Amperometric biosensor for lactate analysis in wine and must during fermentation

Шкотова, Л. В.; Горюшкина, Т. Б.; Tran‐Minh, Canh; Chovelon, Jean‐Marc; Солдаткин, А. П.; Dzyadevych, S. V.

doi:10.1016/j.msec.2007.10.038

Cited by 49 publications

(37 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Several biosensors based on immobilized lactate oxidase (LOx) or LOx together with horseradish peroxidase were described Zaydan et al 2004;Mazzei et al 2007;Parra et al 2006;Shkotova et al 2008). Para et al developed lactate biosensor for the determination of this analyte in wine and beer using two strategies of immobilization of Lox-a direct adsorption and a covalent binding.…”

Section: Lactic Acidmentioning

confidence: 99%

Application of Enzyme Biosensors in Analysis of Food and Beverages

et al. 2011

View full text Add to dashboard Cite

The importance of analyses of different parameters in food products and monitoring of a production process requires quick and reliable analytical methods and devices. For this purpose, biosensors can be a suitable option, whereas most of the current quality control techniques are time consuming, expensive, and unpractical. In this paper, we describe biosensors developed for analysis of different components present in food samples, namely, glucose, fructose, sucrose, lactose, lactic, malic, acetic, ascorbic, citric and amino acids, ethanol, glycerol, and triglyceride. Biosensors showed desirable sensitivity, selectivity, and response time required for various applications. They are often designed to avoid interference from components present in a complex sample to be analyzed.

show abstract

Section: Lactic Acidmentioning

confidence: 99%

Application of Enzyme Biosensors in Analysis of Food and Beverages

et al. 2011

View full text Add to dashboard Cite

show abstract

“…An important biocompound that is in need of reliable monitoring is l-lactate. Biosensor applications for the determination of l-lactate range from biotechnology (food quality control [13], cell culture monitoring [14]) to monitoring different aspects of human health [15]. Some previous examples for the amperometric biosensing of l-lactate have been described using l-lactate oxidases (FMNdependent) and l-lactate dehydrogenases (NAD + -dependent) from various natural sources.…”

Section: Introductionmentioning

confidence: 99%

Comparative study of three lactate oxidases from Aerococcus viridans for biosensing applications

Taurino

Reiss

Richter

et al. 2013

Electrochimica Acta

View full text Add to dashboard Cite

Keywords:l-Lactate oxidases from Aerococcus viridans Engineered and commercial enzymes Multi-walled carbon nanotubes Enzyme biosensor a b s t r a c t A comparison between engineered and commercially available l-lactate oxidases from Aerococcus viridans was conducted for biosensing applications. Enzymes were adsorbed onto the surfaces of graphite electrodes modified with multi-walled carbon nanotubes. Thermostable l-lactate oxidases were cloned with a (i) N-, (ii) a C-terminal His-tag and (iii) a wild-type enzyme. Subsequently to the heterologous expression in Escherichia coli and purification, we determined the kinetic parameters of these enzymes in solution. The kinetics of the wild-type, of the N-terminally His-tagged enzyme and of the commercial l-lactate oxidase from A. viridans were studied with a classical Michaelis-Menten as well as with a substrate inhibition model, while the enzyme carrying a C-terminal His-tag showed no activity. The active enzymes were used to fabricate and comparatively investigate multi-walled carbon nanotubes-based biosensors. The enzyme kinetic results were compared with electrochemical studies. By using both spectrophotometric and amperometric techniques, the inhibition phenomenon fits better to the data especially those data related with Lox-His-N. The electrochemical data of the fabricated enzymatic biosensors showed that the N-terminally His-tagged l-lactate oxidase performed best on carboxyl-modified carbon nanotubes. The sensor based on this engineered enzyme showed the highest sensitivity and lowest detection limit in the range of l-lactate concentration 0-1 mM as well as long term stability over one month.

show abstract

“…27 In the food industry, L-lactate determination is used for control of fermentation and for quality control of several products such as tomato sauces, fruits, juices, milk and wine. 28,29 In order to achieve low detection times at low costs, L-lactate oxidase from Pediococcus species has been used by many laboratories in the construction of lactate oxidase-based bioelectrocatalytic systems. 30 The enzyme has the advantage of high specificity over other enzymes used for lactate determination.…”

Section: Lactate Oxidasementioning

confidence: 99%

Facilitating electron transfer in bioelectrocatalytic systems

Sekretaryova¹

2016

View full text Add to dashboard Cite

During the course of the research underlying this thesis, Alina Sekretaryova was enrolled in Forum Scientium, a multidisciplinary doctoral programme at Linköping University, Sweden Alina Sekretaryova, 2016, unless otherwise noted. Cover design by Alina Sekretaryova Linköping studies in science and technology Dissertation No. 1738 Printed in Sweden by LiU-Tryck, Linköping, Sweden, 2016 iii ABSTRACT Bioelectrocatalytic systems are based on biological entities, such as enzymes, whole cells, parts of cells or tissues, which catalyse electrochemical processes that involve the interaction between chemical change and electrical energy. In all cases, enzymes, isolated or residing inside cells or part of cells, implement biocatalysis. Electron transfer phenomena, within the protein molecules and between biological redox systems and electronics, enable the development of various bioelectrocatalytic systems, which can be used both for fundamental investigations of enzymatic biological processes by electrochemical methods and for applied purposes, such as power generation, bioremediation, chemical synthesis and biosensing.Electrical communication between the biocatalysts redox centre and an electrode is essential for the functioning of the system. This can be established using two main mechanisms: indirect electron transfer and direct electron transfer. The efficiency of the electron transfer influences important parameters such as the turnover rate of the biocatalyst, the generated current density and partially the stability of the system. These in turn determine the response time, sensitivity, detection limit and operational stability of biosensors or the power densities and current output of biofuel cells, and hence they should be carefully considered when designing bioelectrocatalytic systems.This thesis focuses on approaches that facilitate electron transfer in bioelectrocatalytic systems based on mediated and direct electron transfer mechanisms. Both fundamental aspects of electron transfer in bioelectrocatalytic systems and applications of such systems for biosensing and power generation are considered. First, a new hydrophobic mediator for oxidases, unsubstituted phenothiazine, and its improved electron transfer properties in comparison with commonly used mediators are discussed. Application of the mediator in electrochemical biosensors is demonstrated by glucose, lactate and cholesterol sensing. Utilisation of mediated biocatalytic cholesterol oxidation as the anodic reaction for the construction of a biofuel cell, acting as a power supply and an analytical device at the same time, is investigated as a "self-powered" biosensor. In addition, the enhancement of mediated bioelectrocatalysis by the employment of microelectrodes as a transducer is examined. The effect of surface roughness on the current response of the microelectrodes under conditions of convergent diffusion is considered. The applicability of the laccase-based system for total phenol analysis of weakly supported water is demonstrated. Finally, a...

show abstract

Amperometric biosensor for lactate analysis in wine and must during fermentation

Cited by 49 publications

References 26 publications

Application of Enzyme Biosensors in Analysis of Food and Beverages

Application of Enzyme Biosensors in Analysis of Food and Beverages

Comparative study of three lactate oxidases from Aerococcus viridans for biosensing applications

Facilitating electron transfer in bioelectrocatalytic systems

Contact Info

Product

Resources

About