scholarly journals Antibiogram Analysis and Characterization of Bacterial Pathogens from Leucorrhea Patients

2019 ◽  
pp. 1-13
Author(s):  
Nazish Mazhar Ali ◽  
Muhammad Shahzad ◽  
Muqadas Bano ◽  
Iram Liaqat ◽  
Bushra Mazhar ◽  
...  
Keyword(s):  
Research Work ◽  
Optimum Temperature ◽  
Bacterial Strains ◽  
Biochemical Tests ◽  
Plate Method ◽  
Sterile Culture ◽  
Escherchia Coli ◽  
Optimum Ph ◽  
L1 And L2

In recent research work bacteria were isolated from samples of leucorrhea patients admitted in Lady Wellington hospital Lahore (gynae ward) and Basheer welfare hospital Shahdara Lahore. The sampling was done from pregnant and non-pregnant leucorrhea patients aged 18 to 30 years by using sterile culture sticks from vagina. The samples were spread on agar plates and incubated for overnight, bacterial strains were isolated by streak plate method. The strains were named L1, L2, L3 and L4. Identification was carried out by various morphological and biochemical tests. Molecular characterization was also done to characterize bacteria up to species level. L1 strain was identified as Streptococcus pyogens, L2 as Staphylococcus aureus, L3 as Neisseria gonorrheae and L4 as Escherchia coli. Antibiotic resistance was analyzed by disc plate method.  L1, L2 and L3 strains showed maximum sensitivity with Cefepime antibiotics having values 17.74 µg/ml, 13.63 µg/ml and 12 µg/ml respectively. L4 showed max sensitivity with Azithromycin and Cloxacillin antibiotics i.e., 6.25 µg/ml and 6.4 µg/ml respectively. Optimum pH was 6.5 for L1 and L2, while 7 for L3 and L4. Optimum temperature was 37 for all strains.

Immobilization and Characterization of Tannase and its Haze-removing

2009 ◽  
Vol 15 (6) ◽  
pp. 545-552 ◽  
Author(s):  
Erzheng Su ◽  
Tao Xia ◽  
Liping Gao ◽  
Qianying Dai ◽  
Zhengzhu Zhang
Keyword(s):  
Kinetic Parameter ◽  
High Activity ◽  
Green Tea ◽  
Storage Stability ◽  
Residual Activity ◽  
Black Tea ◽  
Optimum Temperature ◽  
Oolong Tea ◽  
Optimum Ph

Tannase was effectively immobilized on alginate by the method of crosslinking-entrapment-crosslinking with a high activity recovery of 76.6%. The properties of immobilized tannase were investigated. Its optimum temperature was determined to be 35 ° C, decreasing 10 °C compared with that of free enzyme, whereas the optimum pH of 5.0 did not change. The thermal and pH stabilities of immobilized tannase increased to some degree. The kinetic parameter, Km, for immobilized tannase was estimated to be 11.6 × 10-4 mol/L. Fe2+ and Mn2+ could activate the activity of immobilized tannase. The immobilized tannase was also applied to treat the tea beverage to investigate its haze-removing effect. The content of non-estern catechins in green tea, black tea and oolong tea increased by 52.17%, 12.94% and 8.83%, respectively. The content of estern catechins in green tea, oolong tea and black tea decreased by 20.0%, 16.68% and 5.04%, respectively. The anti-sediment effect of green tea infusion treated with immobilized tannase was significantly increased. The storage stability and reusability of the immobilized tannase were improved greatly, with 72.5% activity retention after stored for 42 days and 86.9% residual activity after repeatedly used for 30 times.

scholarly journals CHARACTERIZATION OF BACTERIA ASSOCIATED WITH PNEUMONIA IN BLACK BENGAL GOATS

