Journal of Microbiology

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The Role of Wheat Germ Agglutinin in the Attachment of Pseudomonas sp. WS32 to Wheat Root: Jian Zhang , Liyuan Meng , Yuanyuan Cao , Huiping Chang , Zhongyou Ma , Leni Sun , Ming Zhang , Xinyun Tang; J. Microbiol. 2014;52(12):1020-1024. Published online November 29, 2014; DOI: https://doi.org/10.1007/s12275-014-4089-x

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Wheat germ agglutinin (WGA), which is secreted on the surface of wheat root, has been defined as a protein that reversibly and non-enzymatically binds to specific carbohydrates. However, little attention has been paid to the function of WGA in the attachment of bacteria to their host plants. The aim of this study was to investigate the role of WGA in the attachment of Pseudomonas sp. WS32 to wheat roots. Wheat roots were initially treated with double-distilled water, WGA-H (WGA solution that was heated at 100°C for 15 min) and WGA, independently. Subsequently, the roots were coincubated with cell solutions (109 cells/ml). A dilution plate
method
using a solid nutrient medium was employed to determine the adsorption of WS32 to wheat roots. WGA was labeled with fluorescein isothiocyanate and detected using the fluorescent in situ hybridization (FISH) technique. The number of adsorptive WS32 cells on wheat roots was significantly increased when the wheat roots were pretreated with WGA, compared with the control treatment (p = 0.01). However, WGA-H failed to increase the amount of bacterial cells that attached to the wheat roots because of the loss of its physiological activity. The FISH assay also revealed that more cells adhered to WGA-treated wheat roots than to control or WGA-H-treated roots. The results indicated that WGA can mediate Pseudomonas strain WS32’s adherence to wheat seedling roots. The findings of this study provide a better understanding of the processes involved in plant-microbe interactions.

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Isolation and purification of wheat germ agglutinin and analysis of its properties
Han Wang
IOP Conference Series: Earth and Environmental Science.2017; 100: 012021. CrossRef

Isolation and Characterization of Biogenic Amine-Producing Bacteria in Fermented Soybean Pastes: Jin Seok Moon , Seung Kee Cho , Hwa Young Choi , Ji Eun Kim , So-Young Kim , Kyung-Ju Cho , Nam Soo Han; J. Microbiol. 2010;48(2):257-261. Published online May 1, 2010; DOI: https://doi.org/10.1007/s12275-010-0040-y

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Abstract: Biogenic amines (BAs) are produced primarily by microorganisms found in fermented foods and are often implicated in food poisoning. BA-producing bacteria found in fermented soybean pastes were isolated and characterized using a decarboxylating medium and multiplex PCR analysis. Two BA-producing bacteria were isolated from traditional soybean pastes: one was a histamine-producing Clostridium strain, and the other was a tyramine-producing Pseudomonas strain. The Clostridium strain was determined to be a potent histamine producer among the cultures tested. Synthesis of tyramine by Pseudomonas sp. T1 was observed for the first time in this study.

Note] Comparative Analysis of 2,4,6-Trinitrotoluene (TNT)-Induced Cellular Responses and Proteomes in Pseudomonas sp. HK-6 in Two Types of Media: Yun-Seok Cho , Bheong-Uk Lee , Hyung-Yeel Kahng , Kye-Heon Oh; J. Microbiol. 2009;47(2):220-224. Published online May 2, 2009; DOI: https://doi.org/10.1007/s12275-008-0108-0

