Biosensor for acrylamide based on an ion-selective electrode using whole cells of<i>Pseudomonas aeruginosa</i>containing amidase activity

Silva, Nelson A. F.; Gil, Dulce M. A.; Karmali, Amin; Matos, M.

doi:10.1080/10242420802604964

Cited by 35 publications

(16 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…detoxification of nitriles/amide containing industrial effluent Bigey et al (1999), Thompson et al (1988) Peptide synthesis Peptide amidase -modify side chains of amino acids Silva et al (2009) in the living world is not clearly understood and requires further investigation. In the present review some biochemical characteristics, mechanism of action and possible applications of amidases will be reviewed (see Table 1).…”

Section: Amino Acidsmentioning

confidence: 99%

Amidases: versatile enzymes in nature

Sharma

Bhalla

2009

Rev Environ Sci Biotechnol

View full text Add to dashboard Cite

Amidases are ubiquitous enzymes and biological functions of these enzymes vary widely. In past five decades, they turned out to be an attractive tool in industries for the synthesis of wide variety of carboxylic acids, hydroxamic acids and hydrazide, which find applications in commodity chemicals synthesis, pharmaceuticals agrochemicals and waste water treatments etc. Their proteins structures revealed that aliphatic amidases share the typical a/b hydrolase fold (like nitrilase superfamily) and signature amidases are evolutionary related to aspartic proteinases. They hydrolyse wide variety of amides (short chain aliphatic amides, mid-chain amides, arylamides, a-aminoamides and a-hydroxyamides) and can be grouped on the basis of their catalytic site and preferred substrate. They resist denaturation at extreme of pH and temperature because of their strong and compact multimeric structures. Inhibition studies and three-dimensional analysis of the structures identified a Glu59, Lys134, Cys166 catalytic triad and follow ''Bi-bi Ping-Pong'' mechanism reaction for amide hydrolysis and acyl transferase reactions. Many recombinant amidases have been expressed in Escherichia coli as well as in Brevibacterium lactofermentum.

show abstract

Section: Amino Acidsmentioning

confidence: 99%

Amidases: versatile enzymes in nature

Sharma

Bhalla

2009

Rev Environ Sci Biotechnol

View full text Add to dashboard Cite

show abstract

“…The reduction of the concentration of oxygen and the current created from the metabolism of AA could be used to detect AA. Silva, Gil, Karmali, andMatos (2009), Silva, Matos, Karmali, andRocha (2011) designed an electrochemical biosensor based on the electron transfer of a direct biochemical interaction between AA and whole cells of Pseudomonas aeruginosa containing intracellular amidase, which catalyzed the hydrolysis of AA producing ammonium ion and acrylic acid. Using biochemical reactions from microbial metabolism can lead to real-time detection of AA.…”

Section: Electrochemical Biosensing Methodsmentioning

confidence: 99%

Rapid methods for detecting acrylamide in thermally processed foods: A review

et al. 2015

Food Control

View full text Add to dashboard Cite

“…Very recently, one of the authors has demonstrated that whole cells containing amidase activity can be immobilized on a membrane but still retain their catalytic activity. 5 On the other hand a number of ammonium selective membranes have been used with success in CHEMFETs which means it may be possible to detect acrylamide levels via ammonium ions. However, before progressing further, it is important to estimate the impact of the membrane in the voltage-current characteristics of an amorphous semiconductor device and on the sensor sensitivity.…”

Section: Membranementioning

confidence: 99%

Membrane Selectivity versus Sensor Response in Hydrogenated Amorphous Silicon CHEMFETs Using a Semi-Empirical Model

Costa

Fernandes

Vieira³

et al. 2011

J. Nanosci. Nanotech.

View full text Add to dashboard Cite

Toxic amides, such as acrylamide, are potentially harmful to Human health, so there is great interest in the fabrication of compact and economical devices to measure their concentration in food products and effluents. The CHEmically Modified Field Effect Transistor (CHEMFET) based onamorphous silicon technology is a candidate for this type of application due to its low fabrication cost. In this article we have used a semi-empirical modelof the device to predict its performance in a solution of interfering ions. The actual semiconductor unit of the sensor was fabricated by the PECVD technique in the top gate configuration. The CHEMFET simulation was performed based on the experimental current voltage curves of the semiconductor unit and on an empirical model of the polymeric membrane. Results presented here are useful for selection and design of CHEMFET membranes and provide an idea of the limitations of the amorphous CHEMFET device. In addition to the economical advantage, the small size of this prototype means it is appropriate for in situ operation and integration in a sensor array.

show abstract

Biosensor for acrylamide based on an ion-selective electrode using whole cells ofPseudomonas aeruginosacontaining amidase activity

Cited by 35 publications

References 21 publications

Amidases: versatile enzymes in nature

Amidases: versatile enzymes in nature

Rapid methods for detecting acrylamide in thermally processed foods: A review

Membrane Selectivity versus Sensor Response in Hydrogenated Amorphous Silicon CHEMFETs Using a Semi-Empirical Model

Contact Info

Product

Resources

About