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

2021 ◽  
pp. 107657
Author(s):  
Hejia Ni ◽  
Jian Wang ◽  
Yawen Shen ◽  
Xiaoxue Yang ◽  
Jun Cui ◽  
...  
1981 ◽  
Vol 256 (6) ◽  
pp. 3000-3004
Author(s):  
L.A. Bulla ◽  
K.J. Kramer ◽  
D.J. Cox ◽  
B.L. Jones ◽  
L.I. Davidson ◽  
...  

2007 ◽  
Vol 53 (2) ◽  
pp. 284-290 ◽  
Author(s):  
Sonia Chehimi ◽  
François Delalande ◽  
Sophie Sablé ◽  
Mohamed-Rabeh Hajlaoui ◽  
Alain Van Dorsselaer ◽  
...  

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.


2013 ◽  
Vol 64 (1) ◽  
pp. 85-98 ◽  
Author(s):  
Ramasamy Asokan ◽  
Hanchipura Mallesh Mahadeva Swamy ◽  
Geetha G. Thimmegowda ◽  
Riaz Mahmood

Acta Tropica ◽  
2021 ◽  
pp. 106088
Author(s):  
Jiangyu Wu ◽  
Li Wei ◽  
Jiali He ◽  
Kang Fu ◽  
Xinxin Li ◽  
...  

2006 ◽  
Vol 52 (7) ◽  
pp. 651-657 ◽  
Author(s):  
Luis Morales de la Vega ◽  
J Eleazar Barboza-Corona ◽  
Maria G Aguilar-Uscanga ◽  
Mario Ramírez-Lepe

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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