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Abstract: TNT-induced cellular responses and proteomes in Pseudomonas sp. HK-6 were comparatively analyzed in two different media: basal salts (BS) and Luria broth (LB). HK-6 cells could not degrade more than 0.5 mM TNT with BS medium, while in LB medium, they exhibited the enhanced capability to degrade as much as 3.0 mM TNT. Analysis of total cellular fatty acids in HK-6 cells suggested that the relative abundance of several saturated or unsaturated fatty acids is altered under TNT-mediated stress conditions. Scanning electron microscopy showed the presence of perforations, irregular rod formations, and wrinkled extracellular surfaces in cells under TNT stress. Proteomic analysis of soluble protein fractions from HK-6 cultures grown with TNT as a substrate revealed 11 protein spots induced by TNT. Among these, seven proteins (including Alg8, AlgB, NirB, and the AhpC/Tsa family) were detected only in LB medium containing TNT. The proteins AspS, Tsf, and assimilatory nitrate reductase were increasingly expressed only in BS medium containing TNT. The protein dGTPase was found to be induced and expressed when cells were grown in either type of TNT-containing media. These results provide a better understanding of the cytotoxicity and survival mechanism used by Pseudomonas sp. HK-6 when placed under TNT stress conditions.

Journal Articles

S5 Lipase : An Organic Solvent Tolerant Enzyme: Raja Noor Zaliha Raja Abdul Rahman , Syarul Nataqain Baharum , Abu Bakar Salleh , Mahiran Basri; J. Microbiol. 2006;44(6):583-590.; DOI: https://doi.org/2470 [pii]

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Abstract: In this study, an organic solvent tolerant bacterial strain was isolated. This strain was identified as Pseudomonas sp. strain S5, and was shown to degrade BTEX (Benzene, Toluene, Ethyl-Benzene, and Xylene). Strain S5 generates an organic solvent-tolerant lipase in the late logarithmic phase of growth. Maximum lipase production was exhibited when peptone was utilized as the sole nitrogen source. Addition of any of the selected carbon sources to the medium resulted in a significant reduction of enzyme production. Lower lipase generation was noted when an inorganic nitrogen source was used as the sole nitrogen source. This bacterium hydrolyzed all tested triglycerides and the highest levels of production were observed when olive oil was used as a natural triglyceride. Basal medium containing Tween 60 enhanced lipase production to the most significant degree. The absence of magnesium ions (Mg2+) in the basal medium was also shown to stimulate lipase production. Meanwhile, an alkaline earth metal ion, Na+, was found to stimulate the production of S5 lipase.

Stabilities of Artificially Transconjugated Plasmids for the Bioremediation of Cocontaminated Sites: Kyung Pyo Yoon; J. Microbiol. 2005;43(2):196-203.; DOI: https://doi.org/2161 [pii]

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Abstract: Here, we attempted to evaluate the activity of artificially transconjugated multiple plasmids in “designer biocatalysts” for the bioremediation of cocontaminated sites under nonselective conditions. We observed profound losses in the percent survivals of artificially transconjugated plasmid activity (66 - 78% loss immediately after freeze-drying, 99.45 - 99.88% loss by the end of 6 months storage) in reconstituted Pseudomonas sp. KM12TC. Such unpredictable high losses of this particular plasmid appeared to clearly be a deleterious effect. However, even after 6 months of storage, the cells remained able to degrade 95% of phenol within 9 days, and the full efflux of ^73As, as compared to that of the non-freeze-dried cells, was successfully achieved 4 to 9 days later. These results indicate that “stable designer biocatalysts” can remain viable, even after freeze-drying and 6 months of storage.

Characterization of Protocatechuate 4,5-Dioxygenase Induced from p-Hydroxybenzoate-Cultured Pseudomonas sp. K82: Sung-Ho Yun , Chi-Young Yun , Seung Il Kim; J. Microbiol. 2004;42(2):152-155.; DOI: https://doi.org/2029 [pii]

