Production and Characterization of Bioemulsifiers by Thermotolerant Bacteria for Enhanced Oil Recovery Potential

2012 ◽  
Vol 450-451 ◽  
pp. 573-581
Author(s):  
Yang Li ◽  
Cheng Gang Zheng

Three bacterial strains were isolated from oil contaminated soil samples in Yumen oilfield of China and selected due to their capacity of growing under extreme conditions and production of bioemulsifier. The isolates were identified as Brevibacillus sp. XS1, Geobacillus sp. XS2 and Geobacillus sp. XS3 according to 16S rDNA sequence and physiological methods, respectively. The isolates XS1, XS2 and XS3 were thermotolerant with the optimum growth temperature of 50 °C, 60 °C and 55 °C, respectively. All the three isolates were able to produce bioemulsifiers which had little effect on surface tension reduction. The bioemusifiers produced by the three isolates were purified with a production yield of 2.98g/L, 4.24g/L and 3.82 g/L, respectively. The bioemulsifiers were identified as anionic heteropolysaccharides by FTIR analysis and their average molecular weight and polydispersity were investigated by GPC method. The bioemulsifiers produced by Geobacillus sp. XS2 and XS3 exhibited a perfect stability over various temperature (up to 100 °C), pH (range from 2.0 to 12.0) and salinity (up to 30.0% of NaCl concentration) and were considered to be ideal candidates in MEOR process.

Catalysts ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 1262
Author(s):  
Rabia Saleem ◽  
Safia Ahmed

As significant biocatalyst, L-glutaminases find potential applications in various fields, from nourishment to the pharmaceutical industry. Anticancer activity and flavor enhancement are the most promising applications of L-glutaminases. In this study, L-glutaminase was isolated and purified from an old glutamine sample. A selected bacterial isolate was characterized taxonomically by morphological characters, biochemical testing and 16S rDNA sequence homology testing. The taxonomical characterization of the isolate identified it as Achromobacter xylosoxidans strain RSHG1. The isolate showed maximum enzyme production at 30 °C, pH 9, with Sorbitol as a carbon source and L-Glutamine as a nitrogen and inducer source. L-Glutaminsae was purified by using column chromatography on a Sephadex G-75. The enzyme has a molecular weight of 40 KDa, pH optimal 7 and is stable in the pH range of 6–8. The optimum temperature for the catalyst was 40 °C and stable at 35–50 °C. The kinetic studies of the purified L-glutaminase exhibited Km and Vmax of 0.236 mM and 443.8 U/mg, respectively. L-Glutaminase activity was increased when incubated with 20 mM CaCl2, BaCl2, ZnSO4, KCl, MgSO4 and NaCl, whereas EDTA, CoCl2, HgCl, ZnSO4 and FeSO4 decreased the activity of the enzyme. The addition of 8% NaCl enhanced the glutaminase activity. L-Glutaminase immobilized on 3.6% agar was stable for up to 3 weeks.


1999 ◽  
Vol 62 (8) ◽  
pp. 899-904 ◽  
Author(s):  
M. E. JANES ◽  
R. NANNAPANENI ◽  
M. G. JOHNSON

Two bacteriocin-producing bacterial strains were isolated from garlic and ginger root by the agar overlay method. The bacteria were identified by 16S rRNA sequence analyses and fermentation patterns as Leuconostoc mesenteroides (garlic isolate) and Lactococcus lactis (ginger isolate). The bacteriocins were assigned the names leucocin BC2 and lactocin GI3, respectively. Physiochemical properties and antimicrobial spectra of the bacteriocins were determined by the spot-on-lawn method. Both bacteriocins were inhibited by proteolytic enzymes. Leucocin BC2 exhibited a narrow antimicrobial spectrum, inhibiting only Bacillus, Enterococcus, and Listeria species. Lactocin GI3 had a broader spectrum, inhibiting Bacillus, Clostridium, Listeria, Enterococcus, Leuconostoc, Pediococcus, and Staphylococcus species. Both bacteriocins remained active when heated at 90°C for 15 min or 120°C for 20 min. Leucocin BC2 assayed at 37°C showed an inhibitory activity of 1,600 AU/ml, whereas at 8°C the activity was 12,800 AU/ml. Conversely, lactocin GI3 activity was the same at both assay temperatures. Both bacteriocins remained active over a pH range of 2.0 to 9.0 and in various organic solvents. The activity of leucocin BC2 was increased when treated with 0.5% acetic acid and 0.5% lactic acid, whereas lactocin GI3 activity was decreased with either acid. The molecular mass values were 3.7 kDa for leucocin BC2 and 3.9 kDa for lactocin GI3. These results show that the inhibitory substances produced by the bacteria isolated from garlic and ginger are bacteriocins that appear to be different in some characteristics from previously reported bacteriocins.


