Pressure and temperature stability of the main apple allergen Mal d1
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027022%3A_____%2F11%3A00000161" target="_blank" >RIV/00027022:_____/11:00000161 - isvavai.cz</a>
Výsledek na webu
—
DOI - Digital Object Identifier
—
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Pressure and temperature stability of the main apple allergen Mal d1
Popis výsledku v původním jazyce
High-pressure Fourier-transform infrared (FTIR) spectroscopy was used to determine the pressure and temperature stability of Mal d1. This study was triggered by contradictory results in the literature regarding the success of pressure treatment in the destruction of the allergen. The protein unfolded at 55A degrees C when heated at normal atmospheric pressure. We also studied the effect exerted on pressure stability by environmental factors, which can be important for the stability of the protein in theapple. The pressure unfolding was measured under different pD conditions, and the effect of sugar mixture similar to that of the apple and the effect of ionic strength were also studied. In all cases the allergen unfolded with a transition midpoint in the range of 150-250 MPa. Unfolding was irreversible and was followed by aggregation of the unfolded protein. Lowering the pD destabilized the protein, while addition of sugar mixture and of KCl had stabilizing effect.
Název v anglickém jazyce
Pressure and temperature stability of the main apple allergen Mal d1
Popis výsledku anglicky
High-pressure Fourier-transform infrared (FTIR) spectroscopy was used to determine the pressure and temperature stability of Mal d1. This study was triggered by contradictory results in the literature regarding the success of pressure treatment in the destruction of the allergen. The protein unfolded at 55A degrees C when heated at normal atmospheric pressure. We also studied the effect exerted on pressure stability by environmental factors, which can be important for the stability of the protein in theapple. The pressure unfolding was measured under different pD conditions, and the effect of sugar mixture similar to that of the apple and the effect of ionic strength were also studied. In all cases the allergen unfolded with a transition midpoint in the range of 150-250 MPa. Unfolding was irreversible and was followed by aggregation of the unfolded protein. Lowering the pD destabilized the protein, while addition of sugar mixture and of KCl had stabilizing effect.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
BO - Biofyzika
OECD FORD obor
—
Návaznosti výsledku
Projekt
<a href="/cs/project/2B06139" target="_blank" >2B06139: Inaktivace alergenů v potravinách pomocí vysokotlaké pasterace</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2011
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
European Biophysics Journal
ISSN
0175-7571
e-ISSN
—
Svazek periodika
40
Číslo periodika v rámci svazku
2
Stát vydavatele periodika
DE - Spolková republika Německo
Počet stran výsledku
9
Strana od-do
143-151
Kód UT WoS článku
000286606700004
EID výsledku v databázi Scopus
—