期刊
ULTRASONICS SONOCHEMISTRY
卷 78, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.ultsonch.2021.105717
关键词
Ultrasound; Small and uniform ovalbumin; Pectin; Pumpkin seed oil; Emulsification stability; Oxidation stability
资金
- Open Project of Beijing Technology and Business University [W2020JSZX0564]
- National Natural Science Foundation of China [31760477]
- National Key Research and Development Program of China [2018YFD0400302]
- Talent Introduction Start-up Project of Hefei University of Technology
- Cooperative Projects of Hefei University of Technology - Wuhan Xudong Food Co. Ltd. [W2021JSKF0356, W2020JSKF0457]
This study utilized small and uniform ovalbumin and pectin to stabilize pumpkin seed oil in the form of an emulsion, resulting in excellent interfacial, rheological, emulsifying, and antioxidant properties. The physical stability of the emulsions under various stress conditions was improved, and the oxidation of linolenic acid was notably delayed, showing promising potential for food-related applications.
Pumpkin seed oil (PSO), which is a valuable compound with high nutritional value used for the prevention of various chronic diseases, is prone to oxidation. In this work, small and uniform (su) ovalbumin (OVA) and pectin (PEC) were used to stabilize PSO in the form of an emulsion. The results showed that suOVA-PEC-PSO emulsion with a droplet size of 9.82 +/- 0.05 mu m was successfully self-assembled from PSO, PEC, and suOVA solution (with a droplet size of 230.13 +/- 14.10 nm) treated with 300 W ultrasound, owing to the formation of a more stable interfacial film on the surface of droplets. The interfacial, rheological, emulsifying, and antioxidant properties of the suOVA-PES-PSO emulsions were excellent, owing to the synergistic effects between PEC and suOVA solution. Moreover, the physical stability of the suOVA-PEC-PSO emulsions to salt stress, a freeze-thaw cycle, and heat treatment was also increased and the oxidation of linolenic acid was notably delayed. These results have extended the food-related applications of OVA and PSO, and provide a promising foundation for further exploration of the self-assembly of composite emulsions by small and uniform proteins.
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