Abstract
The effect of high-pressure processing (HPP) (150, 300 and 450MPa for 0, 2.5 and 5min) on total sodium dodecyl sulphate (SDS)-soluble and sarcoplasmic proteins in frozen (−10°C for 3months) horse mackerel (Trachurus trachurus) was evaluated. Proteomics tools based on image analysis of SDS–PAGE protein gels and protein identification by tandem mass spectrometry (MS/MS) were applied. Although total SDS-soluble fraction indicated no important changes induced by HPP, this processing modified the 1-D SDS–PAGE sarcoplasmic patterns in a direct-dependent manner and exerted a selective effect on particular proteins depending on processing conditions. Thus, application of the highest pressure (450MPa) provoked a significant degradation of phosphoglycerate mutase 2, glycogen phosphorylase muscle form, pyruvate kinase muscle isozyme, beta-enolase and triosephosphate isomerase and phosphoglucomutase-1. Conversely, protein bands assigned to tropomyosin alpha-1 chain, fast myotomal muscle troponin T and parvalbumin beta 2 increased their intensity after applying a 450-MPa processing.
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