GERMINATION OF UNTREATED OR HYDROGEN PEROXIDE TREATED BACILLUS LICHENIFORMIS SPORES WITH IONIC OR NUTRIENT INITIATORS

The potential use of Bacillus licheniformis coated bioparticles for hydrogen peroxide (H2O2) degradation was assessed in this study. Bioparticles were made by mixing zeolite, activated carbon and cement in ratio 20:5:6 for attachment of biofilm. The efficiency of H2O2 degradation was examined in the presence and absence of biofilm (control) on bioparticles. Optimisation of biofilm development (7 and 10 days) and reusability were also investigated for H2O2degradation. Actively growing bacterial suspension (late exponential phase) of B.licheniformis was used in development of pure culture biofilm. The 7–day biofilm coated bioparticles system successfully achieved complete H2O2 degradation within an hour (highest rate = 1.17 % H2O2 degraded per minute) while the control showed no significant H2O2 degradation. After repeated use of biofilm coated bioparticles, the rate of H2O2 degradation declined to 0.654 % H2O2degraded per minute, and second use, the rate of H2O2 degradation was 0.166 % H2O2 degraded per minute. Field Emission Scanning Electron Microscope (FESEM) images of the biofilm coated bioparticles showed the attachment of cells and formation of extracellular polymeric substances (EPS), whereas the control showed no biofilm formed.

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Bacillus licheniformis SMIA-2 protease used as an additive in detergent formulations

Acta Scientiarum Biological Sciences ◽

10.4025/actascibiolsci.v43i1.55871 ◽

2021 ◽

Vol 43 ◽

pp. e55871

Author(s):

Larissa Pacheco Ferreira ◽

Erica Cruz ◽

Meire Lelis Leal Martins

Keyword(s):

Hydrogen Peroxide ◽

Bacillus Licheniformis ◽

Statistical Design ◽

Cleaning Efficiency ◽

Component Mixture ◽

Linear Alkylbenzene ◽

Bacillus Spp ◽

Broad Variety

Microbial proteases, especially from Bacillus spp., have been widely exploited for a broad variety of applications, such as the improvement of the cleaning efficiency of conventional detergents. In this work, the statistical design of the experiment was used to optimize the concentrations of a three-component mixture: Bacillus licheniformis SMIA-2 protease, Linear Alkylbenzene Sulphate and hydrogen peroxide, in an attempt to prepare an environmentally correct cleaning formulation. The results demonstrated that the combination of 1% (w/v) protease with 1.5% (w/v) LAS and 1% (w/v) H2O2 was effective in removing blood from cloth pieces and that a protease concentration decrease from 1.0% to 0.5% (w/v) would not have a signiﬁcant impact on percent blood removal if LAS concentrations between 1.5-2.0% (w/v) in combination with lower (<0.5%, w/v) concentrations of H2O2 were used. Thus, the protease from Bacillus licheniformis SMIA-2 can be effectively incorporated into cleaning formulations together with LAS and hydrogen peroxide to formulate more sustainable detergents.

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Microanatomy of the Periplasm of Bacillus Licheniformis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100065365 ◽

1971 ◽

Vol 29 ◽

pp. 262-263

Author(s):

B.K. Ghosh

Keyword(s):

Cell Wall ◽

Plasma Membrane ◽

Bacillus Licheniformis ◽

External Environment ◽

Permeability Barrier ◽

Periplasmic Space ◽

Modified Technique ◽

Gram Positive ◽

Gram Negative ◽

Gram Positive Bacteria

Periplasm of bacteria is the space outside the permeability barrier of plasma membrane but enclosed by the cell wall. The contents of this special milieu exterior could be regulated by the plasma membrane from the internal, and by the cell wall from the external environment of the cell. Unlike the gram-negative organism, the presence of this space in gram-positive bacteria is still controversial because it cannot be clearly demonstrated. We have shown the importance of some periplasmic bodies in the secretion of penicillinase from Bacillus licheniformis.In negatively stained specimens prepared by a modified technique (Figs. 1 and 2), periplasmic space (PS) contained two kinds of structures: (i) fibrils (F, 100 Å) running perpendicular to the cell wall from the protoplast and (ii) an array of vesicles of various sizes (V), which seem to have evaginated from the protoplast.

