Activity of lactoperoxidase when adsorbed on protein layers
(2008) In Talanta 76(5). p.1159-1164- 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 paperwe 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 2.9mg/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... (More)
- 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 paperwe 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 2.9mg/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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1229825
- author
- Haberska, Karolina LU ; Svensson, Olof ; Shleev, Sergey LU ; Lindh, Liselott ; Arnebrant, Thomas and Ruzgas, Tautgirdas LU
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Gold electrode, Ellipsometry, MUC5B, BSA, Lactoperoxidase, BSM
- in
- Talanta
- volume
- 76
- issue
- 5
- pages
- 1159 - 1164
- publisher
- Elsevier
- external identifiers
-
- wos:000259750800029
- scopus:50149088075
- pmid:18761171
- ISSN
- 1873-3573
- DOI
- 10.1016/j.talanta.2008.05.017
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004)
- id
- 885199b9-6301-4c70-b9fb-b0e598870f0f (old id 1229825)
- date added to LUP
- 2016-04-01 13:41:23
- date last changed
- 2022-01-27 20:31:45
@article{885199b9-6301-4c70-b9fb-b0e598870f0f,
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 paperwe 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 2.9mg/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.}},
author = {{Haberska, Karolina and Svensson, Olof and Shleev, Sergey and Lindh, Liselott and Arnebrant, Thomas and Ruzgas, Tautgirdas}},
issn = {{1873-3573}},
keywords = {{Gold electrode; Ellipsometry; MUC5B; BSA; Lactoperoxidase; BSM}},
language = {{eng}},
number = {{5}},
pages = {{1159--1164}},
publisher = {{Elsevier}},
series = {{Talanta}},
title = {{Activity of lactoperoxidase when adsorbed on protein layers}},
url = {{https://lup.lub.lu.se/search/files/3533274/1230000.pdf}},
doi = {{10.1016/j.talanta.2008.05.017}},
volume = {{76}},
year = {{2008}},
}