Cross-linked demineralized dentin maintains its mechanical stability when challenged by bacterial collagenase.

The molecular structure, weight loss, and mechanical properties of demineralized dentin of noncrosslinked/crosslinked by glutaraldehyde (GA) were investigated when being challenged by bacterial collagenase solution over time in this study. Raman spectra proved that crosslinking occurred in demineralized dentin matrices after being treated with GA. Meanwhile, the weight of the cross-linked demineralized dentin matrices did not change after being challenged by bacterial collagenase solution up to 1 week. However, the weight of noncross-linked dentin collagen fell by almost 45% after degradation for 5 h, and up to 100% after 19 h. The tensile strength of demineralized dentin matrices did not show a significant change after being crosslinked, while the stiffness of demineralized dentin matrices showed more improvement than that of noncross-linked collagen. The toughness of demineralized dentin matrices decreased slightly after being crosslinked. Importantly, neither the tensile strength of GA-cross-linked demineralized dentin nor its stiffness changed over time in either control buffer or collagenase solution compared with that of noncross-linked controls. These results suggested that improving the degree of crosslinking in dentin collagen could be one method to inhibit its biodegradation and further to increase the durability of dental restorations.