View options
Result details

Results per page
Articles per page View Sort by

3 results matched your search query
Keywords = Hüseyin Kahraman

  • Open Access Research Article
    Export citation: APA   BibTeX   RIS
    Trends Journal of Sciences Research 2018, 3(2), 90-95. http://doi.org/10.31586/Biology.0302.05
    113 Views 245 Downloads PDF Full-text (2.105 MB) PDF Full-text (2.015 MB)  HTML Full-text
    Abstract
    Salinity is one of the important abiotic stress affecting microorganism growth and productivity. To survive these stresses most organisms have to stress-adaptation mechanisms. It's one of these things proline. We did not find any similar studies with P. aeruginosa and E. faecalis in our studies. The highest value for proline
    [...] Read more.
    Salinity is one of the important abiotic stress affecting microorganism growth and productivity. To survive these stresses most organisms have to stress-adaptation mechanisms. It's one of these things proline. We did not find any similar studies with P. aeruginosa and E. faecalis in our studies. The highest value for proline production at 30 ?C 100 rpm was in E. faecalis 11,074 U/ml and in E. coli 6,833 U/ml. The highest proline production in LB medium containing 37 ?C 100 rpm KCl was found to be in E. faecalis 14,604 U/ml and in E. coli 6,557 U/ml. However, there are studies with E. coli. This experiment revealed that the extracellular proline concentration is proportionally linked to the KCl stress. We should first mention that studies similar to those we were less common in the literature. We did not find any similar studies with P. aeruginosa and E. faecalis in our studies.  Full article
    Figures

    Figure 1 of 6

    References
    [1]
    Kaino T, Takagi H. Gene expression profiles and intracellular contents of stress protectants in Saccharomyces cerevisiae under ethanol and sorbitol stresses. Appl Microbiol Biotechnol.2008; 79: 273-83.
    [2]
    Takagi H. Proline as a stress protectant in yeast: physiological functions, metabolic regulations, and biotechnological applications. Appl Microbiol Biotechnol. 2008;81: 211-23.
    [3]
    Brill J, Hoffmann T, Bleisteiner M, Bremer E. Osmotically controlled synthesis of the compatible solute proline is critical for cellular defense of Bacillus subtilis against high osmolarity. J Bacteriol.2011;193(19): 5335-46.
    [4]
    Bayat RA, Ku?vuran ?, Ellialtio?lu ?, ?stun AS. Effects of proline application on antioxidative enzymes activities in the young pumpkin plants (Cucurbita pepo L. and C. moschata Poir.) under Salt Stres. Turk J Agr Nat Sci.2014; 1(1): 25-33.
    [5]
    Masuda M, Takamatu S, Nishimura N, Komatsubara S, et al. Improvement of culture conditions for l-proline production by a recombinant strain of Serratia marcescens. Appl Microbiol Biotechnol.1993;189(43):189-97.
    [6]
    Jensen JVK, Wendisch VF. Ornithine cyclodeaminase-based praline production by Corynebacterium glutamicum. Microbiol Cell Fact.2013; 12: 63-72.
    [7]
    Holmstr?m K, M?ntyl? E, Welin B, Mandal A, et al. Drought tolerance in tobacco. Nature, 1996; 379: 683-84.
    [8]
    Semmler ABT, Whitchurch CB, Mattick JS. A re-examination of twitching motility in Pseudomonas aeruginosa. Microbiol.1999; 145: 2863-73.
    [9]
