Abstract
This study examined the ability of cavitation jet processing to regulate the oxidation concentrations with 2,2’-azobis (2-amidinopropane) dihydrochloride (AAPH) (0.2, 1, and 5 mmol/L) and the structure and emulsification of soy protein isolate (SPI). The tested properties included particle size distribution, hydrophobic properties (sulfhydryl group (SH) and disulfide bond (S-S) contents, surface hydrophobicity (H0)), emulsifying properties (particle size and ζ-potential of emulsions, emulsification activity index (EAI), and emulsification stability index (ESI)), as well as conformational characteristics. The high shear force of cavitation jet treatment reduced the particle size of oxidized SPI and distributed uniformly. Cavitation jet (90 MPa)-treated SPI (AAPH with 1 mmol/L) demonstrated a high H0 (4688.70 ± 84.60), high EAI (71.78 ± 1.52 m2/g), and high ESI (86.73 ± 0.97%). The ordered secondary structure (α-helix and β-turn content) of SPI was enhanced by the cavitation jet. Meanwhile, the distribution of SPI-oxidized aggregates was observed under an atomic force microscope. Therefore, cavitation jet processing combined with oxidation treatment is an effective method to improve the characteristics of SPI and has potential industrial application prospects.
Highlights
Soy protein is a high-quality plant-derived protein
The results showed that peroxy radicals reacted with amino acid side chains of protein molecules under aerobic conditions, and some of them evolved into carbonyl derivatives in subsequent reactions, increasing the carbonyl content [34,35]
The carbonylation degree of oxidized soybean protein isolate (SPI) treated with the cavitation jet was still higher compared with natural SPI, which might be due to the irreversible oxidative modification of oxidative stress [37]
Summary
Soy protein is a high-quality plant-derived protein. Due to its unique nutritional value and excellent functional properties, soy protein has become one of the most important food ingredients widely used in the food industry [1,2]. Soybean protein isolate (SPI) is prone to oxidation and aggregation during storage and transportation, resulting in the loss of protein nutrition, quality degradation, and loss of some functional properties, such as solubility, gelation, and emulsification [3,4]. Protein oxidation is the covalent modification of a protein directly induced by reactive oxygen species or indirectly induced by reaction with secondary by-products of oxidative stress [5]. Researchers are interested in developing simple and sustainable processing methods to effectively regulate the oxidative aggregation behavior of soybean proteins and inhibit the degradation of protein products caused by oxidative damage
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