On December 15, 2001, Yourtee, D. M.; Smith, R. E.; Russo, K. A.; Burmaster, S.; Cannon, J. M.; Eick, J. D.; Kostoryz, E. L. published an article.Category: esters-buliding-blocks The title of the article was The stability of methacrylate biomaterials when enzyme challenged: kinetic and systematic evaluations. And the article contained the following:
This study addressed whether methacrylate monomers and polymers used in dentistry might degrade from enzymolysis by acetylcholinesterase (ACHE), cholesterol esterase (CHE), porcine liver esterase (PRLE), and a pancreatic lipase (PNL). Short (hour) and long-term (day) exposures were performed. Product ratios were used to determine surface hydrolysis of the polymeric materials. Enzyme kinetics were studied for the monomers when challenged by ACHE, CHE, and PRLE. In the case of PRLE, the Vmax for the dimethacrylate substrates varied slightly, but amounted to as much as 10% of that of p-nitrophenylacetate. The Km for triethylene glycol dimethacrylate (TEGDMA) was 197 μM for ACHE and 1107 μM for CHE. The Vmax was 2.7 nmol/min for ACHE and 3.5 nmol/min for CHE. TEGDMA was converted by CHE at 2% the rate of cholesteryl oleate. Long-term incubations of monomers with CHE and ACHE produced degrees of hydrolysis that evidenced structure dependency in the ability of the enzymes to effect hydrolysis. Particularly resistant were aromatic derivatives and those with branching in methacrylate linkages. Overall, the study confirms the ability of physiol. important esterases to catalyze the hydrolysis of biomaterial methacrylates. The experimental process involved the reaction of 2,2-Dimethylpropane-1,3-diyl bis(2-methylacrylate)(cas: 1985-51-9).Category: esters-buliding-blocks
The Article related to methacrylate biomaterial enzyme stability, Pharmaceuticals: Prosthetics and Medical Goods and other aspects.Category: esters-buliding-blocks
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