Influence of different restorative materials on lysozyme and amylase activity of the salivary pellicle in situ

• Published in: Journal of biomedical materials research. Part A Vol. 78A; no. 4; pp. 755 - 761
• Main Authors: Hannig, Christian, Wasser, Mathias, Becker, Klaus, Hannig, Matthias, Huber, Karin, Attin, Thomas
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 15.09.2006
• Subjects: Adult; amylase; Amylases - metabolism; Dental Restoration, Permanent; enzymes; Humans; lysozyme; Male; Muramidase - metabolism; restorative materials; Salivary Glands - enzymology; Salivary Glands - secretion; salivary pellicle; Salivary Proteins and Peptides - metabolism
• ISSN: 1549-3296; 1552-4965
• DOI: 10.1002/jbm.a.30758

Lysozyme and amylase are the most abundant enzymatic components in the salivary pellicle. The purpose of the present study was to determine the influence of different substrata on amylase and lysozyme activity in salivary pellicles formed in situ. Slabs (5 mm diameter) of bovine dentine and enamel, of titanium, gold alloy, resin composite, PMMA, amalgam, and feldspar ceramic were fixed on the buccal sites of individual splints worn by six subjects for 30 min to allow pellicle formation. Thereafter, slabs were removed from the trays and rinsed with running water. Lysozyme activity was determined via lysis of Micrococcus lysodeicticus. Amylase activity was measured with a photometric method using 2‐chloro‐4‐nitrophenyl‐4‐O‐β‐D‐galactopyranosylmaltotriosid (GalG2CNP) as substrate. Both pellicle enzymes were evaluated in the immobilized as well as in the desorbed state. Salivary enzyme activities were also measured. All investigated pellicles exhibited lysozyme and amylase activity. Great intraindividual and interindividual differences were observed. Over all samples, immobilized amylase activity amounted to 0.65 ± 0.64 mU/cm2. Immobilized lysozyme activity was 5.04 ± 1.55 U/cm2. There were no major effects of the substratum on pellicle‐bound amylase and lysozyme activity. Immobilized and desorbed enzyme activities revealed a strong correlation (lysozyme: r = 0.700; amylase: r = 0.990). Salivary enzyme activities had only little impact on pellicle‐bound enzyme activities. Amylase and lysozyme are incorporated in the acquired in situ pellicle on different solid surfaces in an active conformation. Dental material and enzyme activity in the saliva have only little impact on enzymatic activity in the pellicle in situ. © 2006 Wiley Periodicals, Inc. J Biomed Mater Res, 2006