title: Activity of lactoperoxidase when adsorbed on protein layers.
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 2.9mg/m(2). 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.
authors.affiliation: Biomedical Laboratory Science and Technology, Faculty of Health and Society, Malmö University, SE-205 06 Malmö, Sweden.
authors.forename: Karolina
authors.initials: K
authors.lastname: Haberska
authors.forename: Olof
authors.initials: O
authors.lastname: Svensson
authors.forename: Sergey
authors.initials: S
authors.lastname: Shleev
authors.forename: Liselott
authors.initials: L
authors.lastname: Lindh
authors.forename: Thomas
authors.initials: T
authors.lastname: Arnebrant
authors.forename: Tautgirdas
authors.initials: T
authors.lastname: Ruzgas