Characterization of chitinase genes orginated from Serratia marcescens and their additive insecticidal activities to Bacillus thuringiensis strains

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Remziye Nalcacioglu ◽  
Kazim Sezen ◽  
Zihni Demirbag
2003 ◽  
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Noriko Shisa ◽  
Naoya Wasano ◽  
Akira Ohgushi ◽  
Michio Ohba

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Ji Young Choi ◽  
Cha Young Kim ◽  
Yong Hwa Cheong ◽  
Young Ju Choi ◽  
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Roda Al-Thani ◽  
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Najeh Belguith-Ben Hassan ◽  
Lobna Abdelkefi-Mesrati ◽  
...  

1981 ◽  
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pp. 3000-3004
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L.A. Bulla ◽  
K.J. Kramer ◽  
D.J. Cox ◽  
B.L. Jones ◽  
L.I. Davidson ◽  
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François Delalande ◽  
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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.


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