The Effect of Salt on the Gelling Properties and Protein Phosphorylation of Surimi-Crabmeat Mixed Gels
The effects of different salt additions (1.0%, 1.5%, 2.0%, 2.5%, 3.0%, and 3.5%) on the gelling properties and protein phosphorylation of the mixed gels (MG) formed by silver carp (<i>Hypophthalmichthys molitrix</i>) surimi with 10% crabmeat were investigated. The MG’s breaking force, de...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-12-01
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| Series: | Gels |
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| Online Access: | https://www.mdpi.com/2310-2861/8/1/10 |
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| author | Yajun Zhu Yufeng Lu Tao Ye Shaotong Jiang Lin Lin Jianfeng Lu |
| author_facet | Yajun Zhu Yufeng Lu Tao Ye Shaotong Jiang Lin Lin Jianfeng Lu |
| author_sort | Yajun Zhu |
| collection | DOAJ |
| description | The effects of different salt additions (1.0%, 1.5%, 2.0%, 2.5%, 3.0%, and 3.5%) on the gelling properties and protein phosphorylation of the mixed gels (MG) formed by silver carp (<i>Hypophthalmichthys molitrix</i>) surimi with 10% crabmeat were investigated. The MG’s breaking force, deformation, gel strength, and water-holding capacity (WHC) increased as the salt concentration increased. The intrinsic fluorescence intensity of the samples initially decreased and then increased, reaching the lowest when the NaCl concentration was 2.5%. The result of SDS–polyacrylamide gel electrophoresis indicated that large aggregates were formed by protein–protein interaction in the MG containing 2.5% or 3.0% NaCl, decreasing the protein band intensity. It was also found that with the addition of NaCl, the phosphorus content initially increased and then decreased, reaching the maximum when the NaCl concentration was 2% or 2.5%, which was similar to the changing trend of actin band intensity reported in the results of Western blot. These results revealed that the amount of salt used had a significant effect on the degree of phosphorylation of the MG protein. The increase in phosphorylation was linked to improved gelling properties, which could lead to new ideas for manufacturing low-salt surimi products in the future. |
| first_indexed | 2024-03-10T01:27:18Z |
| format | Article |
| id | doaj.art-ef176475e645468f9d3088fdc325d28f |
| institution | Directory Open Access Journal |
| issn | 2310-2861 |
| language | English |
| last_indexed | 2024-03-10T01:27:18Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Gels |
| spelling | doaj.art-ef176475e645468f9d3088fdc325d28f2023-11-23T13:49:49ZengMDPI AGGels2310-28612021-12-01811010.3390/gels8010010The Effect of Salt on the Gelling Properties and Protein Phosphorylation of Surimi-Crabmeat Mixed GelsYajun Zhu0Yufeng Lu1Tao Ye2Shaotong Jiang3Lin Lin4Jianfeng Lu5Engineering Research Center of Bio-Process, Ministry of Education, Hefei University of Technology, Hefei 230009, ChinaEngineering Research Center of Bio-Process, Ministry of Education, Hefei University of Technology, Hefei 230009, ChinaEngineering Research Center of Bio-Process, Ministry of Education, Hefei University of Technology, Hefei 230009, ChinaEngineering Research Center of Bio-Process, Ministry of Education, Hefei University of Technology, Hefei 230009, ChinaEngineering Research Center of Bio-Process, Ministry of Education, Hefei University of Technology, Hefei 230009, ChinaEngineering Research Center of Bio-Process, Ministry of Education, Hefei University of Technology, Hefei 230009, ChinaThe effects of different salt additions (1.0%, 1.5%, 2.0%, 2.5%, 3.0%, and 3.5%) on the gelling properties and protein phosphorylation of the mixed gels (MG) formed by silver carp (<i>Hypophthalmichthys molitrix</i>) surimi with 10% crabmeat were investigated. The MG’s breaking force, deformation, gel strength, and water-holding capacity (WHC) increased as the salt concentration increased. The intrinsic fluorescence intensity of the samples initially decreased and then increased, reaching the lowest when the NaCl concentration was 2.5%. The result of SDS–polyacrylamide gel electrophoresis indicated that large aggregates were formed by protein–protein interaction in the MG containing 2.5% or 3.0% NaCl, decreasing the protein band intensity. It was also found that with the addition of NaCl, the phosphorus content initially increased and then decreased, reaching the maximum when the NaCl concentration was 2% or 2.5%, which was similar to the changing trend of actin band intensity reported in the results of Western blot. These results revealed that the amount of salt used had a significant effect on the degree of phosphorylation of the MG protein. The increase in phosphorylation was linked to improved gelling properties, which could lead to new ideas for manufacturing low-salt surimi products in the future.https://www.mdpi.com/2310-2861/8/1/10surimicrabmeatNaClgelling propertiesprotein phosphorylation |
| spellingShingle | Yajun Zhu Yufeng Lu Tao Ye Shaotong Jiang Lin Lin Jianfeng Lu The Effect of Salt on the Gelling Properties and Protein Phosphorylation of Surimi-Crabmeat Mixed Gels Gels surimi crabmeat NaCl gelling properties protein phosphorylation |
| title | The Effect of Salt on the Gelling Properties and Protein Phosphorylation of Surimi-Crabmeat Mixed Gels |
| title_full | The Effect of Salt on the Gelling Properties and Protein Phosphorylation of Surimi-Crabmeat Mixed Gels |
| title_fullStr | The Effect of Salt on the Gelling Properties and Protein Phosphorylation of Surimi-Crabmeat Mixed Gels |
| title_full_unstemmed | The Effect of Salt on the Gelling Properties and Protein Phosphorylation of Surimi-Crabmeat Mixed Gels |
| title_short | The Effect of Salt on the Gelling Properties and Protein Phosphorylation of Surimi-Crabmeat Mixed Gels |
| title_sort | effect of salt on the gelling properties and protein phosphorylation of surimi crabmeat mixed gels |
| topic | surimi crabmeat NaCl gelling properties protein phosphorylation |
| url | https://www.mdpi.com/2310-2861/8/1/10 |
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