Table 1.
Changes in myofibrillar protein structure under HHP, including source, reaction conditions and relevant results.
| Scheme | Protein | Treatment Conditions | Secondary Structure | H0 and −SH | Reference |
| Silver carp (Hypophthalmichthys molitrix) | Myofibrillar | 200 to 500 MPa for 10 min at 20 °C | 100 MPa, no significant changes; 200 to 300 MPa, slight changes; above 400 MPa, α-helix fraction gradually decreased. | ≥300 MPa, the content of H0 and –SH increased. | [32] |
| Breast meats from Chicken | Myofibrillar | 100 to 500 MPa for 10 min | With increasing pressure, α-helix and β-sheet transformed into random coil and β-turn. | With increasing pressure, the content of H0 and –SH increased. | [26] |
| Pork | Myofibrillar | 200, 400, 600 and 800 MPa for 10 min at 5 or 20 °C | Solubility reduced because of aggregation. | [49] | |
| Eel surimi | Myofibrillar | 100–600 MPa for 15 min at 25 °C | 100–600 MPa, α-helix converted into a random coil and β-turn. | The content of H0 increased, total –SH reduced and reactive –SH increased. | [9] |
| Trichiurus Haumela Surimi | Myofibrillar | 300, 350, 400 and 450 MPa for 5 min at 18 ± 2 °C | The contents of α-helix and β-turn reduced, β-sheet and random coil increased. | [37] | |
| Large white sow biceps femoris |
Myofibrillar | 200, 400 and 600 MPa for 6 min at 20 ± 4 °C | High pressure promoted the α-helix reduction and the increase in β-sheet structures. | [34] | |
| Pre-rigor rabbit muscles | Myofibrillar | 100, 200 and 300 MPa for 15 or 180 s at 25 °C | 100 MPa, the content of H0 and reactive –SH slightly increased, above 200 MPa, the H0 reduced. | [50] | |
| Hake | Myofibrillars | 150, 250 and 500 MPa for 10 min | α-Helix reduced, β-sheet, β-turn and random coil increased. | [51] | |
| Chicken breast muscle (Pectoralis major) | Freeze-dried myofibrillar | 69, 103 and 138 MPa, high pressure homogenizer | Above 103 MPa, α-Helix and β-turn conversion to β-sheet structures occurred. | [52] | |
| Threadfin bream (Nemipterus spp.) | Actomyosin | 200, 400 and 600 MPa for 10, 30 and 50 min at room temperature | With pressure increasing, the H0 significantly increased, and the increasing speed of H0 slowed with treatment time incresing; the total –SH obviously reduced with pressure and time increasing, and the reactive –SH increased. | [14] | |
| Snakehead | Actomyosin | 100–600 MPa for 15 min at room temperature | 100–600 MPa, α-helix converted into random coil and β-turn. | 200–600 MPa, the H0 and reactive –SH increased. | Our work (Unpublished) |
| Hake (Merluccius merluccius) |
Sarcoplasmic | 200, 400 and 600 MPa for 6 min at 20 °C | α-Helix reduced, β-sheet, β-turn and random coil increased. | Above 200 MPa, the H0 and reactive –SH increased. | [53] |
| Eel surimi | Tropomyosin | 100–600 MPa for 15 min at room temperature | 200–400 MPa, β-sheet converted into random coil and β-turn; 500–600 MPa, α-helix converted into β-turn and β-sheet. | With increasing pressure, the content of H0 increased and –SH reduced. | [36] |
| Three-month-old male New Zealand rabbits | Myosin | 100, 150 and 200 MPa for 2 min at 10 °C | α-Helix content reduced as the pressure increased (≤150 MPa), β-sheet, β-turn and random coil increased after HHP. | [54] | |
| Eel surimi | Actin and Myosin | 400 MPa for 15 min at room temperature | 400 MPa, α-helix of actin significantly decreased, and β-sheet, β-turn and random coil increased; α-Helix and β-turn of myosin decreased, and random coil increased. | Our work (unpublished) |
|
| Red abalone (Haliotis rufescens) | Protein | 200, 300, 400 and 500 MPa for 5 min | The intermolecular β-sheet structure was disrupted at 200 MPa; the 310-helix structure significantly reduced at 300 MPa. β-turn was formed at 300, 400, and 500 MPa. | [28] | |
| Palm ruff species | Protein | 450 and 550 MPa for 3 and 4 min at ambient temperature | HHP reduced α-helix and increased β-sheet. | [55] |