Abstract
Whiff (Lepidorhombus whiffiagonis) is a fish frequently consumed in Spain. Lep w 1, its major allergen, is a calcium‐binding β‐parvalbumin. The resistance of Lep w 1 to heat denaturation and to digestion were studied by circular dichroism spectroscopy and by in vitro gastric digestion systems. Purified Lep w 1 was thermally stable up to 65°C at neutral pH. Calcium depletion resulted in a change of its structure as determined by circular dichroism spectroscopy. A partial loss of structure was also observed at acidic pH; however, the allergen retained its full IgE‐binding ability. The partially denatured Lep w 1 was easily digested by pepsin within 2 min. Further, the IgE reactivity of proteins extracted from cooked fish and their stability to proteolysis were analyzed. The extract revealed a higher number of IgE reactive bands than an extract from uncooked fish. IgE binding to these proteins could not be inhibited by an extract from uncooked fish. In contrast to a raw fish extract, the cooked extract showed higher resistance to pepsinolysis. The stability of Lep w 1 to thermal denaturation and digestion explains the high allergenicity of whiff.