Abstract

Chromium(III) sulfate is extensively used in leather processing to stabilize the collagen molecules in hides and skins. Although its excess usage causes severe environmental pollution and health concerns, the role of chromium in stabilizing collagen still remains poorly understood. For the first time, by integrating a number of techniques, including real-time small-angle X-ray scattering, differential scanning calorimetry and natural cross-link analysis, we reveal crucial molecular-level indicators of collagen stability. The results indicate that collagen molecules achieve maximum molecular stability at concentrations as low as 1.8 wt % even if excess chromium (>3.7%) is introduced into the collagen matrix. At low concentrations (1.8% to 3.7%), the active amino acid residues are saturated via covalent bonding with chromium. Any excess chromium interacts purely non-covalently with the collagen molecule and, we propose, can be substituted by environment-friendly alternatives. Further, important natural cros...

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