scholarly journals Mechanism of Sporicidal Activity for the Synergistic Combination of Peracetic Acid and Hydrogen Peroxide

2015 ◽  
Vol 82 (4) ◽  
pp. 1035-1039 ◽  
Author(s):  
Mark J. Leggett ◽  
J. Spencer Schwarz ◽  
Peter A. Burke ◽  
Gerald McDonnell ◽  
Stephen P. Denyer ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Peracetic Acid ◽  
Bacterial Spores ◽  
Spore Coat ◽  
Synergistic Activity ◽  
Wild Type ◽  
Spore Resistance ◽  
Bacterial Endospores ◽  
Synergistic Combination ◽  
Reaction Vessels

ABSTRACTThere is still great interest in controlling bacterial endospores. The use of chemical disinfectants and, notably, oxidizing agents to sterilize medical devices is increasing. With this in mind, hydrogen peroxide (H2O2) and peracetic acid (PAA) have been used in combination, but until now there has been no explanation for the observed increase in sporicidal activity. This study provides information on the mechanism of synergistic interaction of PAA and H2O2against bacterial spores. We performed investigations of the efficacies of different combinations, including pretreatments with the two oxidizers, against wild-type spores and a range of spore mutants deficient in the spore coat or small acid-soluble spore proteins. The concentrations of the two biocides were also measured in the reaction vessels, enabling the assessment of any shift from H2O2to PAA formation. This study confirmed the synergistic activity of the combination of H2O2and PAA. However, we observed that the sporicidal activity of the combination is largely due to PAA and not H2O2. Furthermore, we observed that the synergistic combination was based on H2O2compromising the spore coat, which was the main spore resistance factor, likely allowing better penetration of PAA and resulting in the increased sporicidal activity.

scholarly journals Role of the Spore Coat Layers in Bacillus subtilis Spore Resistance to Hydrogen Peroxide, Artificial UV-C, UV-B, and Solar UV Radiation

2000 ◽  
Vol 66 (2) ◽  
pp. 620-626 ◽  
Author(s):  
Paul J. Riesenman ◽  
Wayne L. Nicholson
Keyword(s):  
Hydrogen Peroxide ◽  
Bacillus Subtilis ◽  
Uv Radiation ◽  
Spore Coat ◽  
Wild Type ◽  
Spore Resistance ◽  
Solar Uv ◽  
Coat Layer ◽  
Artificial Uv ◽  
Uv C

ABSTRACT Spores of Bacillus subtilis possess a thick protein coat that consists of an electron-dense outer coat layer and a lamellalike inner coat layer. The spore coat has been shown to confer resistance to lysozyme and other sporicidal substances. In this study, spore coat-defective mutants of B. subtilis (containing thegerE36 and/or cotE::cat mutation) were used to study the relative contributions of spore coat layers to spore resistance to hydrogen peroxide (H2O2) and various artificial and solar UV treatments. Spores of strains carrying mutations in gerE and/or cotE were very sensitive to lysozyme and to 5% H2O2, as were chemically decoated spores of the wild-type parental strain. Spores of all coat-defective strains were as resistant to 254-nm UV-C radiation as wild-type spores were. Spores possessing thegerE36 mutation were significantly more sensitive to artificial UV-B and solar UV radiation than wild-type spores were. In contrast, spores of strains possessing thecotE::cat mutation were significantly more resistant to all of the UV treatments used than wild-type spores were. Spores of strains carrying both the gerE36 andcotE::cat mutations behaved likegerE36 mutant spores. Our results indicate that the spore coat, particularly the inner coat layer, plays a role in spore resistance to environmentally relevant UV wavelengths.