    Calfee MW, Coleman JP, Pesci EC. Interference with Pseudomonas quinolone signal synthesis inhibits virulence factor expression by Pseudomonas aeruginosa. PNAS, 2001; 98 (20): 11633-37.
    [10]
    Takeuchi S, DiLuzio WR, Weibel DB, Whitesides GM. Controlling the shape of filamentous cells of Escherichia coli. Nano Letters, 2005; 5(9):1819-23.
    [11]
    Kau AL, Martin SM, Lyon W, Hayes E, et al. Enterococcus faecalis tropism for the kidneys in the urinary tract of C57BL/6J mice. Infect Immun.2005; 73(4):2461-68.
    [12]
    Troll W, Lindsley JA. Photometric method for the determination of proline. J Biol Chem. 1954; 215: 655-60.
    [13]
    Sugiura M, Takagi T, Kisumi M. Proline production by regulatory mutants of Serratia marcescens. Appl Microbiol Biotechnol.1985;21: 213-19.
    [14]
    Shibasaki T, Hashimoto S, Mori H, Ozaki A. Construction of a novel hydroxyproline-producing recombinant Escherichia coli by Introducing a proline 4-hydroxylase gene. J Biosci Bioeng. 2000; 90(5): 522-25.
    [15]
    Sugiura M, Suzuki S, Takagi T, Kisumi M. Proline production via the arginine biosynthetic pathway: transfer of regulatory mutations of arginine biosynthesis into a proline-producing strain of Serratia marcescens. Appl Microbiol Biotechnol.1986; 24:153-58.
    [16]
    Csonka LN. Physiological and genetic responses of bacteria to osmotic stress. Microbiol Rev.1989; 53(1):121-147
  • Open Access Research Article
    Export citation: APA   BibTeX   RIS
    Trends Journal of Sciences Research 2015, 2(4), 134-140. http://doi.org/10.31586/Biology.0204.04
    23 Views 189 Downloads PDF Full-text (733.934 KB) PDF Full-text (733.934 KB)  HTML Full-text
    Abstract
    Methionine, a sulfur amino acid, is the first amino acid that is required for many proteins, during synthesis. Our preliminary studies showed that this compound was produced during the late (post-stationary) secondary phase of growth. Therefore, restriction of methionine may be a useful strategy in limiting cancer growth. The bacterial
    [...] Read more.
    Methionine, a sulfur amino acid, is the first amino acid that is required for many proteins, during synthesis. Our preliminary studies showed that this compound was produced during the late (post-stationary) secondary phase of growth. Therefore, restriction of methionine may be a useful strategy in limiting cancer growth. The bacterial strain used in this study was Citrobacter freundii (NRRL B-2643) and their vgb+ recombinant strain. A 1/100 inoculum of overnight cultures grown in LB was made in 50 ml LB in 150 ml Erlenmeyer flasks. Inocula in flasks were grown for 24 h at 30 ?C in a 200 rpm water-bath. For MGL production, 250 ?L of this O/N culture was then inoculated into 150 mL conical flask containing 50 mL of sterile mineral salts medium supplemented with 1 % or 0.1 % (w/v) glucose, respectively. This was incubated for 96 h at 30 ?C, 200 rpm on an orbital shaker. The highest MGL concentration (2,02) was reached by the recombinant strain of Cf[pUC8:15] 72 h after the start of incubation MM+0,1% glucose source. In comparison, the wild type strain produced 3,14 of MGL concentration 72 h was reached MM+0,1% glucose source. The poor media and secondary phase (72 h and up) was used to for MGL production. This is more appropriate. Plasmid is disadvantages in the secondary stage.  Full article
    Figures

