Abstract
Purpose: To undertake comparative kinetic and thermodynamic analyses of the interaction of bovine serum albumin (BSA) with IgG pre-treated with ultra-high pressure (UHP) and moderate heat.Methods: BSA solutions were processed at 100 – 600 MPa and 25 – 40 °C. We applied an optical biosensor based on surface plasmon resonance (SPR). The dissociation and association kinetics of antigen-antibody complexes were measured at different temperatures. By analyzing the resultant sensograms, the association rate constant (ka), dissociation rate constant (kd), equilibrium dissociation constant (KD), and thermodynamic parameters were calculated.Results: The equilibrium disassociation constant, KD, ranged from a low value of 3.15 × 10−7 M (0.1 MPa, 25 °C) to a high value of 66.42 × 10−7 M (600 MPa, 55 °C). Increase in pressure and temperature led to decrease in the affinity of BSA for IgG. Pressure levels above 300 MPa promoted interactions between breakage of disulfide bonds, and the unfolding and aggregation of BSA.Conclusions: These results show that the combination of UHP and moderate heat treatment cdecrease the allergenicity of BSA by changing their protein conformation.Keywords: Ultra - high pressure, Bovine serum albumin, Surface plasmon resonance, Kinetics, Thermodynamics, Allergens
Highlights
Food allergies have become increasingly prevalent and occur especially in infants or children [1]
There are a few papers published on kinetic and thermodynamic changes in the binding properties of bovine serum albumin (BSA) treated by ultrahigh pressure (UHP)
A reduction in affinity was induced by pressure levels of 100 – 600 MPa in the temperature range of 25 – 55 °C
Summary
Food allergies have become increasingly prevalent and occur especially in infants or children [1]. 1 –2 % of infants and 8 % of children suffer from food allergies [2]. It has been reported that allergy to meat is rare; positive skin prick tests to beef were described in only 7.69 % of children with atopic dermatitis [3,4]. BSA has been identified as one of the most important allergens in bovine meat, with a high degree of crossreactions due to the significant sequence and structural similarities of serum albumin from different organisms [5,6]. It has been discovered that the structural changes induced by pressure may reduce or eliminate the antigencity of BSA and pig serum albumin (PSA) [8].
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