Activity of lactoperoxidase when adsorbed on protein layers

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Activity of lactoperoxidase when adsorbed on protein layers

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Publication Article, peer reviewed scientific
Title Activity of lactoperoxidase when adsorbed on protein layers
Author(s) Haberska, Karolina ; Svensson, Olof ; Shleev, Sergey ; Lindh, Liselott ; Arnebrant, Thomas ; Ruzgas, Tautgirdas
Date 2008
English abstract
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.
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Publisher Elsevier B.V.
Host/Issue Talanta;5
Volume 76
ISSN 0039-9140
Pages 1159-1164
Language eng (iso)
Subject(s) Lactoperoxidase; BSM; BSA; MUC5B; Ellipsometry; Gold electrode
Gold electrode
Research Subject Categories::NATURAL SCIENCES
Research Subject Categories::ODONTOLOGY
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