2012 ◽  
Vol 9 (1) ◽  
pp. 67-71 ◽  
Author(s):  
MA Momin ◽  
MA Islam ◽  
MM Khatun ◽  
MM Rahman ◽  
MA Islam
Keyword(s):  
Antimicrobial Agents ◽  
Research Work ◽  
Nutrient Agar ◽  
Blood Agar ◽  
Biochemical Tests ◽  
Highly Sensitive ◽  
Golden Yellow ◽  
Agar Media ◽  
Staphylococcus Spp

The present research work was undertaken for the characterization of the bacterial pathogens responsible for pneumonia in black Bengal goats. Nasal swab samples (n = 50) were collected from the pneumonic black Bengal goats in Mymensingh and Sirajgonj districts. Samples were inoculated onto nutrient agar, eosin methylene blue (EMB) agar, MacConkey agar, and blood agar media for isolation of bacteria. Identification of bacteria was performed by the Gram's staining method, cultural properties and biochemical tests. Antibiotic sensitivity of bacterial isolates was performed against 11 antimicrobial agents. Pasteurella spp were isolated from 25 cases, and Staphylococcus spp from 13 cases. Mixed infection caused by the Pasteurella spp and Staphylococcus spp. were recorded in 12 cases. Pasteurella spp produced whitish, opaque circular and translucent colonies on nutrient agar, smooth, convex, glistening colonies on EMB agar and no hemolysis on blood agar. Staphylococcus spp have shown gray white or golden yellowish colonies on  nutrient agar. Golden yellow colonies without hemolysis or whitish colonies with hemolysis were also produced by Staphylococcus spp. on the blood agar media. Pasteurella spp were indole positive, MR-VP negative and ferment dextrose, sucrose and mannitol with the production of acid. The Staphylococcus spp were positive to MR-VP, coagulase and catalase reactions, negative to indole test and fermented five basic sugars with acid production. Results of cultural and biochemical tests supported that these two isolates belonged to P. multocida and S. aureus. P. multocida were highly sensitive to ciprofloxacin and resistant to penicillin. S. aureus found to be highly sensitive to erythromycin, tetracycline, enrofloxacin, and norfloxacin and less sensitive to amoxicillin. DOI = http://dx.doi.org/10.3329/bjvm.v9i1.11215Bangl. J. Vet. Med. (2011). 9(1): 67-71 

scholarly journals Characterization of Biosynthetic Enzymes for Ectoine as a Compatible Solute in a Moderately Halophilic Eubacterium, Halomonas elongata

1999 ◽  
Vol 181 (1) ◽  
pp. 91-99 ◽  
Author(s):  
Hisayo Ono ◽  
Kazuhisa Sawada ◽  
Nonpanga Khunajakr ◽  
Tao Tao ◽  
Mihoko Yamamoto ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Apparent Molecular Mass ◽  
Optimum Temperature ◽  
Sds Page ◽  
Halomonas Elongata ◽  
Optimum Ph

ABSTRACT 1,4,5,6-Tetrahydro-2-methyl-4-pyrimidinecarboxylic acid (ectoine) is an excellent osmoprotectant. The biosynthetic pathway of ectoine from aspartic β-semialdehyde (ASA), in Halomonas elongata, was elucidated by purification and characterization of each enzyme involved. 2,4-Diaminobutyrate (DABA) aminotransferase catalyzed reversively the first step of the pathway, conversion of ASA to DABA by transamination with l-glutamate. This enzyme required pyridoxal 5′-phosphate and potassium ions for its activity and stability. The gel filtration estimated an apparent molecular mass of 260 kDa, whereas molecular mass measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was 44 kDa. This enzyme exhibited an optimum pH of 8.6 and an optimum temperature of 25°C and had Km s of 9.1 mM forl-glutamate and 4.5 mM for dl-ASA. DABA acetyltransferase catalyzed acetylation of DABA to γ-N-acetyl-α,γ-diaminobutyric acid (ADABA) with acetyl coenzyme A and exhibited an optimum pH of 8.2 and an optimum temperature of 20°C in the presence of 0.4 M NaCl. The molecular mass was 45 kDa by gel filtration. Ectoine synthase catalyzed circularization of ADABA to ectoine and exhibited an optimum pH of 8.5 to 9.0 and an optimum temperature of 15°C in the presence of 0.5 M NaCl. This enzyme had an apparent molecular mass of 19 kDa by SDS-PAGE and a Km of 8.4 mM in the presence of 0.77 M NaCl. DABA acetyltransferase and ectoine synthase were stabilized in the presence of NaCl (>2 M) and DABA (100 mM) at temperatures below 30°C.

