Lysozyme impacts gel properties of egg white protein via electrostatic interactions, polarity differences, local pH regulation, or as a filler.

The effects of lysozyme on egg white gel properties and their underlying causes were investigated under comparison between lysozyme removed with ion exchange resin and three levels of commercial lysozyme powder (1/2, 2/2, 3/2 the natural concentration in egg white) re-added in the lysozyme-removed system. Results showed that a lysozyme-removed gel obtained the best water holding capacity (61.61 %), lowest cooking loss (11.85 %), and enhanced textural properties (hardness, 638.04 g; resilience, 0.57; and gumminess), which was attributed to lysozyme promoting protein aggregation and weakening electrostatic repulsion by charge neutralization and competition for water, and this could be eliminated by removing lysozyme. Besides, the stronger intermolecular interactions (enhanced ionic bonds, hydrogen bonds and inhibited hydrophobic interactions), the shorter transverse relaxation time (T21 and T22), as well as more uniform microstructure formed in the lysozyme-removed gel, allowing the gels to bind more water molecules. With return of lysozyme, the gel properties were weakened to varying degrees, which was also ascribed to the filling of lysozyme in gel matrix narrowed interspace for binding and storage of water. In sum, adjustment on the content of lysozyme can regulate the gel properties of egg white, so as to obtain gels with regulable gel quality and processing characteristics.

The last twenty residues in the head domain of mouse lamin A contain important structural elements for formation of head-to-tail polymers in vitro.

Nuclear lamins are a type of intermediate filament (IF) proteins. They have a characteristic tripartite domain structure with a alpha-helical rod domain flanked by non-alpha-helical N-terminal head and C-terminal tail domains. While the head domain has been shown to be important for the formation of head-to-tail polymers that are critical assembly intermediates for lamin IFs, essential structural elements in this domain have remained obscure. As a first step to remedy this, a series of mouse lamin A mutants in which the head domain (30 amino acid residues) was deleted stepwise from the N-terminus at intervals of 10 residues were bacterially expressed. The assembly properties in vitro of the purified recombinant proteins were explored by electron microscopy. We observed that while a lamin A mutant lacking N-terminal 10 residues formed head-to-tail polymers, a mutant lacking N-terminal 20 residues or the whole head domain (30 residues) showed significantly decreased potency to form head-to-tail polymers. These results suggest that the last 20 residues (from Arg-11 to Gln-30) of the head domain of mouse lamin A contain essential structures for the formation of head-to-tail polymers. The last 20 residues of the head domain include several conserved residues between A- and B-type lamins and also the phosphorylation site for cdc2 kinase, which affects lamin IF organization in vivo and in vitro. Our results provide clues to the molecular mechanism by which the head domain plays a crucial role in lamin polymerization.