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pH and Heat Resistance of the Major Celery Allergen Api g 1

Title data

Rib-Schmidt, Carina ; Riedl, Philipp ; Meisinger, Veronika ; Schwaben, Luisa ; Schulenborg, Thomas ; Reuter, Andreas ; Schiller, Dirk ; Seutter von Loetzen, Christian ; Rösch, Paul:
pH and Heat Resistance of the Major Celery Allergen Api g 1.
In: Molecular Nutrition & Food Research. Vol. 62 (May 2018) Issue 15 .
ISSN 1613-4133
DOI: https://doi.org/10.1002/mnfr.201700886

Abstract in another language

The major celery allergen Api g 1 is a member of the pathogenesis-related 10 class protein family. This study aims to investigate the impact of heat and pH on the native protein conformation required for Immunoglobulin E (IgE) recognition.
Spectroscopic methods, MS and IgE-binding analyses are used to study the effects of pH and thermal treatment on Api g 1.0101. Heat processing results in a loss of the native protein fold via denaturation, oligomerization, and precipitation along with a subsequent reduction of IgE recognition. The induced effects and timescales are strongly pH dependent. While Api g 1 refolds partially into an IgE-binding conformation at physiological pH, acidic pH treatment leads to the formation of structurally heat-resistant, IgE-reactive oligomers. Thermal processing in the presence of a celery matrix or at pH conditions close to the isoelectric point (pI = 4.63) of Api g 1.0101 results in almost instant precipitation.
This study demonstrates that Api g 1.0101 is not intrinsically susceptible to heat treatment in vitro. However, the pH and the celery matrix strongly influence the stability of Api g 1.0101 and might be the main reasons for the observed temperature lability of this important food allergen.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Chair Biopolymers - Univ.-Prof. Dr. Paul Rösch
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 30 Jan 2019 12:16
Last Modified: 30 Jan 2019 12:16
URI: https://eref.uni-bayreuth.de/id/eprint/47137