Protein Deposition on Sport Mouthguards and the Effectiveness of Two Different Cleaning Protocols

Author:

van Vliet Kirsten1,van Splunter Annina2,de Lange Jan1ORCID,Lobbezoo Frank3ORCID,Brand Henk2ORCID

Affiliation:

1. Academic Centre for Dentistry (ACTA)—Academic Medical Center Amsterdam (UMC), Department of Oral and Maxillofacial Surgery, 1081 HV Amsterdam, The Netherlands

2. Academic Centre for Dentistry (ACTA), Department of Oral Biochemistry, 1081 LA Amsterdam, The Netherlands

3. Academic Centre for Dentistry (ACTA), Department of Orofacial Pain and Dysfunction, 1081 LA Amsterdam, The Netherlands

Abstract

Objective: To determine which salivary proteins adhere onto sport mouthguards, and to evaluate the effectiveness of different cleaning strategies in removing deposited protein. Methods: Fifteen healthy volunteers used a mouthguard for 1 h. The deposited salivary proteins were analyzed using gel electrophoresis and Western blotting techniques and compared with the protein composition of unstimulated saliva. In addition, the effectiveness of two different cleaning strategies to remove proteins from the mouthguards were compared: rinsing the mouthguards after use with cold tap water and cleaning the mouthguard with a soluble effervescent tablet. Results: Gel electrophoresis showed deposition of proteins of 50–60 kDa and 14 kDa on the mouthguards used in the mouth for 1 h. Western blotting identified these bands as amylase and lysozyme, respectively. Rinsing the mouthguard with cold tap water after use removed 91% of the total amount of deposited proteins, while cleaning with an effervescent tablet removed 99%. Conclusions: During the use of mouthguards, salivary proteins are deposited on their surface. Because salivary proteins can potentially affect bacterial adhesion to mouthguards, proper cleaning after use is recommended. Cleaning the mouthguard with cold tap water or using an effervescent tablet both seem to be effective strategies to remove proteins deposited on sport mouthguards.

Publisher

MDPI AG

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