Abstract
Denaturation temperature of pepsin-treated collagen from calf skin was measured viscometrically in neutral pH solution by adding glucose which completely depresses collagen fibril formation without denaturing collagen molecules.
The stability of collagen molecules in solution thus obtained was greater at neutral pH than at either acidic or basic pH. The capability of renaturation from denatured state was also highest at neutral pH. The renaturation of denatured collagen molecules seemed even more sensitive to pH of the solution than the denaturation of native ones.
