scholarly journals Biosynthesis of Silver Chloride Nanoparticles Using Bacillus subtilis MTCC 3053 and Assessment of Its Antifungal Activity

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Kanniah Paulkumar ◽  
Shanmugam Rajeshkumar ◽  
Gnanadhas Gnanajobitha ◽  
Mahendran Vanaja ◽  
Chelladurai Malarkodi ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Antifungal Activity ◽  
Silver Chloride ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Cellular Membrane ◽  
X Ray Diffraction ◽  
Xrd Pattern ◽  
Transmission Electron ◽  
Crystalline Nature

The present investigation reported the synthesis of silver chloride nanoparticles using Bacillus subtilis. The adsorption of colloidal silver chloride nanoparticles showed an intense peak at the wavelength of 400 nm after 20 hrs of biomass incubation. The size of the silver nanoparticles ranges from 20 to 60 nm which was obtained from transmission electron microscope (TEM). The X-ray diffraction (XRD) pattern confirmed the crystalline nature of the nanoparticles. The bright circular spots of selected diffraction area (SAED) pattern also confirmed the good crystalline nature of the silver chloride nanoparticles with high magnification of TEM images. The presence of nitrate reductase enzyme in the cellular membrane of B. subtilis was confirmed by sodium dodecyl (SDS) polyacrylamide gel electrophoresis and it was found that the molecular weight is 37 kDa. The possible functional groups of the reductase enzyme in B. subtilis were identified by Fourier transform infrared spectroscopy (FTIR). Finally, antifungal activity of silver chloride nanoparticle was examined against Candida albicans, Aspergillus niger, and Aspergillus flavus. We conclude that the synthesis of silver chloride nanoparticles using microorganisms is more economical and simple. The antifungal property of silver chloride nanoparticles will play a beneficial role in biomedical nanotechnology.

scholarly journals Isolation, heterologous expression, and purification of a novel antifungal protein from Bacillus subtilis strain Z-14

2020 ◽  
Vol 19 (1) ◽  
Author(s):  
Xuechao Zhang ◽  
Xiaojun Guo ◽  
Cuihong Wu ◽  
Chengcui Li ◽  
Dongdong Zhang ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Antifungal Activity ◽  
Pichia Pastoris ◽  
Fungal Infections ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Proteinase K ◽  
Antifungal Protein ◽  
Subtilis Strain

Abstract Background Wheat sheath blight, a soil borne fungal disease caused by Rhizoctonia cerealis, is considered as one of the most serious threats to wheat worldwide. Bacillus subtilis Z-14 was isolated from soil sampled from a wheat rhizosphere and was confirmed to have strong antifungal activity against R. cerealis. Results An antifungal protein, termed F2, was isolated from the culture supernatant of Z-14 strain using precipitation with ammonium sulfate, anion exchange chromatography, and reverse phase chromatography. Purified F2 had a molecular mass of approximately 8 kDa, as assessed using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Edman degradation was used to determine the amino acid sequence of the N-terminus, which was NH2ASGGTVGIYGANMRS. This sequence is identical to a hypothetical protein RBAM_004680 (YP_001420098.1) synthesized by B. amyloliquefaciens FZB42. The recombinant F2 protein (rF2) was heterologously expressed in the yeast host Pichia pastoris, purified using a Niaffinity column, and demonstrated significant antifungal activity against R. cerealis. The purified rF2 demonstrated broad spectrum antifungal activity against different varieties of fungi such as Fusarium oxysporum, Verticillium dahliae, Bipolaris papendorfii, and Fusarium proliferatum. rF2 was thermostable, retaining 91.5% of its activity when incubated for 30 min at 100 °C. Meanwhile, rF2 maintained its activity under treatment by proteinase K and trypsin and over a wide pH range from 5 to 10. Conclusions A novel antifungal protein, F2, was purified from biocontrol Bacillus subtilis Z-14 strain fermentation supernatant and heterologously expressed in Pichia pastoris to verify its antifungal activity against R. cerealis and the validity of the gene encoding F2. Considering its significant antifungal activity and stable characteristics, protein F2 presents an alternative compound to resist fungal infections caused by R. cerealis.

scholarly journals Purification and heterologous expression of a novel antifungal protein from Bacillus subtilis strain Z-14

