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.

Laccases (benzene diol: oxidoreductases, EC 1.10.3.2) are able to catalyze the oxidation of various compounds containing phenolic and aniline structures using dissolved oxygen in water. Laccase structural features and catalytic mechanisms focused on the polymerization of aromatic compounds are reported. A description about the most recent research on the biosynthesis of chemicals and polymers is made. Selected applications of this technology are considered as well as the advantages, shortcomings and future needs related with the use of laccases.

In this work a process for the bio-coloration of bacterial cellulose (BC) membranes was developed. Laccase from Myceliophthora thermophila was immobilized onto BC membranes and retained up to 88% of residual activity after immobilization. Four compounds belonging to the flavonoids family were chosen to test the in situ polymerase activity of immobilized laccase. All the flavonoids were successfully polymerized by laccase giving rise to yellow, orange and dark brown oligomers which conferred color to the BC support. The optimal bio-coloration conditions were studied for two of the tested flavonoids, catechol and catechin, by varying the concentration and time of incubation. High color depth and resistance to washing were obtained for both compounds. The highly porous bacterial cellulose material demonstrated great performance as a bio-coloration support, in contrast to other materials cited in literature, like cotton or wool. The process developed is presented as an environmentally friendly alternative for bacterial cellulose bio-coloration and will contribute deeply for the development of new fashionable products within this material.