Catalase activity and the survival of Pseudomonas putida, a root colonizer, upon treatment with peracetic acid

2001 ◽  
Vol 47 (3) ◽  
pp. 222-228 ◽  
Author(s):  
Anne J Anderson ◽  
Charles D Miller
Keyword(s):  
Hydrogen Peroxide ◽  
Pseudomonas Putida ◽  
Peracetic Acid ◽  
Catalase Activity ◽  
Specific Activity ◽  
Active Oxygen Species ◽  
Oxygen Species ◽  
Deficient Mutant ◽  
Wild Type ◽  
Cell Extracts

Peracetic acid is used as a sterilant in several industrial settings. Cells of a plant-colonizing bacterium, Pseudomonas putida in liquid suspension, were more sensitive to killing by peracetic acid when they lacked a major catalase activity, catalase A. Low doses of peracetic acid induced promoter activity of the gene encoding catalase A and increased total catalase specific activity in cell extracts. Microbes present in native agricultural soils rapidly degraded the active oxygen species present in peracetic acid. The simultaneous release of oxygen was consistent with a role for catalase in degrading the hydrogen peroxide that is part of the peracetic acid-equilibrium mixture. Amendment of sterilized soils with wild-type P. putida restored the rate of degradation of peracetic acid to a higher level than was observed in the soils amended with the catalase A-deficient mutant. The association of the bacteria with the plant roots resulted in protection of the wild-type as well as the catalase-deficient mutant from killing by peracetic acid. No differential recovery of the wild-type and catalase A mutant of P. putida was observed from roots after the growth matrix containing the plants was flushed with peracetic acid.Key words: Pseudomonas putida (Pp), activated oxygen species (AOS), hydrogen peroxide, luciferase, colonization.

scholarly journals Protection of Bacillus pumilus Spores by Catalases

2012 ◽  
Vol 78 (18) ◽  
pp. 6413-6422 ◽  
Author(s):  
Aleksandra Checinska ◽  
Malcolm Burbank ◽  
Andrzej J. Paszczynski
Keyword(s):  
Hydrogen Peroxide ◽  
Bacillus Pumilus ◽  
Toxic Chemicals ◽  
Spore Coat ◽  
Synergistic Activity ◽  
Gaseous Oxygen ◽  
Content Type ◽  
Enhanced Resistance ◽  
Oxygen Gas ◽  
Coat Layer

ABSTRACTBacillus pumilusSAFR-032, isolated at spacecraft assembly facilities of the National Aeronautics and Space Administration Jet Propulsion Laboratory, is difficult to kill by the sterilization method of choice, which uses liquid or vapor hydrogen peroxide. We identified two manganese catalases, YjqC and BPUM_1305, in spore protein extracts of severalB. pumilusstrains by using PAGE and mass spectrometric analyses. While the BPUM_1305 catalase was present in six of theB. pumilusstrains tested, YjqC was not detected in ATCC 7061 and BG-B79. Furthermore, both catalases were localized in the spore coat layer along with laccase and superoxide dismutase. Although the initial catalase activity in ATCC 7061 spores was higher, it was less stable over time than the SAFR-032 enzyme. We propose that synergistic activity of YjqC and BPUM_1305, along with other coat oxidoreductases, contributes to the enhanced resistance ofB. pumilusspores to hydrogen peroxide. We observed that the product of the catalase reaction, gaseous oxygen, forms expanding vesicles on the spore surface, affecting the mechanical integrity of the coat layer, resulting in aggregation of the spores. The accumulation of oxygen gas and aggregations may play a crucial role in limiting further exposure ofBacillispore surfaces to hydrogen peroxide or other toxic chemicals when water is present.

scholarly journals Inhibition Properties of Arylsulfatase and β-Glucuronidase by Hydrogen Peroxide, Hypochlorite, and Peracetic Acid

ACS Omega ◽  
2021 ◽  
Author(s):  
Shu-shu Zhong ◽  
Jun Zhang ◽  
Ze-hua Liu ◽  
Zhi Dang ◽  
Yu Liu
Keyword(s):  
Hydrogen Peroxide ◽  
Peracetic Acid

scholarly journals Escherichia coli MutM Suppresses Illegitimate Recombination Induced by Oxidative Stress