ISOLATION AND CHARACTERIZATION OF BIOTECHNOLOGY RELEVANT BACTERIA FROM MARINE ENVIRONMENT

2015 ◽  
Vol 77 (31) ◽  
Author(s):  
Suganthi Thevarajoo ◽  
Chitra Selvaratnam ◽  
Kian Mau Goh ◽  
Fazilah Abd. Manan ◽  
Zaharah Ibrahim ◽  
...  
Keyword(s):  
16S Rrna ◽  
Marine Environment ◽  
Antibiotic Sensitivity ◽  
Marine Microorganisms ◽  
Bacterial Strains ◽  
Biochemical Tests ◽  
16S Rrna Sequence ◽  
Gram Staining ◽  
Isolation And Characterization

Marine environment remained as largely unexplored source for researchers to discover marine microorganisms with novel properties. This study aims to isolate marine bacteria from the seashore of Desaru, Malaysia. Totally, six bacterial strains were successfully obtained and were identified by complete 16S rRNA sequencing. The characterizations of bacterial strains were performed based on morphological tests, Gram-staining, biochemical tests, and antibiotic sensitivity. The 16S rRNA sequence of D-2, D-4, D-7, D-15, D-31, and D-33 revealed a high identity of 97 to 99% with taxa belong to genera of Pseudomonas, Marinomonas, Exiquobacterium, Micrococcus, Pseudoalteromonas, and Shewanella respectively. Strain D-31 exhibited higher tolerance towards antibiotics kanamycin, ampicillin, and erythromycin while the growth of other strains were retarded by at least two of these antibiotics. We further characterized strain D-4 and D-31 that belonged to Marinomonas sp. and Pseudoalteromonas sp.. Both genera are interesting as earlier researchers have discovered new antibacterial substances, industrial enzymes and unique secondary metabolites.

scholarly journals Purification and characterization of endoglucanase Ss from Clostridium thermocellum

1991 ◽  
Vol 279 (1) ◽  
pp. 67-73 ◽  
Author(s):  
U Fauth ◽  
M P M Romaniec ◽  
T Kobayashi ◽  
A L Demain
Keyword(s):  
Clostridium Thermocellum ◽  
Hydrophobic Interaction Chromatography ◽  
Cellulolytic Enzymes ◽  
Crystalline Cellulose ◽  
Optimum Temperature ◽  
Purification And Characterization ◽  
Specific Antibodies ◽  
Optimum Ph ◽  
Exchange Adsorption

The extracellular cellulolytic enzymes of the thermophilic anaerobe Clostridium thermocellum occur as a protein complex or aggregate known as the cellulosome. By using a combination of ion-exchange, adsorption and hydrophobic-interaction chromatography, it was possible to isolate from extracellular broth a specific endoglucanase of interest without the use of denaturants. The endoglucanase was identified as the cellulosomal subunit Ss by the use of specific antibodies. The enzyme has an Mr of 83,000, an isoelectric point of 3.55, optimum pH of 6.6 and optimum temperature of 70 degrees C. It hydrolyses CM-cellulose and, at a higher rate, the cellodextrins, cellotetraose and cellopentaose, but does not hydrolyse a crystalline cellulose such as Avicel. Cellobiose and cellotriose are also immune to attack. It differs from endoglucanases previously isolated by others and a 76,000-Mr endoglucanase recently isolated in this laboratory.