2020 ◽  
Author(s):  
Xuechao Zhang ◽  
Xiaojun Guo ◽  
Cuihong Wu ◽  
Chengcui Li ◽  
Dongdong Zhang ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Antifungal Activity ◽  
Pichia Pastoris ◽  
Fungal Infections ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Proteinase K ◽  
Antifungal Protein ◽  
Subtilis Strain ◽  
Affinity Column

Abstract Background: Wheat sheath blight, a soil borne fungal disease caused by Rhizoctonia cerealis, is considered as one of the most serious threats to wheat worldwide. Bacillus subtilis Z-14 was isolated from soil sampled from a wheat rhizosphere and has been confirmed to have strong antifungal activity against R. cerealis. Results: An antifungal protein, termed F2, was isolated from the culture supernatant of Z-14 strain using precipitation with ammonium sulfate, anion exchange chromatography, and reverse phase chromatography. Purified F2 had a molecular mass of approximately 9 kDa, as assessed using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Edman degradation was used to determine the amino acid sequence of the N-terminus, which was NH2-ASGGTVGIYGANMRS. This sequence is identical to a hypothetical protein RBAM_004680 (YP_001420098.1) synthesized by B. amyloliquefaciens FZB42. The recombinant F2 protein (rF2) was heterologously expressed in the yeast host Pichia pastoris, purified using Ni‑affinity column, and demonstrated significant antifungal activity against R. cerealis. The purified rF2 was thermostable, retaining 91.5% of its activity when incubated for 30 min at 100 °C. rF2 maintained its activity under treatment by proteinase K and trypsin.Conclusions: A novel antifungal protein F2 was purified from biocontrol Bacillus subtilis Z-14 strain fermentation supernatant and heterologously expressed in Pichia pastoris to certificate the antifungal activity against R. cerealis and the validity of gene sequence of protein F2. Considering its significant antifungal activity and stable characteristics, protein F2 presents an alternative compound to deal with fungal infections caused by R. cerealis.

scholarly journals Isolation, heterologous expression, and purification of a novel antifungal protein from Bacillus subtilis strain Z-14

2020 ◽  
Author(s):  
Xuechao Zhang ◽  
Xiaojun Guo ◽  
Cuihong Wu ◽  
Chengcui Li ◽  
Dongdong Zhang ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Antifungal Activity ◽  
Pichia Pastoris ◽  
Fungal Infections ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Proteinase K ◽  
Antifungal Protein ◽  
Subtilis Strain ◽  
Affinity Column

Abstract Background: Wheat sheath blight, a soil borne fungal disease caused by Rhizoctonia cerealis, is considered as one of the most serious threats to wheat worldwide. Bacillus subtilis Z-14 was isolated from soil sampled from a wheat rhizosphere and was confirmed to have strong antifungal activity against R. cerealis. Results: An antifungal protein, termed F2, was isolated from the culture supernatant of Z-14 strain using precipitation with ammonium sulfate, anion exchange chromatography, and reverse phase chromatography. Purified F2 had a molecular mass of approximately 8 kDa, as assessed using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Edman degradation was used to determine the amino acid sequence of the N-terminus, which was NH2‑ASGGTVGIYGANMRS. This sequence is identical to a hypothetical protein RBAM_004680 (YP_001420098.1) synthesized by B. amyloliquefaciens FZB42. The recombinant F2 protein (rF2) was heterologously expressed in the yeast host Pichia pastoris, purified using a Ni‑affinity column, and demonstrated significant antifungal activity against R. cerealis. The purified rF2 demonstrated broad spectrum antifungal activity against different varieties of fungi such as Fusarium oxysporum, Verticillium dahliae, Bipolaris papendorfii, and Fusarium proliferatum. rF2 was thermostable, retaining 91.5% of its activity when incubated for 30 min at 100 °C. Meanwhile, rF2 maintained its activity under treatment by proteinase K and trypsin and over a wide pH range from 5 to 10.Conclusions: A novel antifungal protein, F2, was purified from biocontrol Bacillus subtilis Z-14 strain fermentation supernatant and heterologously expressed in Pichia pastoris to verify its antifungal activity against R. cerealis and the validity of the gene encoding F2. Considering its significant antifungal activity and stable characteristics, protein F2 presents an alternative compound to resist fungal infections caused by R. cerealis.

