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Activity of lactoperoxidase when adsorbed on protein layers
Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).ORCID iD: 0000-0001-6421-2158
Malmö högskola, Faculty of Odontology (OD).
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2008 (English)In: Talanta: The International Journal of Pure and Applied Analytical Chemistry, ISSN 0039-9140, E-ISSN 1873-3573, Vol. 76, no 5, p. 1159-1164Article in journal (Refereed) Published
Abstract [en]

Lactoperoxidase (LPO) is an enzyme, which is used as an antimicrobial agent in a number of applications, e.g., food technology. In the majority of applications LPO is added to a homogeneous product phase or immobilised on product surface. In the latter case, however, the measurements of LPO activity are seldom reported. In this paper we have assessed LPO enzymatic activity on bare and protein modified gold surfaces by means of electrochemistry. It was found that LPO rapidly adsorbs to bare gold surfaces resulting in an amount of LPO adsorbed of 2.9 mg/m2. A lower amount of adsorbed LPO is obtained if the gold surface is exposed to bovine serum albumin, bovine or human mucin prior to LPO adsorption. The enzymatic activity of the adsorbed enzyme is in general preserved at the experimental conditions and varies only moderately when comparing bare gold and gold surface pretreated with the selected proteins. The measurement of LPO specific activity, however, indicate that it is about 1.5 times higher if LPO is adsorbed on gold surfaces containing a small amount of preadsorbed mucin in comparison to the LPO directly adsorbed on bare gold.

Place, publisher, year, edition, pages
Elsevier, 2008. Vol. 76, no 5, p. 1159-1164
Keywords [en]
Lactoperoxidase, Ellipsometry, Gold electrode, BSM, BSA, MUC5B, Ellipsometry, Gold electrode
National Category
Dentistry
Identifiers
URN: urn:nbn:se:mau:diva-14853DOI: 10.1016/j.talanta.2008.05.017ISI: 000259750800029PubMedID: 18761171Scopus ID: 2-s2.0-50149088075Local ID: 6830OAI: oai:DiVA.org:mau-14853DiVA, id: diva2:1418374
Available from: 2020-03-30 Created: 2020-03-30 Last updated: 2024-02-05Bibliographically approved
In thesis
1. Interactions of Mucins with Biopolymers and Drug Delivery Particles
Open this publication in new window or tab >>Interactions of Mucins with Biopolymers and Drug Delivery Particles
2008 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The main components in the mucous gels apart from water are mucins, which are proteins with high molecular weights and an abundance of negatively charged oligosaccharide side chains. The aim of the investigations was to characterize interactions between mucins and other proteins that are present in the mucous gel, and also between mucins and components used in pharmaceutical formulations. More specifically, the main objectives were (I) to investigate the possibility to assemble multilayer films with mucins and oppositely charged polymers or proteins on solid substrates; (II) to evaluate mucoadhesive proper-ties of drug delivery particles by examination of their interactions with mucins. The construction of multilayer films was performed on silica and hydrophobized silica surfaces by alternate adsorption, and the adsorbed amount and thickness of the films were measured in situ by time resolved ellipsometry. It was demonstrated that films could be assembled using mucins in combination with both chitosan and lactoperoxidase. The build-up was characterized by adsorption and redissolution processes, and the extent of redissolution could be explained by taking the charge densities and concentrations of the components into account. It was also demonstrated that the nature of the substrate can be crucial for the possibilities to assemble multilayer films, and from the results it may be concluded that a high amount of mucin in the first step is important for successful layer-by-layer assembly. Furthermore, it was demonstrated that lactoperoxidase is catalytically active when adsorbed to mucin layers, and it may thereby exert its antimicrobial action. The evaluation of mucoadhesive properties of drug delivery particles was performed with lipid nanoparticles stabilized by a poly(ethylene oxide) based polymer and with particles modified by chitosan. Both types of model particles (unmodified and chitosan modified) were investigated by measuring their adsorption to mucin-coated silica surfaces by ellipsometry. It was shown that the binding of unmodified particles to mucin-coated silica surfaces was weak and pH-dependent. Based on the pH and electrolyte dependence of the adsorption, it was proposed that the interaction is mediated by hydrogen bonding between protonated carboxyl groups in the mucin molecule and oxygen atoms in poly(ethylene oxide). Chitosan modified particles, on the other hand, showed a substantial and strong binding to mucin-coated surfaces, which can probably be attributed to interactions between amino groups in chitosan and negatively charged groups in the mucin layer. The findings from the present investigations are in agreement with previous reports on the interaction of mucins with poly(ethylene oxide) and chitosan. It can therefore be concluded that the methodology applied is useful for evaluating mucoadhesive properties of nanoparticles.

Place, publisher, year, edition, pages
Malmö University, 2008
Series
Malmö University Health and Society Dissertations, ISSN 1653-5383
Keywords
mucin, chitosan, lactoperoxidase, multilayer, mucoadhesion, nanoparticles, ellipsometry
National Category
Physical Chemistry
Identifiers
urn:nbn:se:mau:diva-7339 (URN)5930 (Local ID)978-91-7104-212-5 (ISBN)5930 (Archive number)5930 (OAI)
Note

Note: The papers are not included in the fulltext online.

Paper III and V in dissertation as manuscript, paper IV as accepted manuscript.

Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2024-03-05Bibliographically approved

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Svensson, OlofShleev, SergeyLindh, LiselottArnebrant, ThomasRuzgas, Tautgirdas

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Talanta: The International Journal of Pure and Applied Analytical Chemistry
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