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Effect of ultra-high pressure on the structure and gelling properties of low salt golden threadfin bream (Nemipterus virgatus) myosin
- Wang, Jianyi, Li, Zhiyu, Zheng, Baodong, Zhang, Yi, Guo, Zebin
- Lebensmittel-Wissenschaft + [i.e. und] Technologie 2019 v.100 pp. 381-390
- Nemipterus, bream, gelation, gelling properties, gels, hydrophobicity, moieties, myosin, nuclear magnetic resonance spectroscopy, scanning electron microscopy, sodium chloride, sulfhydryl groups
- The effects of ultra-high pressure (UHP) treatment (150–600 MPa for 5 min) on the conformation and related gelation properties of golden threadfin bream (Nemipterus virgatus) myosin with two different NaCl concentrations (0.3 moL/L and 0.6 moL/L) were investigated. Upon increases in pressure (0.1–600 MPa), myosin unfolded from α-helical to a β-sheets, and buried hydrophobic and sulfhydryl groups became exposed. Therefore, the surface hydrophobicity and the reactive sulfhydryl content increased for both NaCl concentrations. The rheological modulus of groups in a low NaCl concentration (0.3 moL/L) reached a maximum value of 150 MPa, but decreased upon further increases in pressure (300–600 MPa); a similar tendency was also observed in the 0.6 moL/L NaCl groups. Low-field pulsed nuclear magnetic resonance and scanning electron microscopy results with the low NaCl groups indicated that moderate UHP treatment (≤300 MPa) strengthened the water retention and structure properties of the myosin gel, while stronger UHP treatment (≥450 MPa) weakened them. This undesirable effect of excess UHP treatment was somewhat mitigated in the 0.6 moL/L concentration groups. These findings show the potential use of UHP treatment in improving the gelling properties of myosin at low salt concentrations.