Kinetic models of horseradish peroxidase action on a graphite electrode

Ruzgas, Tautgirdas; Gorton, Lo; Emnéus, Jenny; Markó-Varga, György

doi:10.1016/0022-0728(95)03930-f

Cited by 223 publications

(136 citation statements)

References 41 publications

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“…To study the electrochemical properties of electrode-immobilized TOP, we used a method proposed by Ruzgas et al [11]. The method is based on studying the dependence of the kinetic component of current on the concentrations of hydrogen peroxide and an electrondonor substrate.…”

Section: Principles Of the Electrochemical Detection Of Peroxidasesmentioning

confidence: 99%

“…This is an electrochemical analog of a classical method of steady-state enzyme kinetics. Technically, this experiment can be performed either at a rotating disk electrode [11] or under flow conditions [12]. The developed approach is based on a comparison between direct electron transfer and mediated electron transfer at the same electrode.…”

Section: Principles Of the Electrochemical Detection Of Peroxidasesmentioning

confidence: 99%

“…The developed approach is based on a comparison between direct electron transfer and mediated electron transfer at the same electrode. Figure 1 shows the dependence of kinetic current on hydrogen peroxide concentration in double inverse coordinates for native TOP in the absence and in the presence of a mediator (direct electron transfer and mediated electron transfer modes, respectively) [11]. The rate constants of the elementary half reactions of immobilized peroxidase oxidation by hydrogen peroxide (Eq.…”

Section: Principles Of the Electrochemical Detection Of Peroxidasesmentioning

confidence: 99%

“…In addition to the fundamental studies of natural glycosylated TOP performed in 1996-1999 [3][4][5][6], which demonstrated a number of practically promising properties of this enzyme, the new enzyme was also tested for analytical purposes [7][8][9][10][11][12][13][14][15][16][17][18][19][20].…”

mentioning

confidence: 99%

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Tobacco Peroxidase as a New Reagent for Amperometric Biosensors

et al. 2005

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Section: Principles Of the Electrochemical Detection Of Peroxidasesmentioning

confidence: 99%

Section: Principles Of the Electrochemical Detection Of Peroxidasesmentioning

confidence: 99%

Section: Principles Of the Electrochemical Detection Of Peroxidasesmentioning

confidence: 99%

mentioning

confidence: 99%

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Tobacco Peroxidase as a New Reagent for Amperometric Biosensors

et al. 2005

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“…In this work LPO adsorption was studied on gold substrates which due to the electrical conductivity provide possibilities to measure the activity of surface bound LPO by electrochemical means, as illustrated by Fig. 1 (described in Section 3.3), based on our earlier electrochemical studies of peroxidases [16,17].…”

Section: Adsorption Of Lactoperoxidase On Bare Gold Surfacesmentioning

confidence: 99%

Activity of lactoperoxidase when adsorbed on protein layers

Haberska

Svensson

Shleev

et al. 2008

Talanta

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This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues.Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. Contents lists available at ScienceDirect Talanta j o u r n a l h o m e p a g e : w w w . e l s e v i e r . c o m / l o c a t e / t a l a n t a b s t r a c tLactoperoxidase (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/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.

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Redoxproteinschichten auf leitenden Trägern – Systeme für bioelektronische Anwendungen

Willner

Katz

2000

Angewandte Chemie

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Kinetic models of horseradish peroxidase action on a graphite electrode

Cited by 223 publications

References 41 publications

Tobacco Peroxidase as a New Reagent for Amperometric Biosensors

Tobacco Peroxidase as a New Reagent for Amperometric Biosensors

Activity of lactoperoxidase when adsorbed on protein layers

Redoxproteinschichten auf leitenden Trägern – Systeme für bioelektronische Anwendungen

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