Effect of ultrasound on the functional properties and structural changes of chicken liver insoluble proteins isolated by isoelectric solubilization/precipitation
The studies investigated the effects of different ultrasonic powers (180, 360 and 540 W) on the functional properties and structural changes of chicken liver insoluble proteins (CLIPs) isolated by isoelectric solubilization/precipitation (ISP) (with alkaline solubilization at pH 11.0 and pH 12.0 res...
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Elsevier
2025-01-01
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Series: | Ultrasonics Sonochemistry |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S1350417724004140 |
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author | Rongrong Mao Guoyuan Xiong Haibo Zheng Jun Qi Chunhui Zhang |
author_facet | Rongrong Mao Guoyuan Xiong Haibo Zheng Jun Qi Chunhui Zhang |
author_sort | Rongrong Mao |
collection | DOAJ |
description | The studies investigated the effects of different ultrasonic powers (180, 360 and 540 W) on the functional properties and structural changes of chicken liver insoluble proteins (CLIPs) isolated by isoelectric solubilization/precipitation (ISP) (with alkaline solubilization at pH 11.0 and pH 12.0 respectively, and acid precipitation at pH 5.5). Results indicated that ultrasonic significantly increased the solubility of ISP-isolated CLIPs, and narrowed the particle size distribution of D3,2 and D4,3 (P < 0.05). The highest solubility was observed at pH 11.0 and 360 W ultrasound treatment, reaching 77.26 %. The ultrasonic with 360 W exhibited higher shear stress and apparent viscosity. Spectroscopy revealed that compared to without ultrasonic treatment, there was an increase in β-sheet and random curling content accompanied by a decrease in β-turn and α-helix structure when ultrasonication. Ultrasound altered the tyrosine hydrophobic residues to be exposed to the surface of the ISP-isolated CLIPs, thus improving the hydrophilicity. Overall, ultrasound combined with ISP treatment effectively improved the functional properties of CLIPs, and it might be a potential, safe and efficient method for improving the processing properties and broadening the application of insoluble animal-derived proteins. |
format | Article |
id | doaj-art-927f960c4c41404f8a3ae5c44bb22b85 |
institution | Kabale University |
issn | 1350-4177 |
language | English |
publishDate | 2025-01-01 |
publisher | Elsevier |
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series | Ultrasonics Sonochemistry |
spelling | doaj-art-927f960c4c41404f8a3ae5c44bb22b852025-01-11T06:38:42ZengElsevierUltrasonics Sonochemistry1350-41772025-01-01112107165Effect of ultrasound on the functional properties and structural changes of chicken liver insoluble proteins isolated by isoelectric solubilization/precipitationRongrong Mao0Guoyuan Xiong1Haibo Zheng2Jun Qi3Chunhui Zhang4Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization, Ministry of Agriculture and Rural Affairs, Anhui Engineering Research Center for High Value Utilization of Characteristic Agricultural Products, College of Tea & Food Science and Technology, Anhui Agricultural University, Hefei 230036, ChinaSchool of Food Engineering, Anhui Science and Technology University, Chuzhou 233100, China; Corresponding authors.School of Food Engineering, Anhui Science and Technology University, Chuzhou 233100, ChinaKey Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization, Ministry of Agriculture and Rural Affairs, Anhui Engineering Research Center for High Value Utilization of Characteristic Agricultural Products, College of Tea & Food Science and Technology, Anhui Agricultural University, Hefei 230036, China; Corresponding authors.Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaThe studies investigated the effects of different ultrasonic powers (180, 360 and 540 W) on the functional properties and structural changes of chicken liver insoluble proteins (CLIPs) isolated by isoelectric solubilization/precipitation (ISP) (with alkaline solubilization at pH 11.0 and pH 12.0 respectively, and acid precipitation at pH 5.5). Results indicated that ultrasonic significantly increased the solubility of ISP-isolated CLIPs, and narrowed the particle size distribution of D3,2 and D4,3 (P < 0.05). The highest solubility was observed at pH 11.0 and 360 W ultrasound treatment, reaching 77.26 %. The ultrasonic with 360 W exhibited higher shear stress and apparent viscosity. Spectroscopy revealed that compared to without ultrasonic treatment, there was an increase in β-sheet and random curling content accompanied by a decrease in β-turn and α-helix structure when ultrasonication. Ultrasound altered the tyrosine hydrophobic residues to be exposed to the surface of the ISP-isolated CLIPs, thus improving the hydrophilicity. Overall, ultrasound combined with ISP treatment effectively improved the functional properties of CLIPs, and it might be a potential, safe and efficient method for improving the processing properties and broadening the application of insoluble animal-derived proteins.http://www.sciencedirect.com/science/article/pii/S1350417724004140UltrasonicIsoelectric solubilization/precipitationChicken liver insoluble proteinsProtein structureFunctional properties |
spellingShingle | Rongrong Mao Guoyuan Xiong Haibo Zheng Jun Qi Chunhui Zhang Effect of ultrasound on the functional properties and structural changes of chicken liver insoluble proteins isolated by isoelectric solubilization/precipitation Ultrasonics Sonochemistry Ultrasonic Isoelectric solubilization/precipitation Chicken liver insoluble proteins Protein structure Functional properties |
title | Effect of ultrasound on the functional properties and structural changes of chicken liver insoluble proteins isolated by isoelectric solubilization/precipitation |
title_full | Effect of ultrasound on the functional properties and structural changes of chicken liver insoluble proteins isolated by isoelectric solubilization/precipitation |
title_fullStr | Effect of ultrasound on the functional properties and structural changes of chicken liver insoluble proteins isolated by isoelectric solubilization/precipitation |
title_full_unstemmed | Effect of ultrasound on the functional properties and structural changes of chicken liver insoluble proteins isolated by isoelectric solubilization/precipitation |
title_short | Effect of ultrasound on the functional properties and structural changes of chicken liver insoluble proteins isolated by isoelectric solubilization/precipitation |
title_sort | effect of ultrasound on the functional properties and structural changes of chicken liver insoluble proteins isolated by isoelectric solubilization precipitation |
topic | Ultrasonic Isoelectric solubilization/precipitation Chicken liver insoluble proteins Protein structure Functional properties |
url | http://www.sciencedirect.com/science/article/pii/S1350417724004140 |
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