Application of zero-length cross-linking to form lysozyme, horseradish peroxidase and lysozyme–peroxidase dimers: Activity and stability

Succinimidyl Residue Formation in Hen Egg-White Lysozyme Favors the Formation of Intermolecular Covalent Bonds without Affecting Its Tertiary Structure

“…Dimerization of lysozyme during a thermal treatment in the solid state was recently reported. − Polyacrylamide gel electrophoresis under denaturing conditions confirmed that the dry-heating process applied in the present study (80 °C, up to 7 days, pH 3.5) results in covalent lysozyme dimers formation (Figure A). However, the original sample already contained a small amount of dimers, indicating that oligomerization might occur during protein purification, storage, or both; it could also result from a spontaneous process happening under physiological conditions, as suggested by the presence of lysozyme dimers in liquid egg white analyzed by 2D-PAGE after reduction and alkylation .…”

“…Recent studies showed that heating (80 °C) under vacuum a lysozyme powder obtained by freeze-drying a protein solution of which pH was adjusted to 7.0 resulted in dimer formation. ,, The proposed mechanism for the condensation of two amino acids is the formation of an amide linkage between a lysine residue and an acidic residue. This has been well demonstrated for RNase A .…”

Synthesis of Lysozyme–Metallacarborane Conjugates and the Effect of Boron Cluster Modification on Protein Structure and Function

“…It was shown that changes in the enzymatic activity of lysozyme dimers are directly associated with linker length. Directly coupled lysozyme dimers showed enzymatic activity similar to that of single molecules, whereas lysozyme dimers tethered with a linker showed significant increases in biological activity 45–47. At present there is lack of information about the influence of tethering to protein boron cluster(s) on biological activity for any other enzyme.…”