Amylolytic activity and its parametric optimization of an endophytic bacterium Bacillus subtilis with an ethno-medicinal origin

Biologia ◽  
2015 ◽  
Vol 70 (3) ◽  
Author(s):  
Dina Barman ◽  
Mamtaz Sahana Dkhar

AbstractAmylolytic enzymes are a starch hydrolyzing important group of industrial enzymes with a multi-dimensional utility. In the present study, endophytic bacteria were isolated from Potentilla fulgens Wall. and screened for their amylolytic activity. Out of total 13 endophytic bacteria isolated, 3 of them showed positive results for amylolytic activity, i.e. production of halo zone against blue background in starch-containing media. The most promising isolate was identified as Bacillus subtilis subsp. inaquosorum PR

2017 ◽  
Vol 13 (1) ◽  
pp. 37-44 ◽  
Author(s):  
Elsayed Fathi Abd_Allah ◽  
Abdulaziz A. Alqarawi ◽  
Abeer Hashem ◽  
Ramalingam Radhakrishnan ◽  
Asma A. Al-Huqail ◽  
...  

2012 ◽  
Vol 194 (11) ◽  
pp. 893-899 ◽  
Author(s):  
Natalia Malfanova ◽  
Laurent Franzil ◽  
Ben Lugtenberg ◽  
Vladimir Chebotar ◽  
Marc Ongena

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Naomi Shimokawa-Chiba ◽  
Claudia Müller ◽  
Keigo Fujiwara ◽  
Bertrand Beckert ◽  
Koreaki Ito ◽  
...  

AbstractRescue of the ribosomes from dead-end translation complexes, such as those on truncated (non-stop) mRNA, is essential for the cell. Whereas bacteria use trans-translation for ribosome rescue, some Gram-negative species possess alternative and release factor (RF)-dependent rescue factors, which enable an RF to catalyze stop-codon-independent polypeptide release. We now discover that the Gram-positive Bacillus subtilis has an evolutionarily distinct ribosome rescue factor named BrfA. Genetic analysis shows that B. subtilis requires the function of either trans-translation or BrfA for growth, even in the absence of proteotoxic stresses. Biochemical and cryo-electron microscopy (cryo-EM) characterization demonstrates that BrfA binds to non-stop stalled ribosomes, recruits homologous RF2, but not RF1, and induces its transition into an open active conformation. Although BrfA is distinct from E. coli ArfA, they use convergent strategies in terms of mode of action and expression regulation, indicating that many bacteria may have evolved as yet unidentified ribosome rescue systems.


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