scholarly journals Bacterial Endo-Symbiont Inhabiting Tridax procumbens L. and Their Antimicrobial Potential

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Syed Baker ◽  
Kumara Shanthamma Kavitha ◽  
Huvinakola Chinnappa Yashavantha Rao ◽  
Devaraju Rakshith ◽  
Ballagere Puttaraju Harini ◽  
...  

Bacterial symbionts inhabiting Tridax procumbens L. were screened for antimicrobial potential with the aim to isolate potent bacteria bearing significant activity against test pathogens. The selected isolate was subjected to large scale fermentation to extract antimicrobial metabolite. The organic phase was reduced under vacuum pressure and crude ethyl acetate extract (10 mg/mL) was evaluated for antimicrobial activity against panel of test pathogens. The antibacterial activity was measured as a zone of inhibition and compared with standard antibiotics, gentamicin and tetracycline. Similarly, antifungal activity was compared with miconazole and bavistin. Significant activity was conferred against Shigella flexneri (MTCC 731) with 27±1.5 mm zone across the disc. Partially, purification of antimicrobial metabolite with TLC-bioautography and HPLC resulted in active fraction bearing activity at Rf 0.65 and eluting between 4 and 5 retention times. The obtained results are promising enough for future purification and characterization of antimicrobial metabolite. Thus, the study attributes to the growing knowledge on endophytes as one of the rich sources of antimicrobial potentials.

1982 ◽  
Vol 217 (2) ◽  
pp. 574-581 ◽  
Author(s):  
Kunio S. Misono ◽  
Leslie A. Holladay ◽  
Kazuo Murakami ◽  
Kenji Kuromizu ◽  
Tadashi Inagami

2006 ◽  
Vol 44 (1) ◽  
pp. 35 ◽  
Author(s):  
Maja Christiansen ◽  
Charlotte S. Jørgensen ◽  
Inga Laursen ◽  
Lisbeth B. Krogsøe ◽  
Peter Højrup ◽  
...  

1988 ◽  
Vol 16 (14) ◽  
pp. 6397-6410 ◽  
Author(s):  
D. Bhattacharyya ◽  
K. Tano ◽  
G.J. Bunick ◽  
E.C. Uberbacher ◽  
W.D. Behnke ◽  
...  

Vaccine ◽  
2009 ◽  
Vol 27 (42) ◽  
pp. 5855-5864 ◽  
Author(s):  
Debasis Pore ◽  
Pinki Chowdhury ◽  
Nibedita Mahata ◽  
Amit Pal ◽  
Shinji Yamasaki ◽  
...  

2017 ◽  
Vol 64 (4) ◽  
pp. 509-518 ◽  
Author(s):  
Liang-hua Chen ◽  
Feng Cai ◽  
Dan-ju Zhang ◽  
Li Zhang ◽  
Peng Zhu ◽  
...  

1988 ◽  
Vol 55 (1) ◽  
pp. 97-107 ◽  
Author(s):  
Efstathios Alichanidis

SummaryAn extracellular metalloproteinase from Aeromonas hydrophila strain A4, isolated from milk, was purified by a factor of 300 by chromatogrpahy on DEAE-cellulose and Sephadex G-150. The enzyme had a mol. wt of 43000 and contained 2 g atom Ca/mol. It was active over a pH range 4·8–9·5 and had optimum activity on casein at pH 7·0 with Km = 0·17 mM. It was strongly inactivated by metal chelators and the apoenzyme was fully reactivated with Ca2+, Mn2+ or Co2+. Heavy metal ions such as Ag+, Hg2+, Fe2+, Zn2+, Cd2+, Ni2+ and Cu2+ totally or partly inactivated the enzymic activity at 5 mM concentration. The enzyme was not inactivated by diisopropylfluorophosphate, soyabean trypsin inhibitor or sulphydryl group reagents. It was optimally active at 45 °C; above 50 °C activity declined rapidly, but significant activity persisted at 4 °C. It was heat labile in phosphate or Tris-maleate buffer but exogenous Ca2+ afforded protection.


1986 ◽  
Vol 237 (2) ◽  
pp. 415-420 ◽  
Author(s):  
C R Goward ◽  
R Hartwell ◽  
T Atkinson ◽  
M D Scawen

Homogeneous glucokinase (EC 2.7.1.2) from the thermophile Bacillus stearothermophilus was isolated on the large scale by using four major steps: precipitation of extraneous material at pH 5.5, ion-exchange chromatography on DEAE-Sepharose, pseudo-affinity chromatography on Procion Brown H-3R-Sepharose 4B and gel filtration on Ultrogel AcA 34. The purified enzyme had a specific activity of about 330 units/mg of protein and was shown to exist as a dimer of subunit Mr 33,000. Kinetic parameters for the enzyme were determined with a variety of substrates. The glucokinase was highly specific for alpha-D-glucose, and the only other sugar substrate utilized was N-acetyl-alpha-D-glucosamine. The enzyme shows Michaelis-Menten kinetics, with a Km value of 150 microM for alpha-D-glucose. The glucokinase was maximally active at pH 9.0.


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