Abstract
Peanut protein isolate (PPI) was oxidized by peroxyl radicals derived from 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH), and the conformational properties of oxidized PPI were investigated. Oxidation of PPI resulted in gradual carbonyl generation and free sulfydryl group degradation. The analysis of the maximum emission wavelength indicated change in the tertiary conformation of PPI after oxidation. Lower level oxidation could generate soluble protein aggregates with more flexible structure, while higher level oxidation would induce the formation of insoluble aggregates. Result from dynamic light scattering (DLS) and protein solubility showed that protein aggregation was correlated with protein surface hydrophobicity, indicating that protein oxidation and heat treatment could induce protein aggregation, leading to PPI conformational changes.
Highlights
Peanut protein isolate (PPI) was oxidized by peroxyl radicals derived from 2,2-azobis (2-amidinopropane) dihydrochloride (AAPH), and the conformational properties of oxidized PPI were investigated
Result from dynamic light scattering (DLS) and protein solubility showed that protein aggregation was correlated with protein surface hydrophobicity, indicating that protein oxidation and heat treatment could induce protein aggregation, leading to PPI conformational changes
No significant difference of PPI carbonyl content was observed until AAPH concentration reached 1.0 mM
Summary
As an important oilseeds in China, India, and other countries, is a potential source of proteins [1]. Protein functional properties as an important food processing factors influence food quality. These properties include the water/oil binding, emulsification, foam formation, viscosity, and gelation. Some researchers had used various kinds of ROS or byproducts of lipid peroxidation to simulate protein oxidation. They found that protein oxidation affected the conformational and functional properties of food proteins, such as meat protein [11] and soybean protein [12]. AAPHderived peroxyl radicals as the byproduct of lipid peroxidation were used to evaluate the effect of protein oxidation on the conformational properties of PPI in this work
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