A Study on the Mechanisms of Nanoparticle-Stabilized High Internal Phase Emulsions Constructed by Cross-Linking Egg White Protein Isolate with Different Transglutaminase Concentrations
There is an increasing interest in the development of high internal phase emulsions (HIPE) stabilized by food-grade nanoparticles due to their potential applications in the food industry. In this study, cross-linked egg white protein isolates (cEPIs) are prepared by adding 10 u/g, 20 u/g, and 40 u/g...
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| Format: | Article |
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MDPI AG
2022-06-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/12/1765 |
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| author | Yanjie Zhao Peng Wang Yujuan Xu Xianming Zeng Xinglian Xu |
| author_facet | Yanjie Zhao Peng Wang Yujuan Xu Xianming Zeng Xinglian Xu |
| author_sort | Yanjie Zhao |
| collection | DOAJ |
| description | There is an increasing interest in the development of high internal phase emulsions (HIPE) stabilized by food-grade nanoparticles due to their potential applications in the food industry. In this study, cross-linked egg white protein isolates (cEPIs) are prepared by adding 10 u/g, 20 u/g, and 40 u/g of transglutaminase (TG), and the impacts of interface properties of cEPIs and emulsifying of HIPEs are investigated. Relative to the native EPI, the cEPIs have more irregular and agglomerated morphology, and the turbidity and hydrophobicity are significantly increased. The particle size and zeta potential of cEPIs considerably varied with the addition of TG. In HIPE, the formation, physical properties, and microstructure are characterized by visual observations, the Turbiscan stability index, and CLSM. The results indicated that stable and gel-like HIPEs are formed by cEPIs at oil internal phase (<i>φ</i>) values of 0.75–0.90. Especially for the enzyme additions of 20 u/g, the cEPIs had the best storage stability and the lowest TSI value (2.50) and formed a gel network structure at <i>φ</i> values of 0.9 microscopically. Overall, this study can enrich the theoretical frame of interface properties by enzyme treatment. Besides, it would be of great importance for the research of HIPE stabilized by cEPIs appropriate to be applied in food formulations. |
| first_indexed | 2024-03-09T23:48:43Z |
| format | Article |
| id | doaj.art-6f38d72985b044c3919de1d3bc7d6072 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T23:48:43Z |
| publishDate | 2022-06-01 |
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| series | Foods |
| spelling | doaj.art-6f38d72985b044c3919de1d3bc7d60722023-11-23T16:38:45ZengMDPI AGFoods2304-81582022-06-011112176510.3390/foods11121765A Study on the Mechanisms of Nanoparticle-Stabilized High Internal Phase Emulsions Constructed by Cross-Linking Egg White Protein Isolate with Different Transglutaminase ConcentrationsYanjie Zhao0Peng Wang1Yujuan Xu2Xianming Zeng3Xinglian Xu4Key Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaThere is an increasing interest in the development of high internal phase emulsions (HIPE) stabilized by food-grade nanoparticles due to their potential applications in the food industry. In this study, cross-linked egg white protein isolates (cEPIs) are prepared by adding 10 u/g, 20 u/g, and 40 u/g of transglutaminase (TG), and the impacts of interface properties of cEPIs and emulsifying of HIPEs are investigated. Relative to the native EPI, the cEPIs have more irregular and agglomerated morphology, and the turbidity and hydrophobicity are significantly increased. The particle size and zeta potential of cEPIs considerably varied with the addition of TG. In HIPE, the formation, physical properties, and microstructure are characterized by visual observations, the Turbiscan stability index, and CLSM. The results indicated that stable and gel-like HIPEs are formed by cEPIs at oil internal phase (<i>φ</i>) values of 0.75–0.90. Especially for the enzyme additions of 20 u/g, the cEPIs had the best storage stability and the lowest TSI value (2.50) and formed a gel network structure at <i>φ</i> values of 0.9 microscopically. Overall, this study can enrich the theoretical frame of interface properties by enzyme treatment. Besides, it would be of great importance for the research of HIPE stabilized by cEPIs appropriate to be applied in food formulations.https://www.mdpi.com/2304-8158/11/12/1765egg white protein isolatetransglutaminasehigh internal phase emulsionnanoparticlesemulsion physical stability |
| spellingShingle | Yanjie Zhao Peng Wang Yujuan Xu Xianming Zeng Xinglian Xu A Study on the Mechanisms of Nanoparticle-Stabilized High Internal Phase Emulsions Constructed by Cross-Linking Egg White Protein Isolate with Different Transglutaminase Concentrations Foods egg white protein isolate transglutaminase high internal phase emulsion nanoparticles emulsion physical stability |
| title | A Study on the Mechanisms of Nanoparticle-Stabilized High Internal Phase Emulsions Constructed by Cross-Linking Egg White Protein Isolate with Different Transglutaminase Concentrations |
| title_full | A Study on the Mechanisms of Nanoparticle-Stabilized High Internal Phase Emulsions Constructed by Cross-Linking Egg White Protein Isolate with Different Transglutaminase Concentrations |
| title_fullStr | A Study on the Mechanisms of Nanoparticle-Stabilized High Internal Phase Emulsions Constructed by Cross-Linking Egg White Protein Isolate with Different Transglutaminase Concentrations |
| title_full_unstemmed | A Study on the Mechanisms of Nanoparticle-Stabilized High Internal Phase Emulsions Constructed by Cross-Linking Egg White Protein Isolate with Different Transglutaminase Concentrations |
| title_short | A Study on the Mechanisms of Nanoparticle-Stabilized High Internal Phase Emulsions Constructed by Cross-Linking Egg White Protein Isolate with Different Transglutaminase Concentrations |
| title_sort | study on the mechanisms of nanoparticle stabilized high internal phase emulsions constructed by cross linking egg white protein isolate with different transglutaminase concentrations |
| topic | egg white protein isolate transglutaminase high internal phase emulsion nanoparticles emulsion physical stability |
| url | https://www.mdpi.com/2304-8158/11/12/1765 |
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