    Figure 1 of 5

    References
    [1]
    Cavuoto P, Fenech M.F. (2012). A review of methionine dependency and the role of methionine restriction in cancer growth control and life-span extension. Cancer Treatment Rev. 38, 726-736.
    [2]
    Sato D, Nozaki T. (2009). Methionine Gamma-Lyase: The unique reaction mechanism, physiological roles, and therapeutic applications against infectious diseases and cancers. IUBMB Life. 61(11), 1019-1028.
    [3]
    Kudou D, Misaki S, Yamashita M, Tamura T, Esaki N, Inagaki K. (2008). The role of cysteine 116 in the active site of the antitumor enzyme L-methionine ?-lyase from Pseudomonas putida. Biosci Biotechnol Biochem. 72(7), 1722- 1730.
    [4]
    Morozova E.A., Kulikova V.V., Yashin D.V., Anufrieva N.V., Anisimova N.Y., Revtovich S.V., Kotlov M.I., Belyi Y.F., Pokrovsky V.S., Demidkina T.V. (2013). Kinetic Parameters and cytotoxic activity of recombinant methionine ?-lyase from Clostridium tetani, Clostridium sporogenes, Porphyromonas gingivalis and Citrobacter freundii. Acta Naturae. 5(3), 92-98.
    [5]
    Lua S, Chena G.L., Rena C, Kwabi-Addob B, Epner D.E. (2003). Methionine restriction selectively targets thymidylate synthase in prostate cancer cells. Biochem Pharm. 66, 791-800.
    [6]
    Saa L, Mato J.M., Pavlov V. (2012). Assays for methionine ?- lyase and S-adenosyl-L-homocysteine hydrolase based on enzymatic formation of CdS quantum dots in situ. Anal Chem, 84, 8961-8965.
    [7]
    Revtovich S.V., Morozova E.A., Khurs E.N., Zakomirdina L.N., Nikulin A.D., Demidkina T.V., Khomutov R.M. (2011). Three dimensional structures of noncovalent complexes of Citrobacter freundii methionine ?-lyase with substrates. Biochemistry, 76(5), 564-570.
    [8]
    Benavide M.A., Oelschlager D.K., Zhang H.G., Stockard C.R., Vital-Reyes V.S., Katkoori V.R., Manne U, Wang W, Bland K.I., Grizzle W.E. (2007). Methionine inhibits cellular growth dependent on the p53 status of cells. Am J Surgery. 193, 274- 283.
    [9]
    Li H, Huang Y, Zhang J, Du J, Tan H, Lu Y., Zhou, S. (2011). Identification and characterization of a novel methionine ?-lyase gene from deep-sea sediment metagenomic library. World J Microbiol Biotechnol. 27, 2729-2736.
    [10]
    Morozova E.A., Bazhulina N.P., Anufrieva N.V., Mamaeva D.V., Tkachev Y.V., Streltsov S.A., Timofeev V.P., Faleev N.G., Demidkina T.V. (2010). Kinetic and spectral parameters of interaction of Citrobacter freundii methionine ?-lyase with amino acids. Biochemistry. 7(10), 1272-1280.
    [11]
    Ronda L, Bazhulina N.P., Morozova E.A., Revtovich S.V., Chekhov V.O., Nikulin A.D., Demidkina T.V., Mozzarelli A. (2011). Exploring methionine ?-lyase structure-function relationship via microspectrophotometry and X-ray crystallography. Biochim Biophys Acta. 1814, 834-842.
    [12]
    Surowsky B, Fr?hling A, Gottschalk N, Schl?ter O, Knorr D. (2014). Impact of cold plasma on Citrobacter freundii in apple juice: Inactivation kinetics and mechanisms. Int J Food Microbiol. 174, 63-71.
    [13]
    Wanga Z, Xiao Y, Chen W, Tang K, Zhang L. (2009). Functional expression of Vitreoscilla hemoglobin (VHb) in Arabidopsis relieves submergence, nitrosative, photo-oxidative stress and enhances antioxidants metabolism. Plant Science. 176, 66-77.
    [14]
    Soda K. (1968). Microdetermination of D-amino acids and D- amino acid oxidase activity with 3-methyl-2-benzothiazolone hydrazone hydrochloride. Anal Biochem. 25, 228-235.
    [15]
    Tanaka H, Imahara H, Esaki N, Soda K. (1980). Selective determination of L-methionine and L-cysteine with bacterial L-methionine ?-lyase and anti-tumor activity of the enzyme. J Appl Biochem. 2, 439-444.
    [16]
    Kahraman H, Erenler S.O. (2012). Rhamnolipid production by Pseudomonas aeruginosa engineered with the Vitreoscilla hemoglobin gene. Appl Biochem Microbiol. 48(2), 188-193.
    [17]
    Pavillard V, Nicolaou A, Double J.A., Phillips R.M. (2006). Methionine dependence of tumours: A biochemical strategy for optimizing paclitaxel chemosensitivity in vitro. Biochem Pharma. 71, 772-778.
  • Open Access Research Article
    Export citation: APA   BibTeX   RIS
    Trends Journal of Sciences Research 2019, 4(1), 14-20. http://doi.org/10.31586/Microbiology.0401.03
    65 Views 181 Downloads PDF Full-text (661.719 KB) PDF Full-text (669.784 KB) PDF Full-text (669.784 KB)  HTML Full-text
    Abstract
    Motility plays an important role in biofilm formation and movement in different environmental conditions, colonization, and adhesion of bacteria to surfaces. The lowest swimming was 3 (mm) in agar medium and the highest value was 42.67 (mm) with the addition of WCW. The lowest swarming was carried out in agar
    [...] Read more.
    Motility plays an important role in biofilm formation and movement in different environmental conditions, colonization, and adhesion of bacteria to surfaces. The lowest swimming was 3 (mm) in agar medium and the highest value was 42.67 (mm) with the addition of WCW. The lowest swarming was carried out in agar medium with 7.66 (mm), while the highest value was found in N.A medium with the addition of 10% WCW 59.33 (mm). In all experimental conditions, an increase of 2.4 times (swimming) and 6.4 times (swarming) was observed after the addition of WCW to the controls.  Full article
    Figures