Genetics ◽  
1999 ◽  
Vol 151 (2) ◽  
pp. 439-446 ◽  
Author(s):  
Masaaki Onda ◽  
Katsuhiro Hanada ◽  
Hirokazu Kawachi ◽  
Hideo Ikeda
Keyword(s):  
Oxidative Stress ◽  
Escherichia Coli ◽  
Hydrogen Peroxide ◽  
Dna Damage ◽  
Double Strand Breaks ◽  
Illegitimate Recombination ◽  
Recombination Analysis ◽  
Wild Type ◽  
Strand Breaks ◽  
In The Wild

Abstract DNA damage by oxidative stress is one of the causes of mutagenesis. However, whether or not DNA damage induces illegitimate recombination has not been determined. To study the effect of oxidative stress on illegitimate recombination, we examined the frequency of λbio transducing phage in the presence of hydrogen peroxide and found that this reagent enhances illegitimate recombination. To clarify the types of illegitimate recombination, we examined the effect of mutations in mutM and related genes on the process. The frequency of λbio transducing phage was 5- to 12-fold higher in the mutM mutant than in the wild type, while the frequency in the mutY and mutT mutants was comparable to that of the wild type. Because 7,8-dihydro-8-oxoguanine (8-oxoG) and formamido pyrimidine (Fapy) lesions can be removed from DNA by MutM protein, these lesions are thought to induce illegitimate recombination. Analysis of recombination junctions showed that the recombination at Hotspot I accounts for 22 or 4% of total λbio transducing phages in the wild type or in the mutM mutant, respectively. The preferential increase of recombination at nonhotspot sites with hydrogen peroxide in the mutM mutant was discussed on the basis of a new model, in which 8-oxoG and/or Fapy residues may introduce double-strand breaks into DNA.

scholarly journals S-Nitrosothiol Signaling Is involved in Regulating Hydrogen Peroxide Metabolism of Zinc-Stressed Arabidopsis

2019 ◽  
Vol 60 (11) ◽  
pp. 2449-2463 ◽  
Author(s):  
Zs Kolbert ◽  
� Moln�r ◽  
D Ol�h ◽  
G Feigl ◽  
E Horv�th ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Plant Cells ◽  
Thioredoxin Reductase ◽  
Protein S ◽  
Protein Nitration ◽  
Wild Type ◽  
Accumulation Capacity ◽  
Zn Tolerance ◽  
Activity Loss ◽  
New Evidence

Abstract Accumulation of heavy metals such as zinc (Zn) disturbs the metabolism of reactive oxygen (e.g. hydrogen peroxide, H2O2) and nitrogen species (e.g. nitric oxide, NO; S-nitrosoglutathione, GSNO) in plant cells; however, their signal interactions are not well understood. Therefore, this study examines the interplay between H2O2 metabolism and GSNO signaling in Arabidopsis. Comparing the Zn tolerance of the wild type (WT), GSNO reductase (GSNOR) overexpressor 35S::FLAG-GSNOR1 and GSNOR-deficient gsnor1-3, we observed relative Zn tolerance of gsnor1-3, which was not accompanied by altered Zn accumulation capacity. Moreover, in gsnor1-3 plants Zn did not induce NO/S-nitrosothiol (SNO) signaling, possibly due to the enhanced activity of NADPH-dependent thioredoxin reductase. In WT and 35S::FLAG-GSNOR1, GSNOR was inactivated by Zn, and Zn-induced H2O2 is directly involved in the GSNOR activity loss. In WT seedlings, Zn resulted in a slight intensification of protein nitration detected by Western blot and protein S-nitrosation observed by resin-assisted capture of SNO proteins (RSNO-RAC). LC-MS/MS analyses indicate that Zn induces the S-nitrosation of ascorbate peroxidase 1. Our data collectively show that Zn-induced H2O2 may influence its own level, which involves GSNOR inactivation-triggered SNO signaling. These data provide new evidence for the interplay between H2O2 and SNO signaling in Arabidopsis plants affected by metal stress.

scholarly journals Inactivation of Prions by Low-Temperature Sterilization Technology Using Vaporized Gas Derived from a Hydrogen Peroxide–Peracetic Acid Mixture

