Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study.

Qi Zhou, Helin Li, Fang Li, Benpeng Zhang, Xiaojuan Wu, Wei Wu

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Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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6 authors.

Qi ZhouCollege of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.

Helin LiCollege of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.

Fang LiCollege of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.

Benpeng ZhangCollege of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.

Xiaojuan WuCollege of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.

Wei WuCollege of Food Science and Engineering, Central South University of Forestry and Technology, Changsha 410004, China.ORCID 0000-0001-9229-6360

Funding

National Natural Science Foundation of China No. 31771918

6 · The paper itself

Abstract

To provide a strategy for improving the stability of rice bran protein emulsion (RBPE), rice bran proteins (RBPs) with different oxidation extents were prepared from fresh rice bran (RB) stored for different times (0, 1, 3, 5, 10 d), and RBPE was prepared with ultrasonic treatment. The ultrasonic conditions were optimized according to the results of the RBPE’s stability (when RB stored for 0, 1, 3, 5, 10 d, the optimal ultrasonic treatment conditions of RBPE were 500 w and 50 min, 400 w and 30 min, 400 w and 30 min, 300 w and 20 min, 500 w and 50 min, respectively). Additionally, the structural characteristics and the flexibility of RBPE interface protein were characterized, and the results showed that compared with native protein and excessive oxidized protein, the unfolded structure content and flexibility of interface protein of RBPE prepared by moderate oxidized protein under optimal ultrasonic intensity was higher. Furthermore, the correlation analysis showed that the RBPE stability was significantly correlated with the structural characteristics and flexibility of the RBPE interface protein (p < 0.05). In summary, ultrasonic treatment affected the interface protein’s structural characteristics and flexibility, improving the stability of RBPE prepared from oxidized RBP.

Indexed as

emulsion stabilityinterface proteinprotein oxidationultrasonic treatment

Identifiers

PMID36496706

DOI10.3390/foods11233896

PMCPMC9736135

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