Fish Processing and Digestion Affect Parvalbumins Detectability in Gilthead Seabream and European Seabass

Abstract

Consumption of aquatic food, including fish, accounts for 17% of animal protein intake. However, fish consumption might also result in several side-effects such as sneezing, swelling and anaphylaxis in sensitized consumers. Fish allergy is an immune reaction to allergenic proteins in the fish muscle, for instance parvalbumin (PV), considered the major fish allergen. In this study, we characterize PV in two economically important fish species for southern European aquaculture, namely gilthead seabream and European seabass, to understand its stability during in vitro digestion and fish processing. This information is crucial for future studies on the allergenicity of processed fish products. PVs were extracted from fish muscles, identified by mass spectrometry (MS), and detected by sandwich enzyme-linked immunosorbent assay (ELISA) after simulated digestion and various food processing treatments. Secondary structures were determined by circular dichroism (CD) after purification by anion exchange and gel filtration chromatography. In both species, PVs presented as α-helical and β-sheet structures, at room temperature, were shown to unfold at boiling temperatures. In European seabass, PV detectability decreased during the simulated digestion and after 240 min (intestinal phase) no detection was observed, while steaming showed a decrease (p < 0.05) in PVs detectability in comparison to raw muscle samples, for both species. Additionally, freezing (−20 °C) for up to 12 months continued to reduce the detectability of PV in tested processing techniques. We concluded that PVs from both species are susceptible to digestion and processing techniques such as steaming and freezing. Our study obtained preliminary results for further research on the allergenic potential of PV after digestion and processing.

Au@Ag Core–Shell Nanoparticles for Colorimetric and Surface-Enhanced Raman-Scattering-Based Multiplex Competitive Lateral Flow Immunoassay for the Simultaneous Detection of Histamine and Parvalbumin in Fish

“…50 Likewise histamine, parvalbumin is also thermally stable, and its content in canned food might vary depending on techniques employed during food processing. 51,52 Therefore, the development of strategies for the detection and quantification of histamine and parvalbumin in canned tuna fish is of relevance. 52,53 ■ RESULTS AND DISCUSSION Synthesis and Analysis of SERS Tags.…”

“…In tuna it is significantly higher in white than in red muscle, as well as in ventral and dorsal portions of the white muscle . Likewise histamine, parvalbumin is also thermally stable, and its content in canned food might vary depending on techniques employed during food processing. , Therefore, the development of strategies for the detection and quantification of histamine and parvalbumin in canned tuna fish is of relevance. , …”