Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar protein
The purpose of this research was to explore the different hydrodynamic cavitation (HC) times (0, 5, 10, 15, 20 min; power 550 W, pressure 0.14 MPa) on the emulsifying properties of tilapia myofibrillar protein (TMP). Results of pH, particle size, turbidity, solubility, surface hydrophobicity, and re...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2023-01-01
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| Series: | Frontiers in Nutrition |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fnut.2023.1116100/full |
| _version_ | 1797943909473583104 |
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| author | Yucheng Hou Xian’e Ren Xian’e Ren Yongchun Huang Yongchun Huang Kun Xie Keyao Wang Liyang Wang Fengyan Wei Feng Yang Feng Yang |
| author_facet | Yucheng Hou Xian’e Ren Xian’e Ren Yongchun Huang Yongchun Huang Kun Xie Keyao Wang Liyang Wang Fengyan Wei Feng Yang Feng Yang |
| author_sort | Yucheng Hou |
| collection | DOAJ |
| description | The purpose of this research was to explore the different hydrodynamic cavitation (HC) times (0, 5, 10, 15, 20 min; power 550 W, pressure 0.14 MPa) on the emulsifying properties of tilapia myofibrillar protein (TMP). Results of pH, particle size, turbidity, solubility, surface hydrophobicity, and reactive sulfhydryl (SH) group indicated that HC changed the structure of TMP, as confirmed by the findings of intrinsic fluorescence and circular dichroism (CD) spectra. Furthermore, HC increased the emulsifying activity index (EAI) significantly (P < 0.05) and changed the emulsifying stability index (ESI), droplet size, and rheology of TMP emulsions. Notably, compared with control group, the 10-min HC significantly decreased particle size and turbidity but increased solubility (P < 0.05), resulting in accelerated diffusion of TMP in the emulsion. The prepared TMP emulsion showed the highest ESI (from 71.28 ± 5.50 to 91.73 ± 5.56 min), the smallest droplet size (from 2,754 ± 110 to 2,138 ± 182 nm) and the best rheological properties, as demonstrated by the microstructure photographs. Overall, by showing the effect of HC in improving the emulsifying properties of TMP, the study demonstrated HC as a potential technique for meat protein processing. |
| first_indexed | 2024-04-10T20:31:34Z |
| format | Article |
| id | doaj.art-3b8e428d1d8f4f7dbc903d10c3f688f3 |
| institution | Directory Open Access Journal |
| issn | 2296-861X |
| language | English |
| last_indexed | 2024-04-10T20:31:34Z |
| publishDate | 2023-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Nutrition |
| spelling | doaj.art-3b8e428d1d8f4f7dbc903d10c3f688f32023-01-25T05:53:30ZengFrontiers Media S.A.Frontiers in Nutrition2296-861X2023-01-011010.3389/fnut.2023.11161001116100Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar proteinYucheng Hou0Xian’e Ren1Xian’e Ren2Yongchun Huang3Yongchun Huang4Kun Xie5Keyao Wang6Liyang Wang7Fengyan Wei8Feng Yang9Feng Yang10Guangxi Key Laboratory of Green Processing of Sugar Resources, Key Laboratory for Processing of Sugar Resources of Guangxi Higher Education Institutes, School of Biological and Chemical Engineering, Guangxi University of Science and Technology, Liuzhou, ChinaGuangxi Key Laboratory of Green Processing of Sugar Resources, Key Laboratory for Processing of Sugar Resources of Guangxi Higher Education Institutes, School of Biological and Chemical Engineering, Guangxi University of Science and Technology, Liuzhou, ChinaGuangxi Liuzhou Luosifen Research Center of Engineering Technology, Liuzhou, ChinaGuangxi Key Laboratory of Green Processing of Sugar Resources, Key Laboratory for Processing of Sugar Resources of Guangxi Higher Education Institutes, School of Biological and Chemical Engineering, Guangxi University of Science and Technology, Liuzhou, ChinaGuangxi Liuzhou Luosifen Research Center of Engineering Technology, Liuzhou, ChinaGuangxi Key Laboratory of