Biotransformations with Peroxidases

Adam, Waldemar; Lazarus, Michael; Saha‐Möller, Chantu R.; Weichold, Oliver; Hoch, Ute; Häring, Dietmar; Schreier, Peter

doi:10.1007/3-540-69791-8_4

Cited by 111 publications

(117 citation statements)

References 128 publications

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“…In the current work, the biodegradation of cephalexin by bacterial isolates was determined as function of β-lactamase. From the environmental perspective, enzymes are more acceptable due to their biodegradability (Adam et al 1999). One of the simplest methods of administering an enzyme to the target effluent is to introduce the microorganism cells that produce the enzyme into the effluent directly (Mugdha and Usha 2012).…”

Section: Discussionmentioning

confidence: 99%

Biodegradation of Pharmaceutical Wastes in Treated Sewage Effluents by Bacillus subtilis 1556WTNC

Al-Gheethi¹,

Ismail²

2014

Environ. Process.

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The aim of this study was to investigate the potentials for enzymatic biodegradation of pharmaceutical active compounds (β-lactam antibiotics) in treated sewage effluents as a function of β-lactamase produced Bacillus subtilis 1556WTNC. Four β-lactams antibiotics were selected: two of them belong to penicillin's (amoxicillin and ampicillin) and two belong to cephalosporins (cephalexin and cefuroxime); ciprofloxacin (belongs to quinolones) was used as a negative control. The enzymatic biodegradation process was conducted under the optimal conditions for β-lactams production (5.9 log 10 CFU mL −1 ; pH 6.5; temperature 35°C for 12 days) as determined in this research. The maximum biodegradation was 25.03 % at 1 mg mL −1 for amoxicillin, 15.59 % at 0.8 mg mL −1 of ampicillin, 22.59 % at 1 mg mL −1 of cephalexin, 10.62 % at 1 mg mL −1 of cefuroxime, while it was 2.45 % at 0.6 mg mL −1 of ciprofloxacin. B. subtilis 1556WTNC exhibited the potential to produce β-lactamase and biodegrade β-lactam antibiotic genetically and inducibly B. subtilis 1556WTNC could grow and biodegrade β-lactam antibiotics in conditions similar to the characteristics of treated sewage effluents such as pH, temperature, and during short time (12 days), because it was already acclimatized to those conditions. For this reason, treated sewage effluents were used as source to isolate this strain. It can be concluded that B. subtilis 1556WTNC is suitable to remove pharmaceutical residues from the treated sewage effluents and produce effluents at higher quality than that achieved by secondary treatment process.

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Section: Discussionmentioning

confidence: 99%

Biodegradation of Pharmaceutical Wastes in Treated Sewage Effluents by Bacillus subtilis 1556WTNC

Al-Gheethi¹,

Ismail²

2014

Environ. Process.

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“…39 PDDA/PSS/Mb colloids were resuspended in 1 mL of 10 mM pH 5.5 acetate buffer containing 4 mM guaiacol, and H 2 O 2 was added to 1 mM. Production of the colored product 3,3′-dimethoxy-4,4′-biphenoquinone [39][40][41] was monitored by UV-vis spectroscopy at 470 nm. The biocolloids were centrifuged from the reaction mixture before UV-vis spectra were obtained.…”

Section: Methodsmentioning

confidence: 99%

Enzyme−DNA Biocolloids for DNA Adduct and Reactive Metabolite Detection by Chromatography−Mass Spectrometry

