Structural modification by high-pressure homogenization for improved functional properties of freeze-dried myofibrillar proteins powder

- High-pressure homogenization (HPH) modified myofibrillar protein powder (MP-P).
- HPH induced protein dissociation, unfolding and rearrangement in MP-P.
- HPH produced amorphous protein structure with high thermal stability in MP-P.
- 15,000 psi HPH increased protein flexibility for enhanced functionalities in water.
- MP-P can be used as protein supplements in formulated food at low ionic strength.

To expand utilization of meat in various products, the structural, physicochemical and functional changes of water soluble myofibrillar protein powder (WSMP-P) were investigated as affected by high-pressure homogenization (HPH) intensities (0-20,000 psi). HPH modified the structure of WSMP-P by random dissociation (myofibril and myosin polymer dissociation), partial unfolding and rearrangement (actin trimer formation), producing an amorphous protein structure with high thermal stability. α-Helix and β-turn conversion to β-sheet structures occurred at pressures above 15,000 psi, suggesting an increase in myosin conformation flexibility with minor aggregation. Moreover, HPH was able to improve the water solubility and emulsifying properties of WSMP-P. This might be resulted from its unfolded flexible structure with submicron size and high surface net charge in aqueous suspensions induced by HPH. The findings regarding the improved functionality evidence potential of applying WSMP-P as protein supplements in formulated food or beverage at low ionic conditions.

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