Effect of Ultrasonic-Assisted Thermal Treatment on the Structure and Solubility of Rapeseed Protein
The effects of ultrasound (200, 400 and 600 W)-assisted thermal treatment (25, 60 and 90 ℃) on the structure and solubility of rapeseed protein were investigated. For the individual thermal treatment groups, as the heating temperature increased, protein aggregation occurred. The particle size increa...
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China Food Publishing Company
2025-01-01
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| Series: | Shipin Kexue |
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| Online Access: | https://www.spkx.net.cn/fileup/1002-6630/PDF/2025-46-1-012.pdf |
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| author | ZHAO Kangyu, YANG Ping, MA Junkun, SHU Wenjing, YANG Feng, XIE Yisha, LIU Qingqing |
| author_facet | ZHAO Kangyu, YANG Ping, MA Junkun, SHU Wenjing, YANG Feng, XIE Yisha, LIU Qingqing |
| author_sort | ZHAO Kangyu, YANG Ping, MA Junkun, SHU Wenjing, YANG Feng, XIE Yisha, LIU Qingqing |
| collection | DOAJ |
| description | The effects of ultrasound (200, 400 and 600 W)-assisted thermal treatment (25, 60 and 90 ℃) on the structure and solubility of rapeseed protein were investigated. For the individual thermal treatment groups, as the heating temperature increased, protein aggregation occurred. The particle size increased from 1 188.18 to 5 630.00 nm. The solubility decreased from 8.6% to 5.6% and the absolute value of the zeta potential decreased. This was accompanied by a conformational transition from an ordered to a disordered state. After the combined ultrasonic-thermal treatment, the spatial structure of protein molecules was unfolded, thus resulting in the breaking of peptide bonds and the exposure of hydrophobic groups. Compared with the 25 ℃ treatment, its combination with 600 W ultrasonication promoted the breakdown of protein aggregates and reduced the particle size to 1 155.27 nm, leading to the exposure of more polar groups, increased amounts of charged residues, increased surface hydrophobicity, mutual transformation of secondary structures, and a significant improvement in protein solubility (up to 57.31%). The results of this study provide a scientific basis for research on combined modifications and solubility regulation of rapeseed protein. |
| format | Article |
| id | doaj-art-0dc646847ed4434fbec500def793360c |
| institution | Kabale University |
| issn | 1002-6630 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | China Food Publishing Company |
| record_format | Article |
| series | Shipin Kexue |
| spelling | doaj-art-0dc646847ed4434fbec500def793360c2025-02-05T09:08:12ZengChina Food Publishing CompanyShipin Kexue1002-66302025-01-0146110010710.7506/spkx1002-6630-20240313-088Effect of Ultrasonic-Assisted Thermal Treatment on the Structure and Solubility of Rapeseed ProteinZHAO Kangyu, YANG Ping, MA Junkun, SHU Wenjing, YANG Feng, XIE Yisha, LIU Qingqing0(1. Chongqing Key Laboratory of Speciality Food Co-built by Sichuan and Chongqing, School of Food and Bioengineering, Xihua University, Chengdu 610039, China; 2. College of Food Science &Technology, Nanchang University, Nanchang 330027, China)The effects of ultrasound (200, 400 and 600 W)-assisted thermal treatment (25, 60 and 90 ℃) on the structure and solubility of rapeseed protein were investigated. For the individual thermal treatment groups, as the heating temperature increased, protein aggregation occurred. The particle size increased from 1 188.18 to 5 630.00 nm. The solubility decreased from 8.6% to 5.6% and the absolute value of the zeta potential decreased. This was accompanied by a conformational transition from an ordered to a disordered state. After the combined ultrasonic-thermal treatment, the spatial structure of protein molecules was unfolded, thus resulting in the breaking of peptide bonds and the exposure of hydrophobic groups. Compared with the 25 ℃ treatment, its combination with 600 W ultrasonication promoted the breakdown of protein aggregates and reduced the particle size to 1 155.27 nm, leading to the exposure of more polar groups, increased amounts of charged residues, increased surface hydrophobicity, mutual transformation of secondary structures, and a significant improvement in protein solubility (up to 57.31%). The results of this study provide a scientific basis for research on combined modifications and solubility regulation of rapeseed protein.https://www.spkx.net.cn/fileup/1002-6630/PDF/2025-46-1-012.pdfultrasound; rapeseed protein; synergistic effect; protein structure; heat treatment; solubility |
| spellingShingle | ZHAO Kangyu, YANG Ping, MA Junkun, SHU Wenjing, YANG Feng, XIE Yisha, LIU Qingqing Effect of Ultrasonic-Assisted Thermal Treatment on the Structure and Solubility of Rapeseed Protein Shipin Kexue ultrasound; rapeseed protein; synergistic effect; protein structure; heat treatment; solubility |
| title | Effect of Ultrasonic-Assisted Thermal Treatment on the Structure and Solubility of Rapeseed Protein |
| title_full | Effect of Ultrasonic-Assisted Thermal Treatment on the Structure and Solubility of Rapeseed Protein |
| title_fullStr | Effect of Ultrasonic-Assisted Thermal Treatment on the Structure and Solubility of Rapeseed Protein |
| title_full_unstemmed | Effect of Ultrasonic-Assisted Thermal Treatment on the Structure and Solubility of Rapeseed Protein |
| title_short | Effect of Ultrasonic-Assisted Thermal Treatment on the Structure and Solubility of Rapeseed Protein |
| title_sort | effect of ultrasonic assisted thermal treatment on the structure and solubility of rapeseed protein |
| topic | ultrasound; rapeseed protein; synergistic effect; protein structure; heat treatment; solubility |
| url | https://www.spkx.net.cn/fileup/1002-6630/PDF/2025-46-1-012.pdf |
| work_keys_str_mv | AT zhaokangyuyangpingmajunkunshuwenjingyangfengxieyishaliuqingqing effectofultrasonicassistedthermaltreatmentonthestructureandsolubilityofrapeseedprotein |