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Structural and physicochemical properties of the different ultrasound frequency modified Qingke protein
Huijing Chen1, Zehang Guo1, Zhirong Wang2
1College of Food Science, Southwest University, 2 Tiansheng Road, Beibei, Chongqing 400715, PR China; Chinese-Hungarian Cooperative Research Centre for Food Science, Chongqing 400715, PR China; Laboratory of Quality & Safety Risk Assessment for Agri-products on Storage and Preservation (Chongqing), Ministry of Agriculture and Rural Affairs of the People's Republic of China, Chongqing 400715, PR China.
Abstract:
There is a burgeoning demand for modified plant-based proteins with desirable physicochemical and functional properties. The cereal Qingke is a promising alternative protein source, but its use has been limited by its imperfect functional characteristics. To investigate the effect of ultrasound treatment on Qingke protein, we applied single- (40 kHz), dual- (28/40 kHz), and tri- (28/40/50 kHz) frequency ultrasound on the isolated protein and measured subsequent physicochemical and structural changes. The results showed that the physicochemical properties of proteins were modified following ultrasound treatment, and many of these changes significantly increased with increasing frequency. Compared with the native Qingke protein (control), the solubility, foaming activity, stability, and water or oil holding capacity of tri-frequency ultrasound modified Qingke protein increased by 43.54%, 20.83%, 20.51%, 28.9%, and 45.2%, respectively. Furthermore, ultrasound treatment altered the secondary and tertiary structures of the protein resulting in more exposed chromophoric groups and inner hydrophobic groups, as well as reduced β-sheets and increasedrandom coils, relative to the control. Rheological and texture characterization indicated that the values of G' and G'', hardness, gumminess, and chewiness decreased after ultrasound treatment. This study could provide a theoretical basis for the application of multi-frequency ultrasonic technology for modification of Qingke protein to expand its potential use as an alternative protein source.

