Effect of Protein Denaturation Temperature on Rheological Properties of Baltic Herring (Clupea harengus membras) Muscle Tissue

• Published in: Foods Vol. 10; no. 4; p. 829
• Main Authors: Strzelczak, Agnieszka, Balejko, Jerzy, Szymczak, Mariusz, Witczak, Agata
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 11.04.2021; MDPI
• Subjects: Accuracy; Actin; Animal tissues; Baltic herring; Biopolymer denaturation; Calorimetry; Connective tissues; denaturation; Differential scanning calorimetry; DSC; Fish; fish proteins; Food; Food science; Heating; Indium; Kinetics; Model testing; Muscles; Myosin; Protein denaturation; Protein structure; Proteins; Raw materials; Rheological properties; Rheology; Temperature; Thermal properties; Thermodynamic properties; Baltic herring; denaturation; rheology; kinetics; DSC; fish proteins
• ISSN: 2304-8158; 2304-8158
• DOI: 10.3390/foods10040829

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.