2011 ◽  
Vol 183-185 ◽  
pp. 839-843
Author(s):  
Mei Hui Du ◽  
Min Zhao ◽  
Lei Lu ◽  
Tian Nv Wang ◽  
Tai Lun Li ◽  
...  

A newly isolated strain LS02 was estimated for its ability in dye decolorization. The LS02 strain was identified as Bacillus subtilis by the combination of physicochemical tests and 16S rDNA sequence analysis. The isolated strain could oxidize the laccase substrate syringaldazine, indicating the existence of laccase activity. B. subtilis LS02 grown well in the pH range of 5.0~9.0, and showed an optimum growth temperature at 37°C. Indigo carmine could be completely decolorized by B. subtilis LS02 after 4 days, whereas Remazol Brilliant Blue R, reactive black 5 and crystal violet were poorly decolorized. The result indicated that the laccase of B. subtilis LS02 may be suitable for the application in textile bleaching of indigo carmine.


2018 ◽  
Vol 62 (1) ◽  
pp. 75-82 ◽  
Author(s):  
Riddha Mukherjee ◽  
Tanmay Paul ◽  
Suman Kumar Halder ◽  
Jyoti Prakash Soren ◽  
Amrita Banerjee ◽  
...  

An acidophilic α-amylase from Aspergillus niger RBP7 was purified after solid state fermentation on potato peel substrate. Molecular mass of the purified α-amylase was 37.5 kDa and it exhibited 1.4 mg/ml and 0.992 μ/mol/min Km and Vmax values, respectively. The enzyme was stable in the pH range from 2.0 to 6.0, at high NaCl concentration (3 M) and at temperatures between 40 °C and 70 °C. The enzyme showed an optimal activity at pH 3.0 and at 45 °C. The enzyme was inhibited by Hg2+ and was stable in the presence of different surfactants (Tween 60, Tween 80, and SDS at 1% level) and different inhibitory reagents (β-mercaptoethanol, phenylmethylsulfonyl fluoride, and sodium azide). This acidophilic amylase enzyme can digest heterogeneous food materials, i.e. the mixture of rice, fish, bread and curry with comparable activity to the commercial diastase enzymes available.


2011 ◽  
Vol 183-185 ◽  
pp. 773-777 ◽  
Author(s):  
Jun Bo Pan ◽  
Min Zhao ◽  
Lei Lu ◽  
Mei Hui Du ◽  
Guo Fu Li ◽  
...  

Bacterial strains exhibiting laccase activity were isolated from the forest soil. A strain LC02 with syringaldazine oxidation ability was obtained using enrichment medium supplemented with copper ions. The isolated strain was identified as Bacillus amyloliquefaciens using physiological and biochemical tests as well as 16S rDNA sequence analysis. The characterization of spore laccase activity was investigated. The result showed that the optimum pH and temperature of the enzyme was 6.6 and 70°C, respectively. A great thermostability was observed for the spore laccase at 70°C. Laccase activity was strongly inhibited by 0.1 mmol/L NaN3, dithiothreitol and cysteine.


1994 ◽  
Vol 6 (3) ◽  
pp. 201-208 ◽  
Author(s):  
Jayesh R Patel ◽  
Dipan H Sutaria ◽  
Magan N Patel

The present paper reports the synthesis and characterization of a copolymer, The copolymer sample was synthesized by Friedel-Crafts polycondensation of 2-hydroxy-4 ethoxypropiophenone with 1,3-propane diol in the presence of polyphosphoric acid catalyst. The copolymer was characterized by elemental analysis, IR spectroscopy and viscosity study, and its number-average molecular weight (M) was determined by non-aqueous titration and found to be 2855 g mol- 1. Chelation ion-exchange properties have also been studied, employing a batch-equilibration method. It was employed to study selectivity of metal ion uptake over a wide pH range and in media of various ionic strengths. The overall rate of metal uptake follows the order UOl + > Fe3 + > Cu2 + > Ni2 +.


