Enzymatic treatment to decrease the allergenicity of Pru p 3 from peach.

Area of Science:

• Food allergy research
• Protein biochemistry
• Enzymology

Background:

• Pru p 3, a lipid transfer protein from peaches, is a major allergen responsible for severe allergic reactions.
• Its resistance to processing and digestion contributes to the severity of peach allergy.

Purpose of the Study:

• To investigate the effect of various proteases on the degradation and allergenicity of Pru p 3.
• To identify specific proteases capable of reducing Pru p 3 allergenicity for potential hypoallergenic applications.

Main Methods:

• Pru p 3 was isolated using cation exchange chromatography and ultrafiltration.
• Purified Pru p 3 was incubated with fifteen different proteases under varying conditions.
• Degradation was assessed by SDS-PAGE, immunoreactivity by ELISA, peptide size by MALDI-TOF, and clinical reactivity by prick tests.

Main Results:

• Two acid proteases from Aspergillus niger efficiently degraded Pru p 3 at acidic pH, reducing it to peptides < 3.2 kDa.
• These proteases decreased Pru p 3 immunoreactivity by >95% (ELISA) and IgE reactivity by >70% (allergic patient sera).
• In peach-allergic patients, hydrolysates significantly reduced wheal size by 72-85% in prick tests.

Conclusions:

• Acid proteases from Aspergillus niger effectively degrade Pru p 3, a major peach allergen.
• This enzymatic treatment significantly reduces Pru p 3 allergenicity and clinical reactivity.
• Aspergillus niger acid protease shows potential for developing hypoallergenic peach products.