scholarly journals The Properties of Immobilized Invertase Onto a New Support Material; Poly(Methacrylamide/Maleic Acid) Copolymeric Hydrogel

2018 ◽  
Vol 26 (2) ◽  
pp. 307-328 ◽  
Author(s):  
Hesna Nursevin Öztop ◽  
Fatma Banu Çatmaz ◽  
Dursun Saraydin
Keyword(s):  
Maleic Acid ◽  
Storage Stability ◽  
Maximum Velocity ◽  
Optimum Temperature ◽  
Michaelis Constant ◽  
Ph Values ◽  
Optimum Ph ◽  
And Storage ◽  
And Diffusion

Abstract Poly (methacrylamide / maleic acid) PM/MA and poly (methacrylamide) PM hydrogels were prepared aiming to be used as a support for invertase. Spectrophotometric, thermal analysis methods, swelling and diffusion experiments were used for the characterization of hydrogels. The swelling of PM/MA was higher than that of PM in water. The diffusion of water within the hydrogel was found to be non-Fickian. Invertase was immobilized onto PM and PM/MA (samples named PM-I and PM/MA-I respectively). The optimum pH values were found to be; 6.0, 5.0 and 5.5 for free invertase, PM-I and PM/MA-I respectively. The optimum temperature values were found to be 30 °C, 35 °C and 40 °C for free invertase, PM-I and PM/MA-I respectively. The Michaelis constant (Km) and maximum velocity of the enzymes (Vmax) were Km: 11,75 mM, Vmax: 1,95 μmol min−1 for free invertase, Km: 67,24 mM, Vmax: 60,6 μmol min−1 for PM-I and Km: 74,55 mM, Vmax: 18,12 μmol min−1 for PM/MA-I. PM/MA-I showed excellent thermal, operational and storage stability.

scholarly journals The Utilization of Rum Slops by Marine Bacteria. II. Characterization of Efficient Strains.

1969 ◽  
Vol 63 (2) ◽  
pp. 189-194
Author(s):  
D. R. Hale ◽  
T. R. Tosteson
Keyword(s):  
Molecular Weight ◽  
Sea Water ◽  
Necessary Condition ◽  
Bacterial Isolates ◽  
Bacterial Strains ◽  
Biochemical Tests ◽  
Marine Communities ◽  
Water Media ◽  
Physiological And Biochemical

Twenty bacterial isolates from selected marine communities were obtained employing solid, modified sea water media contain ing slops. Thirteen basic morphological, cytological, physiological and biochemical tests were conducted to characterize six of the strains that grew most successfully on the slops media. The ability to hydrolyze high molecular weight sugars and proteins appears to be a necessary condition for the successful growth of some of these isolates on slops media. Tentative identifications of these bacterial strains were made.

scholarly journals Amylolytic ability of bacteria isolated from termite (Coptotermes sp.) gut

2018 ◽  
Vol 23 (1) ◽  
pp. 14 ◽  
Author(s):  
Putri Dwi Mulyani ◽  
Radhiyah Mardhiyah Hamid ◽  
Rifqi Zahroh Janatunaim ◽  
Yekti Asih Purwestri
Keyword(s):  
Amylase Activity ◽  
Rrna Gene ◽  
Optimum Temperature ◽  
Bacterial Isolates ◽  
16S Rrna Gene Sequences ◽  
Clear Zone ◽  
Optimum Ph ◽  
Iodine Test ◽  
Brevibacillus Parabrevis

