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item MAFFIA, G
item Cooke, Peter
item Brown, Eleanor - Ellie

Submitted to: Journal of American Leather Chemists Association
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/31/2003
Publication Date: 4/1/2004
Citation: Maffia, G.J., Seltzer, M.A., Cooke, P.H., Brown, E.M. 2004. Collagen processing. Journal of American Leather Chemists Association. 99(4):164-169.

Interpretive Summary: Collagen, the protein in animal hides and skins, is a significant byproduct of the meat industry. On a laboratory scale, milled collagen dispersions are effective aids in the cleanup of waste water. An understanding of the effects of milling on collagen structure is essential for the design of a larger scale process. Characterization of the collagen before, during, and after the initial processing step established that no chemical changes had occurred. Physically, the strands of the collagen fiber were partially separated, resulting in increased surface area. This knowledge will be used in the development of a larger scale process for the production of collagen dispersions. The introduction of large-scale methods for conversion of waste collagen to bio-based dispersions for cleaning effluent streams will enable meatpackers and tanners to reduce waste disposal costs.

Technical Abstract: Collagen dispersions, produced from fibrils recovered from milled bovine collagen, have shown promise in environmental remediation in applications as settling aids, filtration aids, fractionation media, oil drop stabilizers, and water purification aids. Macroporous structures, processed by controlled lyophilization of collagen dispersions, are suitable as cell culturing substrates. Collagen was structurally characterized during milling to assist in designing a method for scale-up of the production process. In fact, although the initial processing involves a ball mill, the actual operation is more of an unraveling of the fiber to expose the fibrils, which have nanoscale dimensions. During the ball-milling step of production the active surface area of the collagen increases more than 200 times without chemically altering or denaturing the collagen. To demonstrate this throughout the milling process, active surface area per mass, fibril structure, molecular weight distribution, percent lipid, percent nitrogen, and percent ash were monitored.