Green Processing of Sugar Resources, Key Laboratory for Processing of Sugar Resources of Guangxi Higher Education Institutes, School of Biological and Chemical Engineering, Guangxi University of Science and Technology, Liuzhou, ChinaGuangxi Key Laboratory of Green Processing of Sugar Resources, Key Laboratory for Processing of Sugar Resources of Guangxi Higher Education Institutes, School of Biological and Chemical Engineering, Guangxi University of Science and Technology, Liuzhou, ChinaGuangxi Key Laboratory of Green Processing of Sugar Resources, Key Laboratory for Processing of Sugar Resources of Guangxi Higher Education Institutes, School of Biological and Chemical Engineering, Guangxi University of Science and Technology, Liuzhou, ChinaGuangxi Key Laboratory of Green Processing of Sugar Resources, Key Laboratory for Processing of Sugar Resources of Guangxi Higher Education Institutes, School of Biological and Chemical Engineering, Guangxi University of Science and Technology, Liuzhou, ChinaGuangxi Key Laboratory of Green Processing of Sugar Resources, Key Laboratory for Processing of Sugar Resources of Guangxi Higher Education Institutes, School of Biological and Chemical Engineering, Guangxi University of Science and Technology, Liuzhou, ChinaGuangxi Liuzhou Luosifen Research Center of Engineering Technology, Liuzhou, ChinaThe purpose of this research was to explore the different hydrodynamic cavitation (HC) times (0, 5, 10, 15, 20 min; power 550 W, pressure 0.14 MPa) on the emulsifying properties of tilapia myofibrillar protein (TMP). Results of pH, particle size, turbidity, solubility, surface hydrophobicity, and reactive sulfhydryl (SH) group indicated that HC changed the structure of TMP, as confirmed by the findings of intrinsic fluorescence and circular dichroism (CD) spectra. Furthermore, HC increased the emulsifying activity index (EAI) significantly (P < 0.05) and changed the emulsifying stability index (ESI), droplet size, and rheology of TMP emulsions. Notably, compared with control group, the 10-min HC significantly decreased particle size and turbidity but increased solubility (P < 0.05), resulting in accelerated diffusion of TMP in the emulsion. The prepared TMP emulsion showed the highest ESI (from 71.28 ± 5.50 to 91.73 ± 5.56 min), the smallest droplet size (from 2,754 ± 110 to 2,138 ± 182 nm) and the best rheological properties, as demonstrated by the microstructure photographs. Overall, by showing the effect of HC in improving the emulsifying properties of TMP, the study demonstrated HC as a potential technique for meat protein processing.https://www.frontiersin.org/articles/10.3389/fnut.2023.1116100/fullhydrodynamic cavitationmyofibrillar proteinphysicochemical structurerheologyemulsifying property |
| spellingShingle | Yucheng Hou Xian’e Ren Xian’e Ren Yongchun Huang Yongchun Huang Kun Xie Keyao Wang Liyang Wang Fengyan Wei Feng Yang Feng Yang Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar protein Frontiers in Nutrition hydrodynamic cavitation myofibrillar protein physicochemical structure rheology emulsifying property |
| title | Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar protein |
| title_full | Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar protein |
| title_fullStr | Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar protein |
| title_full_unstemmed | Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar protein |
| title_short | Effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia (Oreochromis niloticus) myofibrillar protein |
| title_sort | effects of hydrodynamic cavitation on physicochemical structure and emulsifying properties of tilapia oreochromis niloticus myofibrillar protein |
| topic | hydrodynamic cavitation myofibrillar protein physicochemical structure rheology emulsifying property |
| url | https://www.frontiersin.org/articles/10.3389/fnut.2023.1116100/full |
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