2016 ◽  
Vol 17 (3) ◽  
pp. 792-798 ◽  
Author(s):  
Taketoshi Shimizu ◽  
Takuya Oda ◽  
Hiroyuki Ito ◽  
Ichiro Imai

Algicidal bacteria that attack Dolichospermum crassum were isolated from the Karasuhara Reservoir in October 2010. Phytoplankton monitoring was performed from April 2010 to March 2011, and D. crassum was detected from August to November. At its peak frequency (in early October), it accounted for 23% of all phytoplankton cells. Heterotrophic bacteria were isolated from the surface water, and an algicidal assay was conducted. As a result, 3 out of 47 bacterial strains showed strong algicidal activity, and they completely destroyed the trichomes of D. crassum. An initial inoculation dose of only 1.0 × 102 cells ml−1 of these strains was enough to digest D. crassum. These strains were identified as Rheinheimera spp. according to 16S rDNA sequence analyses. This is the first report about algicidal bacteria that attack D. crassum. Algicidal bacteria could be key agents for controlling D. crassum in reservoirs.


2018 ◽  
Vol 15 (2) ◽  
pp. 373-380
Author(s):  
Nguyễn Kim Thoa ◽  
Trần Thị Hoa ◽  
Trần Đình Mấn ◽  
Tạ Thị Thu Thuỷ

Binh Chau is famous for being a rare open-air hot spring with the highest mouth temperature in Vietnam. From water and sludge samples collected in Binh Chau hot spring, 64 aerobic thermophilic bacterial strains were isolated. Based on the identified characteristics of Bacillus genus, the optimum growth temperature as well as the ability to hydrolyze starch, 22 strains belonging to Geobacillus genus were selected for study on their α-amylase properties. Alpha-amylase from 11 of 22 strains showed pHopt ≥ 7. The optimum temperature of α–amylase ranged from 50oC to 90oC in different strains, of which seven strains showed the Topt of α–amylase at 90 oC. Thermostability of these strains at 90oC was identified, showing the half life of the three most prominent strains TĐ3.2, TG2.2, TG3.7 strains at 5.5 hours, 3.25 hours and 6.5 hours, respectively. Moreover, the addition of 5 mM Ca2+ resulted in improving α–amylase activity of 4 strains (TĐ3.2, TG2.2, TG3.1 and TG3.7) from 1,15 - 1,55 times, as well as in increasing thermostability of all enzymes produced by 7 strains with their new half life varied from 2-7 houts. Comparative analyses of sequences of 16S rRNA gene from the TĐ3.2, TG2.2, TG3.7 strains indicated that they were most closely related to G. caldoxilosilyticus, G. thermoglucosidasius, and G. stearothermophilus respectively (with the homology of 99%, 98% and 99%, respectively). Thus, it could be assumed that the genetic materials of microorganisms in Binh Chau hot spring are of great interest of exploitation in very near future.


1974 ◽  
Vol 31 (01) ◽  
pp. 072-085 ◽  
Author(s):  
M Kopitar ◽  
M Stegnar ◽  
B Accetto ◽  
D Lebez

SummaryPlasminogen activator was isolated from disrupted pig leucocytes by the aid of DEAE chromatography, gel filtration on Sephadex G-100 and final purification on CM cellulose, or by preparative gel electrophoresis.Isolated plasminogen activator corresponds No. 3 band of the starting sample of leucocyte cells (that is composed from 10 gel electrophoretic bands).pH optimum was found to be in pH range 8.0–8.5 and the highest pH stability is between pH range 5.0–8.0.Inhibition studies of isolated plasminogen activator were performed with EACA, AMCHA, PAMBA and Trasylol, using Anson and Astrup method. By Astrup method 100% inhibition was found with EACA and Trasylol and 30% with AMCHA. PAMBA gave 60% inhibition already at concentration 10–3 M/ml. Molecular weight of plasminogen activator was determined by gel filtration on Sephadex G-100. The value obtained from 4 different samples was found to be 28000–30500.


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