Abstract:Bitter apricot kernel contains various bioactive components and nutrients and can be used as value-added food ingredients. However, it is also an allergen which may cause risk to allergic people if they consume foods containing bitter apricot kernel.To investigate the impact of ultra-high pressure on the structure and immunoreactivity of bitter apricot kernel protein isolate, the spatial structure and allergenicity under different pressures were detected by circular dichroism, fluorescence spectroscopy and enzyme linked immunosorbent assay(ELISA). The results demonstrated that ultrahigh pressure treatment at 100~500 MPa for 900 s insignificantly changed the secondary structure of bitter apricot kernel protein isolate. However, with the increase of pressure intensity and processing time, the tertiary structure of bitter apricot kernel protein isolate was unfolded and the hydrophobic groups were thus exposed, which led to the increase of fluorescence intensity and surface hydrophobicity and the decrease of immunoreactivity. The reduced immuno- reactivity of bitter apricot kernel protein isolate was possibly due to the changes of conformational epitopes causing food allergy. This study may provide important implications for the development of safe bitter apricot kernel food and beverage products.
