Collagen functional properties

FIGURE 7.1 Posttranslational modifications in collagen. (From Sikorski, Z.E., Proteins, in Chemical and Functional Properties of Food Components, Sikorski, Z.E., Ed., Technomic Publishing Co. Inc., PA, 1997. With permission.)... 

Investigative studies on the nonenzymatic glycosylation of collagen have elucidated several aspects of its effect in altering the structural and functional properties of collagens. In rats rendered diabetic, examination of tail... 

The interaction between proteases and their inhibitors is, at least by comparison with interactions which take place in food systems, a remarkably simple and straightforward association. Simple correlations of functional properties with different kinds of molecular forces cannot be made. It is possible, however, to illustrate the importance of protein structure and of protein—protein interactions as determinants of the functional properties of food proteins. I would like therefore to look at several food systems in which protein—protein or protein—other constituent interactions play a role and examine the relationship between functionality and protein structure in these systems. One of the simplest areas in which to examine this relationship is the well studied collagen-gelatin transition. 

Previously we have described a biodegradable polymeric template which can induce wound tissue to s)mthesize new skin (1,2). This template, a highly porous, cross-linked collagen-glycosamlnoglycan (CG) network, is currently used to treat excised skin wounds in patients who have suffered extensive burns (3,4). We now report certain structural and functional properties of the newly synthesized tissue. This preliminary characterization of the regrown organ suggests its close similarity to, as well as certain distinct differences from the intact skin adjacent to it. 

Viidik A (1973) Functional properties of collagenous tissues. Int Rev Connect Tissue Res 6 127-215... 

Other studies included the investigation of the stabilizing effect of sorbitol on hen egg white lysozyme and the use of the self-diffusion coefficient, D, to follow the solution and aggregative properties of lysozyme at different pH, temperature, and protein and salt concentrations. The properties of frozen ovalbumin solutions were studied by NMR relaxation spectroscopy. It is known that the functional properties of muscle proteins are affected by protein interactions with ions, and NMR was used to assess protein/water, protein/salt, and protein/protein interactions in myofibrillar protein solutions. Previous X-ray and NMR studies on collagen and peptides were reviewed by Mayo and, more recently, such types of system were characterized by high-resolution H and C NMR. °0 The structure, hydration state, and nature of the interactions between water and gelatin were determined by time domain NMR. ... 

Ranganayaki MD, Ranganathan TS, Jayaraman KS. A novel technique for the preparation of collagen derivatives for cosmetics. Part 3. Functional properties of collagen derivatives. 

Significant improvement of functional properties has been reported for fibers obtained from blends of chitin with various natural polymers such as cellulose, silk fibroin and glycosaminoglycans [48, 50, 51]. Fibers of chitosan blended with alginate, collagen and gelatin have been evaluated for wound dressing and artificial skin applications [52, 53, 108, 136]. 

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