Effects of AAPH on structure, allergenicity and physicochemical properties of shrimp myofibrillar protein

Abstract

Lipid peroxidation has been shown to associate with meat quality by affecting physicochemical properties of myofibrillar proteins. In this work, shrimp myofibrillar protein (MP) was oxidized using 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH), which could generate peroxyl radicals in lipid peroxidation. Results showed that increasing AAPH concentration led to an increase in carbonyl groups and a decrease in free amino and sulfhydryl thiol groups in MP. Secondary structural analysis of MP revealed a conversion of α-helix to β-sheet content after AAPH treatment. SDS-PAGE showed the band intensity of tropomyosin was reduced after AAPH treatment, indicating a reduced allergenicity of tropomyosin. Moderate oxidation (1–10 mmol/L AAPH) promoted the formation of a dense network of MP gel, resulting in enhanced textural and rheological properties. However, excessive oxidation (10–20 mmol/L AAPH) weakened the MP gel strength and decreased its water-holding capacity. These findings provide theoretical guidance for developing shrimp surimi products with desirable textures.