Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring <i>(Clupea harengus membras)</i> Muscle Tissue
The technological properties of raw fish are influenced by the changes in protein structure under heating, which determines the texture and quality of the product. The aim of the study was to examine the protein denaturation temperature and the rheological properties of Baltic herring muscle tissue....
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MDPI AG
2021-04-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/10/4/829 |
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| author | Agnieszka Strzelczak Jerzy Balejko Mariusz Szymczak Agata Witczak |
| author_facet | Agnieszka Strzelczak Jerzy Balejko Mariusz Szymczak Agata Witczak |
| author_sort | Agnieszka Strzelczak |
| collection | DOAJ |
| description | The technological properties of raw fish are influenced by the changes in protein structure under heating, which determines the texture and quality of the product. The aim of the study was to examine the protein denaturation temperature and the rheological properties of Baltic herring muscle tissue. The thermal properties were determined by the differential scanning calorimetry (DSC) method and the rheological properties were determined using dynamic oscillatory tests. DSC showed four peaks associated with denaturing transformations of myosin (39.59 °C), sarcoplasm (51.67 °C), connective tissue (63.16 °C), and actin (74.40 °C). Analysis showed that not all transformations occurred according to the same kinetic model. The first two and the last peak are described by 1st order kinetics, while peak 3 is described by 2nd order kinetics. Correlating the changes in fish tissue structure during heating with the rheological characteristics provides more information. The obtained kinetics models correlated very strongly with the results of model testing. Rheological changes of the G’ and G” values had two inflexion points and demonstrate a high degree of convergence with the DSC changes of herring muscle tissue from 20 to 85 °C. |
| first_indexed | 2024-03-10T12:25:26Z |
| format | Article |
| id | doaj.art-c44a4541d01d46e389712ec85b11e197 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T12:25:26Z |
| publishDate | 2021-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-c44a4541d01d46e389712ec85b11e1972023-11-21T15:05:03ZengMDPI AGFoods2304-81582021-04-0110482910.3390/foods10040829Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring <i>(Clupea harengus membras)</i> Muscle TissueAgnieszka Strzelczak0Jerzy Balejko1Mariusz Szymczak2Agata Witczak3Department of Commodity Science and Quality Assessment, Process Engineering and Fundamentals of Human Nutrition, Faculty of Food Science and Fisheries, West Pomeranian University of Technology in Szczecin, 71-459 Szczecin, PolandDepartment of Commodity Science and Quality Assessment, Process Engineering and Fundamentals of Human Nutrition, Faculty of Food Science and Fisheries, West Pomeranian University of Technology in Szczecin, 71-459 Szczecin, PolandDepartment of Toxicology, Dairy Technology and Food Storage, Faculty of Food Science and Fisheries, West Pomeranian University of Technology in Szczecin, 71-459 Szczecin, PolandDepartment of Toxicology, Dairy Technology and Food Storage, Faculty of Food Science and Fisheries, West Pomeranian University of Technology in Szczecin, 71-459 Szczecin, PolandThe technological properties of raw fish are influenced by the changes in protein structure under heating, which determines the texture and quality of the product. The aim of the study was to examine the protein denaturation temperature and the rheological properties of Baltic herring muscle tissue. The thermal properties were determined by the differential scanning calorimetry (DSC) method and the rheological properties were determined using dynamic oscillatory tests. DSC showed four peaks associated with denaturing transformations of myosin (39.59 °C), sarcoplasm (51.67 °C), connective tissue (63.16 °C), and actin (74.40 °C). Analysis showed that not all transformations occurred according to the same kinetic model. The first two and the last peak are described by 1st order kinetics, while peak 3 is described by 2nd order kinetics. Correlating the changes in fish tissue structure during heating with the rheological characteristics provides more information. The obtained kinetics models correlated very strongly with the results of model testing. Rheological changes of the G’ and G” values had two inflexion points and demonstrate a high degree of convergence with the DSC changes of herring muscle tissue from 20 to 85 °C.https://www.mdpi.com/2304-8158/10/4/829fish proteinsdenaturationDSCkineticsrheologyBaltic herring |
| spellingShingle | Agnieszka Strzelczak Jerzy Balejko Mariusz Szymczak Agata Witczak Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring <i>(Clupea harengus membras)</i> Muscle Tissue Foods fish proteins denaturation DSC kinetics rheology Baltic herring |
| title | Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring <i>(Clupea harengus membras)</i> Muscle Tissue |
| title_full | Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring <i>(Clupea harengus membras)</i> Muscle Tissue |
| title_fullStr | Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring <i>(Clupea harengus membras)</i> Muscle Tissue |
| title_full_unstemmed | Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring <i>(Clupea harengus membras)</i> Muscle Tissue |
| title_short | Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring <i>(Clupea harengus membras)</i> Muscle Tissue |
| title_sort | effect of protein denaturation temperature on rheological properties of baltic herring i clupea harengus membras i muscle tissue |
| topic | fish proteins denaturation DSC kinetics rheology Baltic herring |
| url | https://www.mdpi.com/2304-8158/10/4/829 |
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