Effect of high‐pressure processing on myofibrillar protein structure

Modification of myofibrillar proteins induced by high‐pressure processing has been investigated at pressures ranging from 50 to 600 MPa for 10 min at 20 °C. Analysis by spectroscopic methods and circular dichroism of myofibrillar proteins in phosphate buffer pH 6.0 containing 0.6 M KCl showed no changes in the secondary structure of proteins. However, study of protein conformation by quasielastic light scattering and gel filtration chromatography proved the emergence of aggregation after treatment at pressures higher than 300 MPa. This aggregation was accompanied by enhanced binding of anilino‐1‐naphthalene‐8‐sulphonic acid, which indicated an increase in hydrophobic bonding of myofibrillar proteins. Modification of the tertiary and quaternary structures of proteins may induce a molten globule state.