Hydrothermal Synthesis and Characterization of BiFeO3 Polyhedral Crystallites

2012 ◽  
Vol 174-177 ◽  
pp. 508-511
Author(s):  
Lin Lin Yang ◽  
Yong Gang Wang ◽  
Yu Jiang Wang ◽  
Xiao Feng Wang
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Synthesis And Characterization ◽  
X Ray Diffraction ◽  
Xrd Pattern ◽  
X Ray ◽  
Transmission Electron ◽  
Scanning Electron

BiFeO3 polyhedrons had been successfully synthesized via a hydrothermal method. The as-prepared products were characterized by power X-ray diffraction (XRD) pattern, scanning electron microscopy (SEM) and transmission electron microscopy (TEM). The possible mechanisms for the formation of BiFeO3 polyhedrons were discussed. Though comparison experiments, it was found that the kind of precursor played a key role on the morphology control of BiFeO3 crystals.

Characterization of Layered Double Hydroxide Modified with Sodium Dodecyl Sulfate and its Dispersion in Polyethylene

2013 ◽  
Vol 591 ◽  
pp. 138-141
Author(s):  
Zhi Dong Han ◽  
Xin Ke Zhang ◽  
Yue Wang ◽  
Zheng Quan Jiang ◽  
Peng Wang
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Layered Double Hydroxide ◽  
Sodium Dodecyl ◽  
Melt Blending ◽  
X Ray Diffraction ◽  
Transmission Electron ◽  
Dodecyl Sulfate ◽  
The Matrix ◽  
Mixing Method ◽  
Double Hydroxide

Mg-Al layered double hydroxide (LDH) was modified with sodium dodecyl sulfate (SDS) by regeneration method. The structure of modified LDH (SDS-LDH) was investigated by X-ray diffraction (XRD) and Fourier transform infrared spectroscopy (FTIR). The composites of SDS-LDH and polyethylene (PE) were prepared by melt blending and solution mixing method with maleated PE (PEgMA) as compatibilizer. The structure of the composites and the dispersion of SDS-LDH in the matrix were investigated by XRD and transmission electron microscopy (TEM), respectively. The results reveal that SDS was successfully intercalated into the interlayer space of LDH. SDS-LDH was hardly exfoliated in PE/PEgMA by melt blending. The nanocomposites of PE/(PEgMA/SDS-LDH) were successfully prepared by melt blending PE with SDS-LDH/PEgMA master-batch obtained by solution mixing. Homogeneous dispersion of SDS-LDH in the matrix was observed by TEM.

scholarly journals Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

Materials ◽  
2020 ◽  
Vol 13 (2) ◽  
pp. 358 ◽  
Author(s):  
Haiyan Ju ◽  
Xiuying Liu ◽  
Gang Zhang ◽  
Dezheng Liu ◽  
Yongsheng Yang
Keyword(s):  
Type I Collagen ◽  
Structural Characteristics ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Dry Weight ◽  
Collagen Fibrils ◽  
Type I ◽  
X Ray Diffraction ◽  
Aggregation Structure ◽  
Native Collagen

Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure.

Direct Preparation of Ce0.8Sm0.2O1.9 Powders Oxidized With H2O2 for Low Temperature SOFCs Application

2005 ◽  
Author(s):  
Jianbing Huang ◽  
Zongqiang Mao ◽  
Bin Zhu ◽  
Lizhai Yang ◽  
Ranran Peng ◽  
...  
Keyword(s):  
Single Phase ◽  
Fluorite Structure ◽  
X Ray Diffraction ◽  
Composite Electrolyte ◽  
Xrd Pattern ◽  
Transmission Electron ◽  
Direct Preparation ◽  
Novel Method ◽  
Power Densities

A novel method was developed to prepare fine doped ceria (DCO) powders directly. Ceria doped with 20 mol. % of samarium (Ce0.8Sm0.2O1.9, SDC) was prepared by in-situ oxidization of hydroxide precipitates with H2O2 in the solutions. The resultant powder desiccated at 85°C overnight was characterized by X-ray diffraction (XRD), thermogravimetry /differential thermal analysis (TG/DTA), and transmission electron microscopy (TEM). The XRD pattern showed that the as-dried SDC powder is single phase with a cubic fluorite structure like that of pure CeO2. An anode-supported SOFC was also fabricated based on SDC and 20wt. % (62mol. %Li2CO3–38 mol. %K2CO3) composite electrolyte, LiNiO2 as cathode and NiO as anode, by cold pressing. Using hydrogen as the fuel and air as the oxidant, the I-V and I-P characteristics exhibit excellent performances and the maximum power densities are about 696, 469, 377 and 240 mWcm−2 at 650, 600, 550 and 500°C, respectively.

