Sung H W, Chen W Y, Tsai C C, Hsu H L
Department of Chemical Engineering, National Central University, Chung-Li, Taiwan, Republic of China.
J Biomater Sci Polym Ed. 1997;8(8):587-600. doi: 10.1163/156856297x00191.
The study, using bacterial collagenase, was to investigate the changes in characteristics of a collagen-rich tissue, porcine pericardium, fixed by glutaraldehyde or epoxy compound (ethylene glycol diglycidyl ether) during the course of degradation. Fresh porcine pericardium was used as a control. During degradation, the heat released by the reaction of collagenase with a test sample was monitored by a highly sensitive microcalorimeter. Also, the degree of degradation of each test sample was determined by measuring its increment in free amino group content and changes in denaturation temperature and tensile strength. Microcalorimetric analysis of collagenase degradation of fresh, epoxy-fixed, and glutaraldehyde-fixed tissues revealed that the heat released during degradation correlates well with the degree of tissue degraded. The cleaving of peptide bonds in biological tissue by collagenase degradation may increase its free amino group content and reduce its denaturation temperature and tensile strength. It was noted that the fresh tissue cannot resist bacterial collagenase degradation, while the glutaraldehyde-fixed tissue had a relatively better resistance to degradation than its epoxy-fixed counterpart.
