Issue 83, 2016

High enzymatic activity preservation of malate dehydrogenase immobilized in a Langmuir–Blodgett film and its electrochemical biosensor application for malic acid detection

Abstract

In this study, malate dehydrogenase (MDH) enzyme was immobilized on a cation octadecylamine (ODA+) monolayer at the air–water interface. Pressure–area (πA) isotherm studies confirmed that the ODA–MDH system formed a stable monolayer at the air–water interface. The as-prepared MDH–ODA monolayer was transferred onto an indium tin oxide coated glass substrate (ITO) by the Langmuir–Blodgett (LB) method as an MDH–ODA/ITO LB film and characterized using FT-IR, SEM and UV-Vis absorption spectroscopy. The catalytic activity of the enzyme immobilized electrode (MDH–ODA/ITO) was assayed by sensing malic acid (MA) in the range of 10.0–50.0 mM. The high and preserved enzymatic activity of MDH in in vitro media was explored by following the absorbance (A340 nm) of nicotinamide adenine dinucleotide (NADH). Moreover, the highly sensitive electrochemical biosensor behavior of the MDA–ODA/ITO electrode for MA detection was displayed by cyclic voltammetry studies. The electrochemical studies revealed that a voltammetric current from the MDA–ODA/ITO electrode was obtained, while the ODA/ITO electrode did not show this current response. The MDA–ODA/ITO ​demonstrated sensitive electrochemical sensor ability for quantification of MA in both standard solutions and real samples.

Graphical abstract: High enzymatic activity preservation of malate dehydrogenase immobilized in a Langmuir–Blodgett film and its electrochemical biosensor application for malic acid detection

Supplementary files

Article information

Article type
Paper
Submitted
08 Jul 2016
Accepted
16 Aug 2016
First published
17 Aug 2016

RSC Adv., 2016,6, 79792-79797

High enzymatic activity preservation of malate dehydrogenase immobilized in a Langmuir–Blodgett film and its electrochemical biosensor application for malic acid detection

B. Gür, M. Işık, K. D. Kıranşan, M. Alanyalıoğlu, Ş. Beydemir and K. Meral, RSC Adv., 2016, 6, 79792 DOI: 10.1039/C6RA17465E

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