Investigators at University of Toronto Describe Findings in Enzymes and Coenzymes (Biodegradation of composite resin with ester linkages: Identifying human salivary enzyme activity with a potential role in the esterolytic process)
By a News Reporter-Staff News Editor at Biotech Week -- Fresh data on Enzymes and Coenzymes are presented in a new report. According to news reporting out of Toronto, Canada, by NewsRx editors, research stated, "The ester linkages contained within dental resin monomers (such as Bisphenol A-glycidylmethacrylate (BisGMA) and triethylene glycol dimethacrylate (TEGDMA)) are susceptible to hydrolytic degradation by salivary esterases, however very little is known about the specific esterase activities implicated in this process. The objective of this work was to isolate and identify the dominant proteins from saliva that are associated with the esterase activities shown to be involved in the degradation of BisGMA."
Our news journalists obtained a quote from the research from the University of Toronto, "Human whole saliva was collected and processed prior to separation in a HiPrep 16/60 Sephacryl S-200 HR column. The fraction with the highest esterase activity was further separated by an anion exchange column (Mono-Q (10/100G)). Isolated fractions were then separated by gel electrophoresis, and compared to a common bench marker esterase, cholesterol esterase (CE), and commercial albumin which has been reported to express esterase activity. Proteins suspected of containing esterase activity were analyzed by Mass Spectroscopy (MS). Commercially available proteins, similar to the salivary esterase proteins identified by MS, were used to replicate the enzymatic complexes and confirm their degradation activity with respect to BisGMA. MS data suggested that the enzyme fraction with the highest esterase activity was contained among a group of proteins consisting of albumin, Zn-a2-glycoprotein, a-amylase, TALD01 protein, transferrin, lipocalin2, and prolactin-induced protein. Studies concluded that the main esterase bands on the gels in each fraction did not overlap with CE activity, and that albumin activity emerged as a lead candidate with significant esterase activity relative to BisGMA degradation, particularly when it formed a complex with Zn-a2-glycoprotein, under slightly basic conditions. Signcance."
According to the news editors, the research concluded: "These enzyme complexes can be used as a physiologically relevant formulation to test the biostability of composite resins."
For more information on this research see: Biodegradation of composite resin with ester linkages: Identifying human salivary enzyme activity with a potential role in the esterolytic process. Dental Materials, 2014;30(8):848-860. Dental Materials can be contacted at: Elsevier Sci Ltd, The Boulevard, Langford Lane, Kidlington, Oxford OX5 1GB, Oxon, England. (Elsevier - www.elsevier.com; Dental Materials - www.elsevier.com/wps/product/cws_home/601024)
Our news journalists report that additional information may be obtained by contacting K.H. Cai, University of Toronto, Toronto, ON, Canada. Additional authors for this research include Y. Delaviz, M. Banh, Y. Guo and J.P. Santerre (see also Enzymes and Coenzymes).
Keywords for this news article include: Toronto, Ontario, Canada, North and Central America, Dentistry, Enzymes and Coenzymes, Glycoconjugates, Glycoproteins
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