Effect of ultrasound on protein functionality

The review focus on the effect of ultrasound on protein functionality. The presence of transient ultrasonic mechanical waves induce various sonochemical and sonomechanical effects on a protein. Sonochemical effects include the breakage of chains and/or the modification of side groups of aminoacids. Sonomechanical modifications by enhanced molecular agitation, might lead to the transient or permanent modification of the 3D structure of the folded protein. Since the biological function of proteins depends on the maintenance of its 3D folded structure, both sonochemical and sonomechanical effects might affect its properties. A protein might maintain its 3D structure and functionality after minor sonochemical effects, however, the enhanced mass transfer by sonomechanical effects might expose internal hydrophobic residues of the protein, making protein unfolding to an irreversible denatured state. Ultrasound enhanced mass transport effects are unique pathways to change the 3D folded structure of proteins which lead to a new functionality of proteins as support shield materials during the formation microspheres. Enzymes are proteins and their reactions should be conducted in a reactor set-up where enzymes are protected from sonic waves to maximize their catalytic efficiency. In this review, focused examples on protein dispersions/emulsions and enzyme catalysis are given.

Automated summary

The review focuses on the effect of ultrasound on protein functionality, with sonochemical and sonomechanical effects potentially leading to transient or permanent changes in protein structure. Sonomechanical effects, through enhanced mass transfer, can expose internal hydrophobic residues in proteins, resulting in protein unfolding to an irreversible denatured state.