Changes to the tropomyosin structure alter the angiotensin-converting enzyme inhibitory activity and texture profiles of eel balls under high hydrostatic pressure

Abstract

Changes in the structure of tropomyosin (TM) altered the texture profiles of eel balls and the inhibitory activity of the angiotensin-converting enzyme (ACE).

Effects of High Hydrostatic Pressure on the Conformational Structure and Gel Properties of Myofibrillar Protein and Meat Quality: A Review

“…With increasing pressure, the hardness, springiness and chewiness values of red swamp crayfish (Procambarus clarkia) initially increased sharply, then decreased slightly, but all were higher than those of the control [82]. In our work, the texture parameters including hardness, springiness, chewiness and cohesiveness of eel balls were significantly improved with HHP treatment, and the optimum treating pressure was 400 MPa [9,36]. As for the eel surimi, the hardness, chewiness, gel strength and water-holding capacity increased significantly as well under HHP treatment, while the viscosity decreased [9,36].…”

“…The hardness, elasticity, mastic ability and cohesiveness increased by 3.00, 1.61, 5.96 and 1.23 times, respectively, when treated at 400 MPa for 15 min. In our work [9,36], further exploration of the protein structure revealed that the texture parameters of eel products were negatively correlated with the α-helix and β-sheet of proteins, but positively correlated with the random coil and β-turn of proteins (Figure 3). These results indicated that food textures can be directly related to the secondary and tertiary structures of MP.…”

“…In our work, the texture parameters including hardness, springiness, chewiness and cohesiveness of eel balls were significantly improved with HHP treatment, and the optimum treating pressure was 400 MPa [9,36]. As for the eel surimi, the hardness, chewiness, gel strength and water-holding capacity increased significantly as well under HHP treatment, while the viscosity decreased [9,36]. The hardness, elasticity, mastic ability and cohesiveness increased by 3.00, 1.61, 5.96 and 1.23 times, respectively, when treated at 400 MPa for 15 min.…”

“…With an increasing in pressure level, a gradual increase in β-sheets content is normally observed, but in the case of tropomyosin, the β-sheets content decreased at lower pressures and increased at higher pressures [36]. Li et al attributed this to the fact that, at a relatively lower pressure, intermolecular hydrogen bonds could be broken, rather than intramolecular hydrogen bonds [36]. With an increase in pressure, the intramolecular hydrogen bonds would be destroyed, leading to the transformation of α-helix to β-sheet, β-turn, and random coil, thus resulting in an increase of β-sheet content.…”

“…Some studies have suggested that HHP induces water infiltration into protein cavities, strengthening the hydrogen bonds between the protein and water molecules, wakening the intramolecular hydrogen bonds, resulting in changes to protein configuration [34,35]. With an increasing in pressure level, a gradual increase in β-sheets content is normally observed, but in the case of tropomyosin, the β-sheets content decreased at lower pressures and increased at higher pressures [36]. Li et al attributed this to the fact that, at a relatively lower pressure, intermolecular hydrogen bonds could be broken, rather than intramolecular hydrogen bonds [36].…”