Pathogens ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 24
Author(s):  
Akikazu Sakudo ◽  
Daiki Anraku ◽  
Tomomasa Itarashiki
Keyword(s):  
Hydrogen Peroxide ◽  
Medical Devices ◽  
Neurodegenerative Disorders ◽  
Peracetic Acid ◽  
Protein Misfolding ◽  
Prion Diseases ◽  
Proteinase K ◽  
Acid Mixture ◽  
Cover Glass ◽  
Standard Mode

Prion diseases are proteopathies that cause neurodegenerative disorders in humans and animals. Prion is highly resistant to both chemical and physical inactivation. Here, vaporized gas derived from a hydrogen peroxide–peracetic acid mixture (VHPPA) was evaluated for its ability to inactivate prion using a STERIACE 100 instrument (Saraya Co., Ltd.). Brain homogenates of scrapie (Chandler strain) prion-infected mice were placed on a cover glass, air-dried, sealed in a Tyvek package, and subjected to VHPPA treatment at 50–55 °C using 8% hydrogen peroxide and <10% peracetic acid for 47 min (standard mode, SD) or 30 min (quick mode, QC). Untreated control samples were prepared in the same way but without VHPPA. The resulting samples were treated with proteinase K (PK) to separate PK-resistant prion protein (PrPres), as a marker of the abnormal isoform (PrPSc). Immunoblotting showed that PrPres was reduced by both SD and QC VHPPA treatments. PrPres bands were detected after protein misfolding cyclic amplification of control but not VHPPA-treated samples. In mice injected with prion samples, VHPPA treatment of prion significantly prolonged survival relative to untreated samples, suggesting that it decreases prion infectivity. Taken together, the results show that VHPPA inactivates prions and might be applied to the sterilization of contaminated heat-sensitive medical devices.

scholarly journals RpoS-Dependent Stress Response and Exoenzyme Production in Vibrio vulnificus

2003 ◽  
Vol 69 (10) ◽  
pp. 6114-6120 ◽  
Author(s):  
A. Hülsmann ◽  
T. M. Rosche ◽  
I.-S. Kong ◽  
H. M. Hassan ◽  
D. M. Beam ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Stress Response ◽  
Mutant Strain ◽  
Environmental Changes ◽  
Vibrio Vulnificus ◽  
High Sensitivity ◽  
Striking Difference ◽  
Wild Type ◽  
Hydrolytic Activities ◽  
In The Wild

ABSTRACT Vibrio vulnificus is an estuarine bacterium capable of causing rapidly fatal infections through both ingestion and wound infection. Like other opportunistic pathogens, V. vulnificus must adapt to potentially stressful environmental changes while living freely in seawater, upon colonization of the oyster gut, and upon infection of such diverse hosts as humans and eels. In order to begin to understand the ability of V. vulnificus to respond to such stresses, we examined the role of the alternate sigma factor RpoS, which is important in stress response and virulence in many pathogens. An rpoS mutant of V. vulnificus strain C7184o was constructed by homologous recombination. The mutant strain exhibited a decreased ability to survive diverse environmental stresses, including exposure to hydrogen peroxide, hyperosmolarity, and acidic conditions. The most striking difference was a high sensitivity of the mutant to hydrogen peroxide. Albuminase, caseinase, and elastase activity were detected in the wild type but not in the mutant strain, and an additional two hydrolytic activities (collagenase and gelatinase) were reduced in the mutant strain compared to the wild type. Additionally, the motility of the rpoS mutant was severely diminished. Overall, these studies suggest that rpoS in V. vulnificus is important for adaptation to environmental changes and may have a role in virulence.

What induces colitis? Hydrogen peroxide or peracetic acid

Endoscopy ◽  
2008 ◽  
Vol 40 (03) ◽  
pp. 231-231 ◽  
Author(s):  
R. Coriat ◽  
U. Chaput ◽  
Z. Ismaili ◽  
S. Chaussade
Keyword(s):  
Hydrogen Peroxide ◽  
Peracetic Acid
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