    Figure 1 of 4

    References
    [1]
    Mannik J, Driessen R, Galajda P, Keymer JE, Dekker C. Bacterial growth and motility in sub-micron constrictions. Pnas 2009; 106 (35): 14861–14866.
    [2]
    Semmler A B T, Whitchurch CB, Mattick J.S. A re-examination of twitching motility in Pseudomonas aeruginosa. Microb. 1999; 145: 2863–2873.
    [3]
    Deziel E, Comeau Y, Villemur R. Initiation of Biofilm Formation by Pseudomonas aeruginosa 57RP Correlates with Emergence of Hyperpiliated and Highly Adherent Phenotypic Variants Deficient in Swimming, Swarming and Twitching. J Bacteriol. 2001; 183(4): 1195-1204.
    [4]
    Tremblay J, Richardson AP, Lépine F, Déziel E. Self-produced extracellular stimuli modulate the Pseudomonas aeruginosa swarming motility behavior. Environ Microb. 2007; 9(10): 2622–2630.
    [5]
    Overhage J, Bains M, Brazas M D, Hancock R.E.W. Swarming of Pseudomonas aeruginosa is a Complex Adaptation Leading to Increased Production of Virulence Factors and Antibiotic Resistance. J Bacteriol. 2008; 190(8): 2671–2679.
    [6]
    Tremblay J, Déziel E. Improving the reproducibility of Pseudomonas aeruginosa swarming motility assays. J Basic Microb. 2008; 48: 509–515.
    [7]
    Copeland MF, Weibel D.B. Bacterial Swarming A Model System for Studying Dynamic Selfassembly. NIH Public Access. 2009; 5(6): 1174–1187.
    [8]
    Morris J D, Hewitt JL, Wolfe LG, Kamatkar NG, Chapman SM, Diener JM, Courtney AJ, Matthew Leevy W, Shrout J.D. Imaging and Analysis of Pseudomonas aeruginosa Swarming and Rhamnolipid Production. Appl Environ Microb. 2011; 77(23): 8310–8317.
    [9]
    Wolska K, Szweda P, Lada K, Rytel E, Gucwa K, Kot B, Piechota M. Motility activity, slime production, biofilm formation and genetic typing by ERIC-PCR for Pseudomonas aeruginosa strains isolated from bovine and other sources (human and environment). Pol J Vet Sci. 2014; 17(2): 321–329.
    [10]
    Yeung A T Y, Torfs E C W, Jamshidi F, Bains M, Wiegand I, Hancock R E W, Overhage J. Swarming of Pseudomonas aeruginosa Is Controlled by a Broad Spectrum of Transcriptional Regulators, Including MetR. J Bacteriol. 2009; 191(18): 5592–5602.
    [11]
    Swiecicki JM, Sliusarenko O, Weibel D.B. From swimming to swarming Escherichia coli cell motility in two-dimensions. NIH Public Access. 2013; 5(12):1490–1494.
    [12]
    Goh S.N. Effects of Different Amino Acids on Biofilm Growth, Swimming Motility and Twitching Motility in Escherichia coli BL21. J Biol Life Sci. 2013; 4(2): 104-115.
    [13]
    Inoue T, Shingaki R, Fukui K. Inhibition of swarming motility of Pseudomonas aeruginosa by branched-chain fatty acids. FEMS Microbiol Lett. 2008; 281: 81-86.
    [14]
    Morris J D, Hewitt JL, Wolfe LG, Kamatkar NG, Chapman SM, Diener JM, Courtney AJ, Matthew Leevy W, Shrout J.D. Imaging and Analysis of Pseudomonas aeruginosa Swarming and Rhamnolipid Production. Appl Environ Microb. 2011; 77(23): 8310–8317.
    [15]
    Yang A, Tang WS, Si T, Tang J.X. Influence of Physical Effects on the Swarming Motility of Pseudomonas aeruginosa. Biophys J. 2017; 112:1462–1471.
    [16]
    Overhage J, Lewenza S, Marr A K, Hancock R.E.W. Identification of Genes Involved in Swarming Motility Using a Pseudomonas aeruginosa PAO1 Mini-Tn5-lux Mutant Library. Am Soc for Microb. 2007; 189 (5): 2164–2169.
    [17]