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Abstract: Pseudomonas sp. K82 has been reported to be an aniline-assimilating soil bacterium. However, this strain can use not only aniline as a sole carbon and energy source, but can also utilize benzoate, phydroxybenzoate, and aniline analogues. The strain accomplishes this metabolic diversity by using different aerobic pathways. Pseudomonas sp. K82, when cultured in p-hydroxybenzoate, showed extradiol cleavage activity of protocatechuate. In accordance with those findings, our study attempted the purification of protocatechuate 4,5-dioxygenase (PCD 4,5). However the purified PCD 4,5 was found to be very unstable during purification. After Q-sepharose chromatography was performed, the crude enzyme activity was augmented by a factor of approximately 4.7. From the Q-sepharose fraction which exhibited PCD 4,5 activity, two subunits of PCD4,5 ([alpha]subunit and [beta] subunit) were identified using the N-terminal amino acid sequences of 15 amino acid residues. These subunits were found to have more than 90% sequence homology with PmdA and PmdB of Comamonas testosteroni. The molecular weight of the native enzyme was estimated to be approximately 54 kDa, suggesting that PCD4,5 exists as a heterodimer ([alpha]_1[beta]_1). PCD 4,5 exhibits stringent substrate specificity for protocatechuate and its optimal activity occurs at pH 9 and 15^oC. PCR amplification of these two subunits of PCD4,5 revealed that the [alpha] subunit and [beta] subunit occurred in tandem. Our results suggest that Pseudomonas sp. K82 induced PCD 4,5 for the purpose of p-hydroxybenzoate degradation.

cloning of Gene Encoding for Siderophore biosynthesis in Fluorescent Pseudomonas sp.: Koh, Han Cheol , Ha, Sung Cheol , Na, Jung A , Kim, Ho Sang , Yeo, Myeong Gu , Lee, Jung Sup , Kim, Sung Jun , Park, yeal; J. Microbiol. 1995;33(1):28-33.

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Abstract: Pseudomonas sp. strain PY002, isolated from soil, was mutagenized with a transposon Tn5(21). To screening of siderophore biosunthesis defective mutant, 138 kanamycin resistant mutants were tested of growth on MKB medium supplemented with iron chelator(bipydidyl and EDDHA) and in vitro antibiosis. Among 138 mutants, 32 mutants do not excreted a siderophore and lose their antibiotic activity. So, these mutants were designated Flu^-Sid^-. A gene bank of DNA from Pseudomonas sp. strain PY002 was constructed using the broad-host range conjugative cosmid pLAFR3. The recombinant cosmids contained insert DNA averaging 21 kb in length and the frequence of transduction into E. coli HB101 per 1㎍ of insert DNA was 9 × 10³. Nonfluorescent mutants were complemented by mating the gene bank en masse and identifying the 108 fluorescent transconjugants. Restriction enzyme analysis of these complemented transconjugants revealed three different types and they were named pCOM61, pCOM91 and pCOM97. Sizes of their insert DNA were 30kb, 26kb and 28kb, respectively.

Cloning of the Gene Responsible for Dechlorination of 4-Chlorobenzoate from Pseudomonas sp. DJ-12: Chae, Jong Chan , Kim, Young Chang , Kim, Young Soo , Kim, Chi Kyung; J. Microbiol. 1995;33(1):34-39.

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Abstract: The gene responsible for dechlorination of 4-chlorobenzoate(4CBA) was cloned from chromosomal DNA of Pseudomonas sp. DJ-12 in Escherichia coli XL1-Blue by using pBluescript SK(+) phagemid vector. Two recombinant plasmids of pCJ1 and pCJ2 carrying dechlorinase gene were constructed. The inserted DNAs in the pCJ1 and pCJ2 were found to have the fragment of 9.5 kb carrying dechlorinase gene, but they were oriented in opposite direction. The inserted DNA of 3.4kb in the pCJ101 subclone carrying dechlorinase gene had two restriction sites for AccI and each one site for HincII, KpnI, PstI, and SacIi but the dechlorinase gene in pCJ101 was found to be placed over the HincII site. The dechlorinase fenes in the recombinant cells of E. coli CJ1 and CJ101 were well expressed to show the dechlorination activity of 4CBA. The proteins encoded by dechlorinase genes in E. coli CJ1 and CJ101 were about 49 kDa in molecular weight. But this protein was not produced by E. coli CJ102, CJ103 and E. coli XL1-Blue. Therefore, the proteins produced by Pseudomonas sp. DJ-12 and the cloned cells of E. coli CJ1 and CJ101 were thought to be the dechlorinase enzyme which was the product of dechlorinase gene.

