The use of Fourier transform infrared spectroscopy to assay for urease from Pseudomonas aeruginosa and Canavalia ensiformis

Karmali, K.; Karmali, Amin; Teixeira, Ana Clara Monte; Curto, M.J Marcelo

doi:10.1016/j.ab.2004.04.020

Cited by 14 publications

(9 citation statements)

References 21 publications

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“…However, substrate as well as product must have different spectra. FTIR spectroscopy also enables enzyme kinetics investigation [78]. Attenuated Total Reflection Fourier Transform Infrared (ATR-FTIR) spectroscopy was recommended to enzymatic activity analysis [79].…”

Section: Methods For Detecting Of Ureolytic Activitymentioning

confidence: 99%

Bacterial Urease and its Role in Long-Lasting Human Diseases

Konieczna

Żarnowiec²,

Kwinkowski³

et al. 2012

CPPS

232

155

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Urease is a virulence factor found in various pathogenic bacteria. It is essential in colonization of a host organism and in maintenance of bacterial cells in tissues. Due to its enzymatic activity, urease has a toxic effect on human cells. The presence of ureolytic activity is an important marker of a number of bacterial infections. Urease is also an immunogenic protein and is recognized by antibodies present in human sera. The presence of such antibodies is connected with progress of several long-lasting diseases, like rheumatoid arthritis, atherosclerosis or urinary tract infections. In bacterial ureases, motives with a sequence and/or structure similar to human proteins may occur. This phenomenon, known as molecular mimicry, leads to the appearance of autoantibodies, which take part in host molecules destruction. Detection of antibodies-binding motives (epitopes) in bacterial proteins is a complex process. However, organic chemistry tools, such as synthetic peptide libraries, are helpful in both, epitope mapping as well as in serologic investigations. In this review, we present a synthetic report on a molecular organization of bacterial ureases - genetic as well as structural. We characterize methods used in detecting urease and ureolytic activity, including techniques applied in disease diagnostic processes and in chemical synthesis of urease epitopes. The review also provides a summary of knowledge about a toxic effect of bacterial ureases on human body and about occurrence of anti-urease antibodies in long-lasting diseases.

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Section: Methods For Detecting Of Ureolytic Activitymentioning

confidence: 99%

Bacterial Urease and its Role in Long-Lasting Human Diseases

Konieczna

Żarnowiec²,

Kwinkowski³

et al. 2012

CPPS

232

155

View full text Add to dashboard Cite

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“…When a molecular structure is modified in an enzymatic reaction, the infrared spectrum is altered and changes in infrared absorption can be followed to monitor the progress of the reaction. Measurements of enzyme activity with infrared spectroscopy are relatively straightforward and several studies have been published comprising urea hydrolysis by urease [1,2], cefoxitin hydrolysis by β-lactamase [3], deacylation of cinnamoyl-chymotrypsin [4], ATP hydrolysis by the Ca 2+ -ATPase [5–7], dephosphorylation of fructose 1,6-bisphosphate by fructose-1,6 bisphosphatase [8] and of 4-nitrophenylphosphate by alkaline phosphatase [9], oxidation of d -glucose by glucose oxidase [10], hydrolysis of sucrose by β-fructofuranosidase [11–13], of maltose by amyloglucosidase [13] and of starch by amylogucosidase [14,15] and α-amylase [15,16], hydrolysis of amides [17,18] and synthesis of hydroxamic acid derivatives [18] by amidase, hydrolysis of several organophosphorus compounds by diisopropyl fluorophosphatase [19], the reaction of α-ketoglutarate and Ala to Glu and pyruvate by glutamic-pyruvic transaminase [20], consumption of oxalate and production of formate and CO 2 by oxalate decarboxylase [21], and acetone-butanol fermentation [22]. …”

Section: Introductionmentioning

confidence: 99%

Following Enzyme Activity with Infrared Spectroscopy

Kumar

Barth

2010

Sensors

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Fourier transform infrared (FTIR) spectroscopy provides a direct, “on-line” monitor of enzymatic reactions. Measurement of enzymatic activity is based on the fact that the infrared spectra of reactants and products of an enzymatic reaction are usually different. Several examples are given using the enzymes pyruvate kinase, fumarase and alcohol dehydrogenase. The main advantage of the infrared method is that it observes the reaction of interest directly, i.e., no activity assay is required to convert the progress of the reaction into an observable quantity.

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“…Of the three absorbance peaks identified and investigated to quantify the activity of the enzyme urease, the peak at 1,362 cm −1 was the most sensitive (greatest A over concentrations) and was the best indicator of urease activity in the control urease assay of Jackbean urease (Figures 1c and 2a-c). Karmali et al (2004) and Krishna et al (2011) also found that the 1,362-1,365 cm −1 bicarbonate peak was the most suitable for monitoring urea hydrolysis. The bicarbonate peak at 1,362 cm −1 was therefore the only peak selected to describe the urease activity in crop residues for this study.…”

Section: Identification Of Fti-r Peaks For Assaysmentioning

confidence: 92%

“…The most common urease activity assay is a colorimetric method to determine the accumulation of ammonia with phenolic compounds (Follmer et al 2004;Witte and Medina-Escobar 2001). Alternatively, Karmali et al (2004) used Fourier transform infrared spectroscopy (FTI-R) to successfully determine reaction kinetics of the urea hydrolysis reaction. The use of FTI-R allows for real-time measurements of the disappearance of substrate (urea) and the accumulation of products without disturbance to the reaction vessel or reacting materials.…”

Section: Introductionmentioning

confidence: 99%

Ureolytic Activity of Soybean and Corn Residue Extracts

Frame

Ridgley

Gaasch

et al. 2014

Communications in Soil Science and Plant Analysis

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The enzyme urease is responsible for the rapid hydrolysis of urea in agroecosystems where more than 50% of the applied nitrogen (N) can be lost via ammonia volatilization. The objectives of the study were to (1) extract urease from corn (Zea mays L.) and soybean (Glycine max L.) and (2) compare the urease activity from soybean and corn residues to Jackbean (Canavalia ensiformis) urease using Fourier transform infrared spectroscopy (FTI-R). Concentrations of urea and sodium bicarbonate ranging from 0 to 200 mM were analyzed with FTI-R to determine the correlation to peak height. Bicarbonate produced the most responsive peaks to concentration at 1,362 cm −1 . Urease extracted from soybean residue was active, producing a bicarbonate peak at 1362 cm −1 , whereas no urease activity was observed in corn residue. Variation among urease activities in crop residues could suggest a need for more precise nitrogen management in conservation tillage agroecosystems to reduce ammonia volatilization.

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The use of Fourier transform infrared spectroscopy to assay for urease from Pseudomonas aeruginosa and Canavalia ensiformis

Cited by 14 publications

References 21 publications

Bacterial Urease and its Role in Long-Lasting Human Diseases

Bacterial Urease and its Role in Long-Lasting Human Diseases

Following Enzyme Activity with Infrared Spectroscopy

Ureolytic Activity of Soybean and Corn Residue Extracts

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