Common blue mussel (Mytilus edulis) is a sessile organism that has unique ability to attach to a wide array of organic and inorganic marine surfaces using its holdfast structures. Strong adhesion to surfaces is essential for mussel survival, movement, and self-defense. Mussel proteins from byssal thread are structural components connecting soft mussel tissues to marine surfaces via an adhesive plaque in the distal end, while adhesive proteins from byssal plaque are responsible for mussel adhesion. Adhesive proteins are small molecules containing a high proportion of post-translationally modified amino acids such as 3,4-dihydroxyphenylalanine (DOPA). High DOPA content, small molecular size, protein flexibility, the presence of metal ions, and a high oxidation state enable strong mussel adhesion to surfaces. Mussel adhesion mechanisms depend on the composition and interactions of mussel proteins, as well as their interactions with the environment. Difficulties in the extraction of mussel adhesion proteins hamper mechanism studies and their practical applications. Development of recombinant mussel proteins and biomimetics will advance our understanding of adhesion mechanisms. In this paper, recent advances in the characterization of mussel adhesive proteins (MAPs), mussel adhesion mechanisms, application of MAPs, and the development of biomimetic biopolymers are reviewed.

With the constant increase in protein demand globally, it is expedient to develop a strategy to effectively utilize protein, particularly those extracted from plant origin, which has been associated with low digestibility, poor techno‐functional properties, and inherent allergenicity. Several thermal modification approaches have been developed to overcome these limitations and showed excellent results. Nevertheless, the excessive unfolding of the protein, aggregation of unfolded proteins, and irregular protein crosslinking have limited its application. Additionally, the increased consumer demand for natural products with no chemical additives has created a bottleneck for chemical‐induced protein modification. Therefore, researchers are now directed toward other nonthermal technologies, including high‐voltage cold plasma, ultrasound, high‐pressure protein, etc., for protein modification. The techno‐functional properties, allergenicity, and protein digestibility are greatly influenced by the applied treatment and its process parameters. Nevertheless, the application of these technologies, particularly high‐voltage cold plasma, is still in its primary stage. Furthermore, the protein modification mechanism induced by high‐voltage cold plasma has not been fully explained. Thus, this review meets the necessity to assemble the recent information on the process parameters and conditions for modifying proteins by high‐voltage cold plasma and its impact on protein techno‐functional properties, digestibility, and allergenicity.