Abstract
The molecular-mass distribution and amino acid composition of globular (albumin, lysozyme) and fibrillar (collagen) proteins subjected to treatment in electron-beam plasmas of various gases were experimentally studied. The samples were treated in the forms of powders and freeze-dried thin films. The electron-beam plasma treatment of powdered collagen resulted in the formation of low-molecular-mass compounds only. The modification of albumin and lysozyme was accompanied by polymerization of the proteins against the background of insignificant degradation. The plasma-stimulated processes occurred in the surface layer of powder particles, whereas the bulk of the sample remained intact. The degradation and polymerization processes in thin films of globular proteins occurred throughout the entire volume of the sample.
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