Aim: To evaluate whether inclusion of more physiological conditions, such as sub-optimal and lower pepsin concentrations, in combination with pancreatin digestion, improved the performance of digestibility protocols used in characterization of protein stability.Methods: Four pairs of established allergens and their related non/weakly-allergenic counterparts (seed albumins, muscle tropomyosins, plant lipid transfer proteins [LTP] and collagens) plus fish parvalbumin, were subjected to nine combinations of pH (1.2-2.5-4.0) and pepsin-to-protein ratio (PPR: 10-1-0.1 U/µg) for pepsin digestion, followed by pancreatin digestion in the presence of bile salts. Digestion was monitored by SDS-PAGE in conjunction with Coomassie staining and immunoblotting using rabbit antisera and human IgE.Results: At pH 4.0 and at PPR 0.1 most proteins, both allergen and non-allergen, were highly resistant to pepsin. Under conditions known to favor pepsin proteolysis, the established major allergens Ara h 2, Pru p 3 and Pen a 1 were highly resistant to proteolysis, while the allergen Cyp c 1 was not. However, this resistance to pepsin digestion only made Ara h 2 and to a lesser extent Pen a 1 and Pru p 3 stand out compared to their non-allergenic counterparts. Largely irrespective of preceding pepsin digestion conditions, pancreatin digestion was very effective for all tested proteins, allergens and non-allergens, except for Cyp c 1 and bovine collagen.Conclusions: Sub-optimal pH, low pepsin-to protein ratio, and sequential pepsin and pancreatin digestion protocols do not improve the predictive value in distinguish allergens from non-allergens. Digestion conditions facilitating such distinction differ per protein pair.

AB - Background: Susceptibility to pepsin digestion of candidate transgene products is regarded an important parameter in the weight-of-evidence approach for allergenicity risk assessment of genetically modified crops. It has been argued that protocols used for this assessment should better reflect physiological conditions encountered in representative food consumption scenarios.Aim: To evaluate whether inclusion of more physiological conditions, such as sub-optimal and lower pepsin concentrations, in combination with pancreatin digestion, improved the performance of digestibility protocols used in characterization of protein stability.Methods: Four pairs of established allergens and their related non/weakly-allergenic counterparts (seed albumins, muscle tropomyosins, plant lipid transfer proteins [LTP] and collagens) plus fish parvalbumin, were subjected to nine combinations of pH (1.2-2.5-4.0) and pepsin-to-protein ratio (PPR: 10-1-0.1 U/µg) for pepsin digestion, followed by pancreatin digestion in the presence of bile salts. Digestion was monitored by SDS-PAGE in conjunction with Coomassie staining and immunoblotting using rabbit antisera and human IgE.Results: At pH 4.0 and at PPR 0.1 most proteins, both allergen and non-allergen, were highly resistant to pepsin. Under conditions known to favor pepsin proteolysis, the established major allergens Ara h 2, Pru p 3 and Pen a 1 were highly resistant to proteolysis, while the allergen Cyp c 1 was not. However, this resistance to pepsin digestion only made Ara h 2 and to a lesser extent Pen a 1 and Pru p 3 stand out compared to their non-allergenic counterparts. Largely irrespective of preceding pepsin digestion conditions, pancreatin digestion was very effective for all tested proteins, allergens and non-allergens, except for Cyp c 1 and bovine collagen.Conclusions: Sub-optimal pH, low pepsin-to protein ratio, and sequential pepsin and pancreatin digestion protocols do not improve the predictive value in distinguish allergens from non-allergens. Digestion conditions facilitating such distinction differ per protein pair.

U2 - 10.1186/s13601-018-0216-9

DO - 10.1186/s13601-018-0216-9

M3 - Journal article

C2 - 30116520

VL - 8

SP - 30

JO - Clinical and Translational Allergy

JF - Clinical and Translational Allergy

SN - 2045-7022

ER -

ID: 59013922