Table 2.

Effects of HHP on myofibrillar gel.

Source	Protein	Treatment Conditions	Results	Reasons	References
Ice-bathed chicken breast meat	Myofibrillar	100, 150, 200, 250 and 300 MPa for 10 min Containing 0.3 M NaCl and 20 mM CaCl2	At 200 MPa (optimal pressure), the MP-Ca gel was strongest and the WHC was highest.	The solubilization of myosin heavy chain and actin increased, aggregation ability of MP reduced and the Tyr and Trp residues increased exposure (0.1 to 200 MPa).	[57]
Six-week-old commercial broilers	Myofibrillar	100, 200, 300, 400 and 500 MPa (±10 MPa) with a speed of 3.5 MPa/s for 10 min	At 200 MPa (optimal pressure), the MP gel was strongest.	The solubilization of MP increased below 200 MPa.	[26]
M. psoas from rabbits	Myosin	100–400 MPa at 20 °C for 10 min containing 0.6 M NaCl, pH 6.5	Gels were formed at 400 MPa.	Myosin was unfolded, resulting in exposure of hydrophobic groups, the heavy chain became very weak and associated to form gels.	[42]
Cod and turkey muscle	Myofibrillar/myosin	200–800 MPa for 20 min at ambient temperature	Pressure-induced myosin denaturation leads to very different gels to heat.	Disulfide bonds and hydrophobic interactions.	[58]
Bovine muscles (biceps femoris)	Myofibrillar	0–600 MPa for 0–1800 s	HHP can change the gel properties.	Surface hydrophobicity and reactive sulfhydryl groups increase around 450 MPa, which induced significant decreases in viscosity and solubility.	[59]
Live round tilapia (Orechromis niloticus)		50–300 MPa for 30 min	Above 200 MPa, Gels were softer, more viscous.	Hydrogen bonds and hydrophobic interactions.	[60]
Chicken breast meat	Myofibrillar	100, 200, 300, 400, 500 MPa (±10 MPa) for 10 min	200 MPa was the optimum pressure for the WHC of MP gel.	HHP caused more disulfide bond and stronger electrostatic repulsion, and hydrophobic interactions.	[44]
Tilapia (Oreochromis niloticus) surimi		0, 100, 200, 300, and 400 MPa for 15 min	Gels formed by pressurization were dense and flexible.	Disulfide bonds played a significant role in gel formation, and tyrosine residues involved in hydrogen bond formation with a lower intensity ratio.	[61]
Golden threadfin bream (Nemipterus virgatus)	Myosin contained deacetylated konjac glucomannan	100, 200, 300, 400 and 500 MPa (±15 MPa) for 5 min	Suitable pressure level (0.1–300 MPa) could improve thermal gelling ability and gelation properties.	Hydrophobic interactions were dominating mechanism to enhance gel strength.	[62]
Greater lizardfish (S. tumbil) surimi		Heating treatment (control), optimal high-pressure treatment (P), optimal MTGase treatment (M), MTGase combined with high pressure (MP), MTGase combined with setting, and high pressure (MSP)	MSP exhibited the highest gel strength, a higher water-holding capacity than the control sample.	Greater proportion of hydrogen bonds formed and non-disulfide covalent bonding catalyzed by MTGase under HHP.	[63]
Chicken breast meat (Musculus pectoralis major)	Myofibillar	Pressure/temperature:0.1, 200 or 400 MPa at 20 or 75 °C for 30 min	The gel induced by heating under pressure had a uniform porous microstructure and higher water-holding capacity.	High pressure in the HUP treatment prevented (HHP combined simultaneously with heating) myofibillar from being heat-denatured and reduced protein secondary structural transformation and hydrophobic residues exposure.	[64]