Effects of high hydrostatic pressure on the structural characteristics of parvalbumin of cultured large yellow croaker (Larimichthys crocea)

Abstract

Parvalbumin (PV) induces IgE-mediated allergic reactions and is an important allergen in fish species. The effects of high hydrostatic pressure (HHP) treatment (300, 450, 600 MPa; 10 min) on the structural characteristics of PV in cultured large yellow croakers (Larimichthys crocea) were investigated. The effects of HHP treatment were analyzed by free sulfhydryl content, surface hydrophobicity, circular dichroism spectroscopy (CD), laser Raman spectroscopy, and endogenous fluorescence spectroscopy. The results showed that after HHP treatment, the free sulfhydryl content in PV decreased slightly and the surface hydrophobicity increased, indicating changes in the tertiary structure of PV. CD showed that with increase in pressure, the content of α-helix in the secondary structure of PV decreased slightly. This indicated that the stability of the secondary structure of PV was affected by HHP treatment. The secondary structure of PV was dominated by α-helix and that the α-helix content in PV also increased. The redshift of endogenous fluorescence spectroscopy decreases the fluorescence intensity. Practical applications Parvalbumin (PV) in the large yellow croaker is the main allergen with a molecular weight of 12 kDa. It is an allergy risk to consumers. The application of high hydrostatic pressure (HHP) treatment of 200 to 400 MPa could be successfully applied to changes of the tertiary and secondary structure of PV. This suggests a direct and important relationship between the structural characteristics and allergenicity of PV. The application of HHP treatment effectively reduced the allergenicity of PV. It is useful to desensitization of the large yellow croaker before processing. 1 | INTRODUC TI ON Fish are a key food resource of human populations worldwide, with the earliest aquaculture activities dating as far back as 3,500 BC. Approximately one-sixth of the world's protein intake is from fish, with the proportion being much high in certain developing countries and regions that depend heavily on oceans for food. The large yellow croaker (Larimichthys crocea), which belongs to the family Sciaenidae of the order Perciformes, is a warm-temperate demersal neritic fish species that exhibits schooling and migratory behaviors. How to cite this article: Zhang H, Liao H, Lu Y, et al. Effects of high hydrostatic pressure on the structural characteristics of parvalbumin of cultured large yellow croaker (Larimichthys crocea).

High Hydrostatic Pressure: Influences on Allergenicity, Bioactivities, and Structural and Functional Properties of Proteins from Diverse Food Sources

“…The unfolding of native proteins under HHP conditions altered their tertiary structure, subsequently hiding the active immunoglobulin G binding site within the structure and thereby reducing IgG binding capacity [ 108 ]. This phenomenon correlated with higher surface hydrophobicity observed under HHP treatment in various seafood, including threadfin bream [ 106 ], squid [ 100 ], silver pomfret [ 105 ], large yellow croaker [ 102 ], eel surimi [ 97 ], bighead carp [ 95 ], scallops [ 99 ], and oysters [ 98 ]. HHP treatment exposed hydrophobic regions previously buried inside the structure, replacing the native active sites [ 98 ].…”

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“…For fish products, high hydrostatic pressure (300-600 MPa for 10 min) treatment could effectively reduce the allergenicity of cultured large yellow croakers (Larimichthys crocea) by altering the stability of the secondary and tertiary structure of parvalbumin (H. Zhang et al, 2020).…”

“…For fish products, high hydrostatic pressure (300–600 MPa for 10 min) treatment could effectively reduce the allergenicity of cultured large yellow croakers ( Larimichthys crocea ) by altering the stability of the secondary and tertiary structure of parvalbumin (H. Zhang et al., 2020). Conversely, drying increased the IgE binding activity in Atlantic cod tested by an indirect competitive ELISA (Sletten et al., 2010).…”

Effect of Processing on Fish Protein Antigenicity and Allergenicity

“…The effect of glycation on parvalbumin allergenicity is also dependent on sugar structure, protein concentration, and glycation condition [ 121 ]. Non-thermal processing such as high hydrostatic pressure (HHP) could alter the secondary and tertiary structure of parvalbumin, which could effectively reduce its antigenicity [ 130 ]. It should be noted that a decrease in allergenicity in some fish allergic patients does not guarantee this function in other patients.…”