Abstract
Summary
1) The use of hide powder as a substrate in the demonstration of collagenase activity is not valid.
2) Collagens from several sources, prepared by methods designed not to alter properties, are resistant to the action of trypsin, chymotrypsin, and papain. The collagens are readily attacked (solubilized) by the proteolytic enzyme(s) of CI. histolyticum and by pepsin. The proteolytic enzyme(s) of CI. perfringens filtrates are 10-20-fold weaker than those of CI. histolyticum filtrates in the degradation of collagen.
3) The reported increased solubilization of collagens in water at the shrinkage temperature (68-70°C) after incubation with enzymes can be attributed to residual enzyme.
4) Denaturation of collagen by heat and urea produces a general susceptibility to common proteolytic enzymes.
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