Protein structural changes during preparation and storage of surimi

The changes in protein structure associated with the preparation and frozen of surimi were investigated. Raw surimi was prepared by repeatedly washing Alaska pollock flesh with chilled water. The product was either slowly frozen or underwent rapid freezing using liquid air; in either case it was then subjected to frozen storage at-20 degrees C for 24 mo. Fourier transform infrared/attenuated total reflectance (FTIR/ATR) spectroscopy showed that during preparation of surimi, the alpha-helix content increased with increased number of washing cycles. Differential scanning calorimetry (DSC) revealed a shift in the thermal transition of actin to a higher temperature during surimi preparation. Electrophoresis, FTIR/ATR spectroscopy, and DSC results revealed a loss of myofibrillar proteins from surimi after 3 washing cycles, suggesting that 3 washing cycles were adequate to prepare surimi. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed relatively minor changes in protein subunit structure with some loss of the myosin light chains (MLC); myosin heavy chain (MHC), actin, and tropomyosin were found to be relatively stable. Native-PAGE showed no major changes in surimi after 24 mo storage at-20 degrees C. FTIR/ATR spectroscopy indicated a significant decrease in alpha-helix relative to beta-sheet structure in surimi after 2 y of storage at-20 degrees C. The loss alpha-helical content was more significant in slowly frozen surimi compared with rapid-frozen surimi samples. DSC results revealed a shift in the thermal transition of actin to lower temperatures during frozen storage of surimi.