Synthesis of Zn Doped CdSe Quantum Dots via Inverse Micelle Technique

2014 ◽  
Vol 807 ◽  
pp. 115-121 ◽  
Author(s):  
Fatihah Aplop ◽  
Mohd Rafie bin Johan
Keyword(s):  
Quantum Dots ◽  
Quantum Confinement Effect ◽  
Blue Shift ◽  
X Ray Diffraction ◽  
Cdse Qds ◽  
Xrd Pattern ◽  
Transmission Electron ◽  
Inverse Micelle ◽  
Cadmium Selenide Quantum Dots ◽  
The Fourier Transform

Zinc doped Cadmium Selenide Quantum Dots (CdSe/Zn QDs) were synthesized via inverse micelle technique. The absorption spectra exhibit a strong blue-shift characteristic due to quantum confinement effect. The X-ray Diffraction (XRD) pattern showed the zinc-blende phase of Zn doped CdSe QDs. Transmission Electron Microscopy (TEM) images suggested that the sizes of QDs were falls in range between 2 – 8 nm, with narrow size distribution. The TEM images also revealed that the Zn doped CdSe QDs were spherical, having a compact and dense structure. The optical bandgap of Zn-doped CdSe QDs are smaller than the undoped CdSe QDs as shown in Tauc’s plot. The fourier transform infrared spectra proves the complexion of CdSe-Zn QDs.

scholarly journals The purification of a novel amylase from Bacillus subtilis and its inhibition by wheat proteins

1983 ◽  
Vol 209 (2) ◽  
pp. 561-564 ◽  
Author(s):  
A R Orlando ◽  
P Ade ◽  
D Di Maggio ◽  
C Fanelli ◽  
L Vittozzi
Keyword(s):  
Bacillus Subtilis ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Alpha Amylase ◽  
Wheat Protein ◽  
Wheat Proteins ◽  
Maximal Inhibition ◽  
Molecular Weights ◽  
Amylase Inhibitors

A new alpha-amylase (EC 3.2.1.1) from Bacillus subtilis was purified by affinity chromatography. The molecular weight of the purified enzyme, estimated from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, was 93000, which is very different from the molecular weights of two well-characterized amylases from B. subtilis. Electrofocusing showed an isoelectric point of 5. Amylase shows a broad maximum of activity between pH 6 and 7; maximal inhibition of enzyme by wheat-protein alpha-amylase inhibitors is displayed at pH 7.

Electrophoretic and electron microscopic examination of the adductor and diductor muscles of an articulate brachiopod, Terebratalia transversa

1982 ◽  
Vol 60 (4) ◽  
pp. 550-559 ◽  
Author(s):  
William P. Eshleman ◽  
Jerrel L. Wilkens ◽  
Michael J. Cavey
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electron Microscopic Examination ◽  
Light Chains ◽  
Electron Microscopic ◽  
Electrophoretic Patterns ◽  
Transmission Electron ◽  
Adductor Muscles ◽  
Regulation Of Contraction

The proteins of the striated adductor muscles, smooth adductor muscles, and diductor muscles of the articulate brachiopod Terebratalia transversa have been examined by sodium dodecyl sulfate – polyacrylamide gel electrophoresis. Electrophoretic patterns indicate the presence of paramyosin in all of these valve muscles. Tentative identification has also been made of the proteins responsible for actin and for myosin regulation of contraction (troponin–tropomyosin and myosin light chains, respectively). The myofilaments of the striated adductor cells, smooth adductor cells, and diductor cells have been characterized by transmission electron microscopy. The smooth adductor cells and the diductor cells exhibit very thick myofilaments which are fusiform in shape, exceptionally long, and axially banded. Morphological features of these thick myofilaments are consistent with those of paramyosin filaments found in other muscles and myoepithelia. Although the striated adductor cells contain paramyosin, it is not manifest in the thick myofilaments.

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