Cloning and characterization of the Cry79Aa1 gene from a lepidopteran active strain of Bacillus thuringiensis

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.

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Diversity analysis and characterization of Coleoptera-, Hemiptera- and Nematode-active cry genes in native isolates of Bacillus thuringiensis

Annals of Microbiology ◽

10.1007/s13213-013-0636-7 ◽

2013 ◽

Vol 64 (1) ◽

pp. 85-98 ◽

Cited By ~ 1

Author(s):

Ramasamy Asokan ◽

Hanchipura Mallesh Mahadeva Swamy ◽

Geetha G. Thimmegowda ◽

Riaz Mahmood

Keyword(s):

Bacillus Thuringiensis ◽

Diversity Analysis ◽

Cry Genes

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Construction and Characterization of a Recombinant Bacillus thuringiensis subsp. israelensis Strain That Produces Cry11B

Journal of Invertebrate Pathology ◽

10.1006/jipa.2001.5038 ◽

2001 ◽

Vol 78 (1) ◽

pp. 37-44 ◽

Cited By ~ 31

Author(s):

Hyun-Woo Park ◽

Armelle Delécluse ◽

Brian A Federici

Keyword(s):

Bacillus Thuringiensis ◽

Bacillus Thuringiensis Subsp

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Characterization of a novel Bacillus thuringiensis toxin active against Aedes aegypti larvae

Acta Tropica ◽

10.1016/j.actatropica.2021.106088 ◽

2021 ◽

pp. 106088

Author(s):

Jiangyu Wu ◽

Li Wei ◽

Jiali He ◽

Kang Fu ◽

Xinxin Li ◽

...

Keyword(s):

Bacillus Thuringiensis ◽

Aedes Aegypti ◽

Bacillus Thuringiensis Toxin

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Purification and characterization of an exochitinase from Bacillus thuringiensis subsp. aizawai and its action against phytopathogenic fungi

Canadian Journal of Microbiology ◽

10.1139/w06-019 ◽

2006 ◽

Vol 52 (7) ◽

pp. 651-657 ◽

Cited By ~ 49

Author(s):

Luis Morales de la Vega ◽

J Eleazar Barboza-Corona ◽

Maria G Aguilar-Uscanga ◽

Mario Ramírez-Lepe

Keyword(s):

Bacillus Thuringiensis ◽

Sodium Dodecyl ◽

Sclerotium Rolfsii ◽

Phytopathogenic Fungi ◽

Purification And Characterization ◽

Chitinolytic Enzyme ◽

Bacillus Thuringiensis Subsp ◽

Sds Page ◽

Fusarium Sp

A chitinolytic enzyme from Bacillus thuringiensis subsp. aizawai has been purified and its molecular mass was estimated ca. 66 kDa by sodium dodecyl sulfate – polyacryamide gel electrophoresis (SDS–PAGE). The enzyme was able to hydrolyze chitin to chitobiosides but not carboxymethylcellulose, cellulose, pullulan, and laminarin. Optimal pH and temperature were detected at 6 and 50 °C, respectively. Stability, in the absence of substrate, was observed at temperatures less than 60 °C and pH between 5 and 8. Enzyme activity was significantly inhibited by K+ and EDTA and completely inhibited by Hg2+. Purified chitinase showed lytic activity against cell walls from six phytopathogenic fungi and inhibited the mycelial growth of both Fusarium sp. and Sclerotium rolfsii. The biocontrol efficacy of the enzyme was tested in the protection of bean seeds infested with six phytopathogenic fungi.Key words: chitinase, Bacillus thuringiensis, purification, phytopathogenic fungi.

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