Identifying enzyme activities within human saliva which are relevant to dental resin composite biodegradation

• Published in: Biomaterials 2005-07, Vol.26 (20), p.4259-4264
• Main Authors: Lin, Benjamin A., Jaffer, Fayaaz, Duff, Missy D., Tang, Yi Wen, Santerre, J. Paul
• Format: Article
• Language: English
• Subjects: Biodegradation; Biodegradation, Environmental; Bone Cements - analysis; Bone Cements - chemistry; Composites; Enzyme Activation; Enzymes; Esterases - chemistry; Humans; Hydrolysis; Materials Testing; Monomers; Polymethyl Methacrylate - analysis; Polymethyl Methacrylate - chemistry; Resin; Resin Cements - analysis; Resin Cements - chemistry; Saliva; Saliva - chemistry; Saliva - enzymology
• ISSN: 0142-9612; 1878-5905
• DOI: 10.1016/j.biomaterials.2004.11.001

Esterase activities similar to those of cholesterol and pseudocholine esterases (CE and PCE, respectively) have been detected within whole human saliva. Since commercial CE has been shown to possess distinct activity relative to PCE for select components in dental composites, it is hypothesized that esterases isolated from human saliva will also show selectivity towards specific monomer elements within the composites. The objective of this work was to carry out the isolation of these activities from whole human saliva and study their individual effects on resin monomers such as Bis-phenyl glycidyl dimethacrylate (aromatic structure) and triethylene glycol dimethacrylate (hydrophilic structure), and on cured composites containing the latter monomers. Human saliva samples were processed, fractionated on a gel filtration column and assayed for CE and PCE-like activity. Selected fractions were incubated at 37 °C with the above monomers and select commercial composites. Degradation was monitored using high-performance liquid chromatography. The fraction with the highest cholesterol esterase-like character preferentially degraded the aromatic monomer and significantly degraded more of the composite's material relative to a fraction containing low amounts of the cholesterol esterase activity but elevated pseudocholine esterase-like activity. Hence, it was concluded that select salivary esterases had preferences for distinct composite resin components.