et al. 2008

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Silica microbead bioreactors (0.5 µm diameter) coated with DNA and enzymes were fabricated to measure reactive metabolite and DNA-adduct formation rates relevant to genotoxicity screening. Cytochrome (cyt) P450 2E1, cyt P450 cam , and myoglobin (Mb) were incorporated into thin films with DNA using the electrostatic layer-bylayer (LbL) method. The utility of these biocolloids was demonstrated by oxidation of guaiacol, styrene, and (4-methylnitrosoamino)-1-(3-pyridyl)-1-butanone (NNK). Enzyme turnover rates for formation of reactive metabolites were monitored using gas chromatography/mass spectrometry (GC/MS) and liquid chromatography-mass spectrometry (LC-MS). Capillary LC-MS/MS was employed to determine DNA nucleobase adducts after catalyzing the reactive metabolite formation with DNAenzyme biocolloids and then using neutral thermal hydrolysis on the biocolloids. Dramatic improvements in surface area to volume ratio over similar films on macroscopic surfaces opens new avenues for genotoxicity screening and enabled the first use of pure cyt P450 enzymes in enzyme-DNA films to produce DNA adducts. The method makes possible identification and formation rate measurements of major and minor DNA adducts as well as the metabolites themselves in <5 min of reaction time using relevant human liver enzymes.Toxicity is often not identified sufficiently early in developing new pharmaceutical, agricultural, personal care, and dietary products. Roughly 30% of drug development failures result from toxicity issues, driving drug costs up significantly. 1-4 Conventional in vitro biological tests such as Ames, chromosome aberration, mouse lymphoma, and Comet assays provide qualitative answers to toxicity questions based on bulk DNA damage but do not give chemical structure or site-specific DNA damage information. 5,6 Animal testing may not relate to human exposure because of metabolic and physiological differences between humans and animal models. 2,4,7 While all these toxicity tests are valuable, we believe that rapid, high-throughput toxicity screening methods for new chemicals that provide chemical structure information about reactive intermediates at early stages of commercial development are important goals to complement conventional microbiological and animal tests.Bioactivation of xenobiotic molecules by metabolic enzymes often results in reactive metabolites that damage biomolecules, including DNA, in a major toxicity pathway. [8][9][10] An example is the metabolism of lipophilic compounds by liver cytochrome (cyt) P450 (or CYP) enzymes creating reactive electrophilic metabolites. 4,11 These electrophiles attack nucleophilic DNA sites, primarily guanines, potentially resulting in genotoxicity. Depending on the adduct site, additional metabolism, and DNA repair processes, covalent DNA adducts can lead to mutations, teratogenesis, and carcinogenesis. 12-14 Thus, nucleobase adducts are key biomarkers for predicting cancer risk in humans and for exposure to toxic chemicals, and sensitive liquid chromatography-mass spectromet...

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“…They catalyze the oxidation of several important substrates and play important roles in various physiological processes in plants (Passardi et al 2005;Hamid, Khalil-ur-Rehman 2009). They are heme-containing proteins and are involved in the oxidation of broad range of substrates using hydrogen peroxide as the oxidant (Adam et al 1999;Galati, O'Brien 2004). Peroxidases have been used in biotechnology, biomedicine, pharmacy and agriculture (Veitch, Smith 2001).…”

Section: Introductionmentioning

confidence: 99%

“…However, studies are still ongoing to identify peroxidases from other sources with properties suitable for biotechnological, biomedical and other industrial applications (Regalado et al 2004). Some peroxidases from these sources have shown potential for applications as biocatalysts and bioelectrocatalysts (Adam et al 1999;Torres et al 2003;Carlos et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Catalytic and kinetic properties of purified Eichhornia crassipes leaf peroxidase

Arise¹,

Osundahunsi²,

Farohunbi³

et al. 2016

EEB

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Peroxidase from Eichhornia crassipes leaf was purified 23.58 fold with 18.58% yield by means of (NH 4 ) 2 SO 4 precipitation, ion exchange and Sephadex G-75 gel filtration chromatography. Optimum temperature and substrate-dependent pH optimum for enzyme activity were 40 °C and pH 4.0, 9.0 and 6.0 for 2,2'-azino-bis-(3-ethylbenzthiazolin)-6-sulfonate (ABTS), guaiacol and pyrogallol, respectively. The enzyme had high pH stability and moderate thermal stability at temperatures up to 60 °C; the activation energy of inactivation of the enzyme was ~122.29 kJ mol -1 . Temperature-denaturing and spontaneous recovery were shown to be time-dependent while Ca 2+ -enhanced recovery of the denatured enzyme was in a time-dependent manner. The enzyme showed preferential affinity for ABTS over guaiacol and pyrogallol with K M values of 31.11, 21.91 and 6.45 mM respectively. It was reversibly inhibited by Pb 2+ , Hg 2+ and EDTA while urea only caused loss of ~30.40% activity after 60 min of incubation. E. crassipes leaf peroxidase has potential use for broad range of applications.

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Biotransformations with Peroxidases

Cited by 111 publications

References 128 publications

Biodegradation of Pharmaceutical Wastes in Treated Sewage Effluents by Bacillus subtilis 1556WTNC

Biodegradation of Pharmaceutical Wastes in Treated Sewage Effluents by Bacillus subtilis 1556WTNC

Enzyme−DNA Biocolloids for DNA Adduct and Reactive Metabolite Detection by Chromatography−Mass Spectrometry

Catalytic and kinetic properties of purified Eichhornia crassipes leaf peroxidase

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