Cargando…
Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study
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 co...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9736135/ https://www.ncbi.nlm.nih.gov/pubmed/36496706 http://dx.doi.org/10.3390/foods11233896 |
_version_ | 1784846948076879872 |
---|---|
author | Zhou, Qi Li, Helin Li, Fang Zhang, Benpeng Wu, Xiaojuan Wu, Wei |
author_facet | Zhou, Qi Li, Helin Li, Fang Zhang, Benpeng Wu, Xiaojuan Wu, Wei |
author_sort | Zhou, Qi |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9736135 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-97361352022-12-11 Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study Zhou, Qi Li, Helin Li, Fang Zhang, Benpeng Wu, Xiaojuan Wu, Wei Foods Article 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. MDPI 2022-12-02 /pmc/articles/PMC9736135/ /pubmed/36496706 http://dx.doi.org/10.3390/foods11233896 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Zhou, Qi Li, Helin Li, Fang Zhang, Benpeng Wu, Xiaojuan Wu, Wei Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study |
title | Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study |
title_full | Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study |
title_fullStr | Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study |
title_full_unstemmed | Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study |
title_short | Strategy and Mechanism of Rice Bran Protein Emulsion Stability Based on Rancidity-Induced Protein Oxidation: An Ultrasonic Case Study |
title_sort | strategy and mechanism of rice bran protein emulsion stability based on rancidity-induced protein oxidation: an ultrasonic case study |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9736135/ https://www.ncbi.nlm.nih.gov/pubmed/36496706 http://dx.doi.org/10.3390/foods11233896 |
work_keys_str_mv | AT zhouqi strategyandmechanismofricebranproteinemulsionstabilitybasedonrancidityinducedproteinoxidationanultrasoniccasestudy AT lihelin strategyandmechanismofricebranproteinemulsionstabilitybasedonrancidityinducedproteinoxidationanultrasoniccasestudy AT lifang strategyandmechanismofricebranproteinemulsionstabilitybasedonrancidityinducedproteinoxidationanultrasoniccasestudy AT zhangbenpeng strategyandmechanismofricebranproteinemulsionstabilitybasedonrancidityinducedproteinoxidationanultrasoniccasestudy AT wuxiaojuan strategyandmechanismofricebranproteinemulsionstabilitybasedonrancidityinducedproteinoxidationanultrasoniccasestudy AT wuwei strategyandmechanismofricebranproteinemulsionstabilitybasedonrancidityinducedproteinoxidationanultrasoniccasestudy |