Impact of High Hydrostatic Pressure on the Antigenicity and Conformational Integrity of β-Conglycinin from Soybeans and Tropomyosin from Oysters
學生姓名:
李佳佳
指導教授:
陳冠文
學 期:
113下
摘 要:
High hydrostatic pressure (HHP) is an emerging non-thermal food processing technology that modifies protein conformation and reduces allergenicity. This study examined the effects of HHP and heat treatment on tropomyosin (TM) in oyster and β-conglycinin in soybean. HHP
preserved TM’s molecular weight but induced structural unfolding, reducing IgG-binding, particularly at 600 MPa, as evidenced by FTIR and fluorescence spectroscopy. At 600 MPa, the α-helix content of TM decreased from 76.28% to 30.04%, while the β-sheet content increased from 7.57% to 37.48%, indicating significant structural rearrangement. Increased surface hydrophobicity and secondary structural rearrangements contributed to reduced allergenicity. For β-conglycinin, HHP alone reduced antigenicity by 36.22%, while 400 MPa HHP combined with 100°C heat for 20 minutes achieved an 87.04% reduction. Structural changes, including disrupted β-sheet and α-helix structures and increased β-turns and random coils, masked allergenic epitopes and further lowered immunoreactivity. The transmittance changes in the Amide I, II, and III bands confirmed these structural modifications. Western blot and ELISA confirmed these reductions, supporting the role of HHP and heat in modifying allergen structures. These findings highlight HHP, especially with heat, as a promising method for producing hypoallergenic seafood and plant-based proteins, though further studies on digestibility and bioavailability are needed.
preserved TM’s molecular weight but induced structural unfolding, reducing IgG-binding, particularly at 600 MPa, as evidenced by FTIR and fluorescence spectroscopy. At 600 MPa, the α-helix content of TM decreased from 76.28% to 30.04%, while the β-sheet content increased from 7.57% to 37.48%, indicating significant structural rearrangement. Increased surface hydrophobicity and secondary structural rearrangements contributed to reduced allergenicity. For β-conglycinin, HHP alone reduced antigenicity by 36.22%, while 400 MPa HHP combined with 100°C heat for 20 minutes achieved an 87.04% reduction. Structural changes, including disrupted β-sheet and α-helix structures and increased β-turns and random coils, masked allergenic epitopes and further lowered immunoreactivity. The transmittance changes in the Amide I, II, and III bands confirmed these structural modifications. Western blot and ELISA confirmed these reductions, supporting the role of HHP and heat in modifying allergen structures. These findings highlight HHP, especially with heat, as a promising method for producing hypoallergenic seafood and plant-based proteins, though further studies on digestibility and bioavailability are needed.
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