## Abstract 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 den
Detection of salivary α-amylase and lysozyme exposed on the pellicle formed in situ on different materials
✍ Scribed by Christian Hannig; Karin Huber; Ivo Lambrichts; Jan Gräser; Jan D'Haen; Matthias Hannig
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 223 KB
- Volume
- 83A
- Category
- Article
- ISSN
- 1549-3296
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✦ Synopsis
Abstract
Amylase and lysozyme are components of the salivary pellicle, exposing considerable enzymatic activity in the immobilized state. The purpose of the present study was to elucidate the influence of different solid substrata on the amount and distribution of amylase and lysozyme exposed on the surface of the salivary pellicle formed in situ. Slabs of titanium, feldspar ceramic, and bovine enamel were fixed on the buccal sites of individual splints worn by three subjects for 3 or 30 min, respectively, to allow pellicle formation. Subsequently, slabs were removed from the splints and rinsed with running water. Detection of amylase and lysozyme was performed by FEI‐SEM after gold‐immunolabeling of the enzymes. Both enzymes were found to be distributed randomly at the pellicle surface. Irrespective of formation time and substratum, significantly more labeled lysozyme molecules (5.23 ± 4.5 μm^−2^) were detected compared with amylase (3.4 ± 2.9 μm^−2^). Neither the substratum nor the pellicle formation time had significant impact on the amount of the respective enzyme that could be detected. This study for the first time provides evidence, that amylase and lysozyme are exposed at the surface of the salivary pellicle formed in situ on titanium and ceramics. Both enzymes are distributed randomly on the surface of the pellicle, irrespective of the underlying substratum. © 2007 Wiley Periodicals, Inc. J Biomed Mater Res 2007
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