Selective-Targeted Effect of High-Pressure Processing on Proteins Related to Quality: a Proteomics Evidence in Atlantic Mackerel (Scomber scombrus)

The effect of high hydrostatic pressure (HHP) treatment (150, 300, and 450 MPa for 0, 2.5, and 5 min) on total sodium dodecyl sulfate (SDS)-soluble and sarcoplasmic proteins in frozen (-10 A degrees C for 3 months) Atlantic mackerel (Scomber scombrus) was evaluated. Proteomics tools based on image analysis of SDS-polyacrylamide gel electrophoresis (SDS-PAGE) protein gels and protein identification by tandem mass spectrometry (MS/MS) were applied. Total SDS-soluble proteins, composed in high proportion of myofibrillar proteins, were stable under pressurization treatment in terms of solubility and electrophoretic gel profiles. However, pressurization reduced sarcoplasmic proteins' solubility, modified their one-dimensional (1-D)/two-dimensional (2-D) SDS-PAGE patterns in a direct-dependent manner, and exerted a selective effect on particular sarcoplasmic proteins depending on processing conditions. Thus, protein bands assigned to creatine kinase, fructose-bisphosphate aldolase A, glycogen phosphorylase, and beta-enolase were degraded at 300-450 MPa. Additionally, the stability of triosephosphate isomerase B, phosphoglucomutase, and phosphoglycerate kinase-1 was found to be HHP-reduced when submitted at 450 MPa. HHP processing (300-450 MPa) also induced a cross-linking product formation of pyruvate kinase and two compounds derived from tropomyosin at 450 MPa. Frozen storage time of pressurized samples induced an additional lessening in protein solubility, but electrophoretic patterns were not modified. The present investigation emphasizes the higher lability of sarcoplasmic proteins under HHP treatment and the important role of these proteins in the sensory quality enhancement provided by milder HHP conditions on frozen mackerel. HHP technology is expected to boost the development of novel tailored processing approaches to tackle food quality challenges.