    O’May C, Tufenkji N. The Swarming Motility of Pseudomonas aeruginosa is Blocked by Cranberry Proanthocyanidins and Other Tannin-Containing Materials. Appl Environ Microb. 2011; 77(9): 3061–3067.
    [18]
    Murray TS, Kazmierczak B.I. Pseudomonas aeruginosa Exhibits Sliding Motility in the Absence of Type IV Pili and Flagella. J Bacteriol. 2008; 190(8): 2700–2708.
    [19]
    Kohler T, Curty L K, Barja F, Delden CV, Pechere J.C. Swarming of Pseudomonas aeruginosa Is Dependent on Cell-to-Cell Signaling and Requires Flagella and Pili. J Bacteriol. 2000; 182(21): 5990–5996
    [20]
    Vicario JC, Dardanelli MS, Giordano W. Swimming and swarming motility properties of peanut-nodulating rhizobia. FEMS Microbiol Lett. 2015; 362: 1-6.
    [21]
    Samad T, Billings N, Birjiniuk A, Crouzier T, Doyle PS, Ribbeck K. Swimming bacteria promote dispersal of non-motile Staphylococcal species. The ISME J. 2017; 1-5.
    [22]
    Lovewell RR, Hayes SM, O’Toole GA, Berwin B. Pseudomonas aeruginosa flagellar motility activates the phagocyte PI3K/Akt pathway to induce phagocytic engulfment. Am J Physiol Lung Cell Mol Physiol. 2014; 306: 698-707.
    [23]
    Murray TS, Kazmierczak B.I. FlhF Is Required for Swimming and Swarming in Pseudomonas aeruginosa. J Bacteriol. 2006; 188(19): 6995–7004.
    [24]
    Lauga E, DiLuzio W R, Whitesides G M, Stone H.A. Swimming in Circles: Motion of Bacteria near Solid Boundaries. Biophys J. 2006; 90: 400-412.
    [25]
    Mittal N, Budrene E O, Brenner M P, Oudenaarden A.V. Motility of Escherichia coli cells in clusters formed by chemotactic aggregation. PNAS 2003; 100(23): 13259–13263.
    [26]
    Ng W. Retarded swarming motility in Bacillus subtilis NRS-762 and Pseudomonas aeruginosa PRD-10. Peer J Preprints. 2018; 1-10.
    [27]
    Granum PE, Lund T. Bacillus cereus and its food poisoning toxins. FEMS Microbiol Lett. 1997; 157: 223-228.
    [28]
    Callegan MC, Novosad BD, Ramirez R, Ghelardi E, Senesi S. Role of Swarming Migration in the Pathogenesis of Bacillus Endophthalmitis. IOVS 2006; 47(10): 4461- 4467.
    [29]
    Habib F, Rind R, Durani N, Bhutto A L, Buriro R S, Tunio A, Aijaz N, Lakho SA, Bugti AG, Shoaib M. Morphological and Cultural Characterization of Staphylococcus aureus Isolated from Different Animal Species. J Appl Environ Biol Sci. 2015; 5(2): 15-26.
    [30]
    Pollitt EJG, Crusz SA, Diggle S.P. Staphylococcus aureus forms spreading dendrites that have characteristics of active motility. Sci Rep. 2015; 1-12.
    [31]
    Kim HS, Hahn H, Kim J, Jang DM, Lee JY, Back JM, Im HN, Kim H, Han BW, Suh S.W. Structural basis for the substrate recognition of peptidoglycan pentapeptides by Enterococcus faecalis VanYB . Int J Biol Macromol. 2018; 119: 335–344.
    [32]
    Todokoro D, Eguchi H, Suzuki T, Suzuki M, Imaohji HN, Kuwahara T, Nomura T, Tomita H, Akiyama H. Genetic diversity and persistent colonization of Enterococcus faecalis on ocular surfaces. Jpn J Ophthalmol. 2018; 62: 699–705.
    [33]
    Fuente-Núñez C, Korolik V, Bains M, Nguyen U, Breidenstein EBM, Horsman S, Lewenza S, Burrows L, Hancock R.E.W. Inhibition of Bacterial Biofilm Formation and Swarming Motility by a Small Synthetic Cationic Peptide. Antimicrob Agents Ch. 2012; 56(5): 2696–2704.
Filter options
Publication Date
From to
Refine Publication Date
Subject Areas
Refine Subjects
Article Types
Refine Article Types
Countries / Territories
Refine Countries / Territories