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Peroxidase Localization in Hartmanella Trophozoites

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100065778 ◽

1971 ◽

Vol 29 ◽

pp. 346-347 ◽

Cited By ~ 1

Author(s):

George E. Childs ◽

Joseph H. Miller

Keyword(s):

Hydrogen Peroxide ◽

Ultrastructural Localization ◽

Pathogenic Strain ◽

Oxidative Enzymes ◽

Differential Centrifugation ◽

Electron Microscopic ◽

Microscopic Studies ◽

The Subject ◽

Axenic Cultures

Biochemical and differential centrifugation studies have demonstrated that the oxidative enzymes of Acanthamoeba sp. are localized in mitochondria and peroxisomes (microbodies). Although hartmanellid amoebae have been the subject of several electron microscopic studies, peroxisomes have not been described from these organisms or other protozoa. Cytochemical tests employing diaminobenzidine-tetra HCl (DAB) and hydrogen peroxide were used for the ultrastructural localization of peroxidases of trophozoites of Hartmanella sp. (A-l, Culbertson), a pathogenic strain grown in axenic cultures of trypticase soy broth.

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Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100123969 ◽

1992 ◽

Vol 50 (1) ◽

pp. 712-713

Author(s):

Xiaorong Zhu ◽

Richard McVeigh ◽

Bijan K. Ghosh

Keyword(s):

Alkaline Phosphatase ◽

Bacillus Licheniformis ◽

Self Assembly ◽

Gel Electrophoresis ◽

Culture Supernatant ◽

Regular Structure ◽

The Self ◽

Cellular Distribution ◽

Structural Protein ◽

Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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Fluorescent proteins for in vivo imaging, where's the biliverdin?

Biochemical Society Transactions ◽

10.1042/bst20200444 ◽

2020 ◽

Vol 48 (6) ◽

pp. 2657-2667

Author(s):

Felipe Montecinos-Franjola ◽

John Y. Lin ◽

Erik A. Rodriguez

Keyword(s):

Hydrogen Peroxide ◽

In Vivo Imaging ◽

Near Infrared ◽

Fluorescent Protein ◽

Fluorescent Proteins ◽

Fluorescent Imaging ◽

Infrared Light ◽

Red Fluorescent Protein ◽

Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

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Protective effect of chitooligosaccharides on hydrogen peroxide-induced PC-12 cells death by inhibition of oxidative damage

Cell Biology International ◽

10.1042/cbi034s027d ◽

2010 ◽

Vol 34 (8) ◽

pp. S27-S27

Author(s):

Xueling Dai ◽

Ping Chang ◽

Ke Xu ◽

Changjun Lin ◽

Hanchang Huang ◽

...

Keyword(s):

Hydrogen Peroxide ◽

Oxidative Damage ◽

Protective Effect ◽

Pc 12 Cells ◽

Cells Death

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Signal-regulated oxidation of proteins via MICAL

Biochemical Society Transactions ◽

10.1042/bst20190866 ◽

2020 ◽

Vol 48 (2) ◽

pp. 613-620

Author(s):

Clara Ortegón Salas ◽

Katharina Schneider ◽

Christopher Horst Lillig ◽

Manuela Gellert

Keyword(s):

Signal Transduction ◽

Hydrogen Peroxide ◽

Cell Death ◽

Redox Regulation ◽

Signal Transduction Pathways ◽

Cellular Functions ◽

Intracellular Signals ◽

Amino Acid Side Chains ◽

Specific Receptors ◽

Sulfur Containing

Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

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