Covalent binding of ultrasound-treated japonica rice bran protein to catechin: Structural and functional properties of the complex

Ultrason Sonochem. 2023 Jan 12;93:106292. doi: 10.1016/j.ultsonch.2023.106292. Online ahead of print.ABSTRACTDue to the existence of many disulfide bonds in japonica rice bran protein (JRBP) molecules, their solubility is poor, which seriously affects other functional properties. To improve the functional characteristics of JRBP molecules, they were processed by ultrasound technology, and JRBP-catechin (CC) covalent complex was prepared. The structural and functional properties of indica and japonica rice bran proteins and their complexes were compared; furthermore, the changes in the structural and functional properties of JRBP-CC under different ultrasound conditions were investigated. The results showed that compared with indica rice bran protein (IRBP), the secondary structure of JRBP-CC was very different, the water holding capacity (WHC) was higher, and the emulsification performance was better. Different ultrasound conditions had different effects on the functional properties of JRBP-CC. When the ultrasound power was 200 W, the λmax redshift of the JRBP-CC complex was the most significant, the particle size was the smallest, the absolute value of the zeta potential was the largest, and the hydrophobicity and microstructure of the JRBP-CC complex were the best. Concurrently, the maximum WHC and oil holding capacity (OHC) of JRBP-CC under these conditions were 7.54 g/g and 6.87 g/g, respectively. Moreover, the emulsifying activity index (EAI) and emulsifying stability i...
Source: Ultrasonics Sonochemistry - Category: Chemistry Authors: Source Type: research
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