BSR 2, BSR 3, BSR 8, and BSR 9, different bacteria isolated from the termite gut, have been shown to possess cellulolytic activities, but their amylolytic ability has heretofore been unknown. This study attempted to fill in this knowledge gap. The formation of a clear zone using the iodine test showed that the bacteria were able to produce and secrete amylase. Based on the results, the best cultivation times for strains BSR 2, BSR 3, BSR 8, and BSR 9 were 6, 3, 2, and 2 d, respectively, yielding amylase activities of 2.59 ± 0.13 U/mg, 2.00 ± 0.08 U/mg, 1.67 ± 0.10 U/mg, and 1.55 ± 0.12 U/mg, respectively. BSR 2 had the highest amylase activity compared with the other bacterial isolates. The optimum ph for bacterial amylase activity of BSR 2 was 7.0, and the optimum temperature was 40°C. The molecular characterization of isolates BSR 2, BSR 3, BSR 8, and BSR 9 was based on 16S rRNA gene sequences. Isolates BSR 8 and BSR 9 were thus identified as Brevibacillus parabrevis and Brevibacillus sp. With similarities amounting to 92.48% and 95.91%, while the BSR 3 isolate was identified as Pseudomonas alcaligenes with a similarity of 94.29%, and the BSR 2 isolate could not be identified yet.

Isolation and Characterization of Laccase Activity in a Novel Bacillus amyloliquefaciens LC02

2011 ◽  
Vol 183-185 ◽  
pp. 773-777 ◽  
Author(s):  
Jun Bo Pan ◽  
Min Zhao ◽  
Lei Lu ◽  
Mei Hui Du ◽  
Guo Fu Li ◽  
...  
Keyword(s):  
Bacillus Amyloliquefaciens ◽  
Laccase Activity ◽  
Copper Ions ◽  
Bacterial Strains ◽  
Biochemical Tests ◽  
16S Rdna Sequence ◽  
16S Rdna Sequence Analysis ◽  
Isolation And Characterization ◽  
Physiological And Biochemical

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.

scholarly journals Purification and Characterization of an Extracellular Protease from Xenorhabdus nematophila Involved in Insect Immunosuppression

2002 ◽  
Vol 68 (3) ◽  
pp. 1297-1304 ◽  
Author(s):  
C. Caldas ◽  
A. Cherqui ◽  
A. Pereira ◽  
N. Simões
Keyword(s):  
Erwinia Amylovora ◽  
Steinernema Carpocapsae ◽  
Erwinia Chrysanthemi ◽  
Chromogenic Substrate ◽  
Optimum Temperature ◽  
Xenorhabdus Nematophila ◽  
Purification And Characterization ◽  
Cecropin A ◽  
Optimum Ph

ABSTRACT Xenorhabdus nematophila, a bacterium pathogenic for insects associated with the nematode Steinernema carpocapsae, releases high quantities of proteases, which may participate in the virulence against insects. Zymogram assays and cross-reactions of antibodies suggested that two distinct proteases were present. The major one, protease II, was purified and shown to have a molecular mass of 60 kDa and an estimated isoelectric point of 8.5. Protease II digested the chromogenic substrate N-tosyl-Gly-Pro-Arg-paranitroanilide (pNA) with V max and Km values of 0.0551 μM/min and 234 μM, respectively, and the substrate dl-Val-Leu-Arg-pNA with V max and Km values of 0.3830 μM/min and 429 μM, respectively. Protease II activity was inhibited 93% by Pefabloc SC and 45% by chymostatin. The optimum pH for protease II was 7, and the optimum temperature was 23°C. Proteolytic activity was reduced by 90% at 60°C for 10 min. Sequence analysis was performed on four internal peptides that resulted from the digestion of protease II. Fragments 29 and 45 are 75 and 68% identical to alkaline metalloproteinase produced by Pseudomonas aeruginosa. Fragment 29 is 79% identical to a metalloprotease of Erwinia amylovora and 75% identical to the protease C precursor of Erwinia chrysanthemi. Protease II showed no toxicity to hemocytes but destroyed antibacterial activity on the hemolymph of inoculated insects' larvae and reduced 97% of the cecropin A bacteriolytic activity.

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