An in-depth characterization of the entomopathogenic strain Bacillus pumilus 15.1 reveals that it produces inclusion bodies similar to the parasporal crystals of Bacillus thuringiensis

2016 ◽  
Vol 100 (8) ◽  
pp. 3637-3654 ◽  
Author(s):  
Diana C. Garcia-Ramon ◽  
C. Alfonso Molina ◽  
Antonio Osuna ◽  
Susana Vílchez
Keyword(s):  
Bacillus Thuringiensis ◽  
Inclusion Bodies ◽  
Bacillus Pumilus ◽  
Parasporal Crystals

Characterization of Bacillus thuringiensis parasporal crystals using laser speckle technique: effect of crystal concentration and dimension

2015 ◽  
Vol 54 (12) ◽  
pp. 3725 ◽  
Author(s):  
Rana Nassif ◽  
Christelle Abou Nader ◽  
Jihane Rahbany ◽  
Fabrice Pellen ◽  
Dominique Salameh ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Laser Speckle ◽  
Technique Effect ◽  
Parasporal Crystals

Parasporal crystals produced by oligosporogenous mutants of Bacillus thuringiensis (Spo− Cr+)

1980 ◽  
Vol 26 (4) ◽  
pp. 486-491 ◽  
Author(s):  
Donovan E. Johnson ◽  
Debra M. Niezgodski ◽  
George M. Twaddle
Keyword(s):  
Bacillus Thuringiensis ◽  
Inclusion Bodies ◽  
Insect Cells ◽  
Crystalline Inclusion ◽  
Wild Type ◽  
In Vitro Technique ◽  
Mutant Strains ◽  
Embedded Particles ◽  
Parasporal Crystals

Six oligosporogenic (Spo−) mutant strains of Bacillus thuringiensis were selected from survivors of treatment with N-methyl-N′-nitro-N-nitrosoguanidine. Each strain was blocked at or before stage II of spore development, but all produced typical bipyramidal-shaped crystalline inclusion bodies. Toxicity of the parasporal endotoxin isolated from the mutant strains was assayed by an in vitro technique using cultured insect cells, and was comparable with that of normal wild-type parasporal protein. Multiple parasporal inclusion bodies per cell were often produced, and smaller embedded particles were numerous and distinct.

scholarly journals Purification and characterization of the entomocidal protoxin of Bacillus thuringiensis.

1981 ◽  
Vol 256 (6) ◽  
pp. 3000-3004
Author(s):  
L.A. Bulla ◽  
K.J. Kramer ◽  
D.J. Cox ◽  
B.L. Jones ◽  
L.I. Davidson ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Purification And Characterization

scholarly journals Purification and characterization of carboxymethylcellulase from Bacillus pumilus EWBCM1 isolated from earthworm gut (Eudrilus eugeniae)

2021 ◽  
Vol 33 (1) ◽  
pp. 101261
Author(s):  
Thiruvengadam Shankar ◽  
Subbiah Sankaralingam ◽  
Chellapandian Balachandran ◽  
Arunachalam Chinnathambi ◽  
Omaima Nasif ◽  
...  
Keyword(s):  
Bacillus Pumilus ◽  
Eudrilus Eugeniae ◽  
Purification And Characterization ◽  
Earthworm Gut

Refolding, purification, and characterization of constitutive-active human-Smad8 produced as inclusion bodies in ClearColi® BL21 (DE3)

2021 ◽  
Vol 184 ◽  
pp. 105878
Author(s):  
Carla Lizbeth Segovia-Trinidad ◽  
Bastian Quaas ◽  
Zhaopeng Li ◽  
Antonina Lavrentieva ◽  
Yvonne Roger ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Purification And Characterization

scholarly journals Characterization of a Dye-Decolorizing Peroxidase from Irpex lacteus Expressed in Escherichia coli: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates

2021 ◽  
Vol 7 (5) ◽  
pp. 325
Author(s):  
Laura Isabel de de Eugenio ◽  
Rosa Peces-Pérez ◽  
Dolores Linde ◽  
Alicia Prieto ◽  
Jorge Barriuso ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Inclusion Bodies ◽  
Veratryl Alcohol ◽  
Dye Decolorization ◽  
Irpex Lacteus ◽  
Type D ◽  
Lignin Peroxidases

A dye-decolorizing peroxidase (DyP) from Irpex lacteus was cloned and heterologously expressed as inclusion bodies in Escherichia coli. The protein was purified in one chromatographic step after its in vitro activation. It was active on ABTS, 2,6-dimethoxyphenol (DMP), and anthraquinoid and azo dyes as reported for other fungal DyPs, but it was also able to oxidize Mn2+ (as manganese peroxidases and versatile peroxidases) and veratryl alcohol (VA) (as lignin peroxidases and versatile peroxidases). This corroborated that I. lacteus DyPs are the only enzymes able to oxidize high redox potential dyes, VA and Mn+2. Phylogenetic analysis grouped this enzyme with other type D-DyPs from basidiomycetes. In addition to its interest for dye decolorization, the results of the transformation of softwood and hardwood lignosulfonates suggest a putative biological role of this enzyme in the degradation of phenolic lignin.

Purification and partial amino acid sequence of thuricin S, a new anti-Listeriabacteriocin from Bacillus thuringiensis

2007 ◽  
Vol 53 (2) ◽  
pp. 284-290 ◽  
Author(s):  
Sonia Chehimi ◽  
François Delalande ◽  
Sophie Sablé ◽  
Mohamed-Rabeh Hajlaoui ◽  
Alain Van Dorsselaer ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Proteinase K ◽  
Terminal Sequence ◽  
Partial Amino Acid Sequence ◽  
Ph Values ◽  
Heat Stable ◽  
Isolation And Characterization ◽  
Terminal Amino ◽  
Edman Sequencing

We report the isolation and characterization of a new bacteriocin, thuricin S, produced by the Bacillus thuringiensis subsp. entomocidus HD198 strain. This antibacterial activity is sensitive to proteinase K, is heat-stable, and is stable at a variety of pH values (3–10.5). The monoisotopic mass of thuricin S purified by high perfomance liquid chromatography, as determined with mass spectrometry ESI-TOF-MS, is 3137.61 Da. Edman sequencing and NanoESI-MS/MS experiments provided the sequence of the 18 N-terminal amino acids. Interestingly, thuricin S has the same N-terminal sequence (DWTXWSXL) as bacthuricin F4 and thuricin 17, produced by B. thuringiensis strains BUPM4 and NEB17, respectively, and could therefore be classified as a new subclass IId bacteriocin.

Sign in / Sign up

Export Citation Format

Share Document