Improvement of 4-chlorobiphenyl degradation bya recombinant strain, pseudomonas sp. DJ12-C: Kim, Ji Young , Kim, Young Chang , Lim, Jai Yun , Lee, Ki Sung , Ka, Jong Ok , Min, Kyung Hee , Kim, Chi Kyung; J. Microbiol. 1997;35(1):53-60.

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Abstract: Pseudomonas sp. P20 and Pseudomonas sp. DJ-12 isolated from the polluted environment are capable of degrading biphenyl and 4-chlorobiphenyl (4CB) to produce benzoic acid and 4-chlorobenzoic acid (4CBA) respectively, by pcbABCD-encoded enzymes. 4CBA can be further degraded by Pseudomonas sp. DJ-12, but not by Pseudomonas sp P20. However, the meta-cleavage activities of 2,3-dihydroxybiphenyl (2, 3-DHBP) and 4-chloro-2,3-DHBP dioxygenases (2, 3-DHBD) encoded by pcbC in Pseudomonas sp. P20 were stronger than Pseudomonas sp. DJ-12. In this study, the pcbC gene encoding 2, 3-DHBD was cloned from the genomic DNA of Pseudomonas sp. P20 by using pKT230. A hybrid plasmid pKK1 was constructed and E. coli KK1 transformant was selected by transforming the pKK1 hybrid plasmid carrying pcbC into E. coli XL1-Blue. By transferring the pKK1 plasmide of E. coli KK1 into Pseudomonas sp. DJ-12 by conjugation, a recombinant strain Pseudomonas sp. P20, Pseudomonas sp. DJ-12, and the recombinant cell assay methods. Pseudomonas sp. DJ12-C readily degraded 4CB and 2, 3-DHBP to produce 2-hydroxy-6-oxo-6-phenylhexa-2, 4-dienoic acid (HOPDA), and the resulting 4CBA and benzoic acid were continuously catabolized. Pseudomonas sp. DJ12-C degraded 1 mM 4CB completely after incubation for 20 h, but Pseudomonas sp. P20 and Pseudomonas sp. DJ-12 showed only 90% and Pseudomonas sp. DJ-12 had, but its degradation activity to 2, 3-DHBP, 3-methylcatechol, and catechol was improved.

Isolation of pseudomonas sp. S-47 and its degradation of 4-chlorobenzoic acid: Seo, Dong In , Lim, Jai Yun , Kim, Young Chang , Min, Kyung Hee , Kim, Chi Kyung; J. Microbiol. 1997;35(3):188-192.

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Abstract: The strain of S-47 degrading 4-chlorobenzoic acid (4CBA) was isolated from Ulsan chemical industrial complex by enrichment cultivation with 1 mM 4CBA. The strain was Gram-negative rod and grew optimally at 30℃ and pH 7 under aerobic condition, so that the organism was identified as a species of Pseudomonas. Pseudomonas sp. S-47 degraded 4-chlorobenzoic acid to produce a yellow-colored meta-cleavage product, which was confirmed to be 5-chloro-2-hydroxymuconic semialdehyde (5C-2HMS) by UV-visible spectrophotometry. 5C-3HMS was proved trometry. This means that Pseudomonas sp. S-47 degraded 4CBA via 4-chlorocatechol to 5C-2HMS by meta-cleavage reaction and then to 5C-2HMA by 5C-2HMS dehydrogenase.

Dechlorination of 4-Chlorobenzoate by Pseudomonas sp. DJ-12: Chae, Jong Chan , Kim, Chi Kyung; J. Microbiol. 1997;35(4):290-294.

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Abstract: 4-Chlorobiphenyl-degrading Pseudomonas sp. DJ-12 was able to degrade 4-chlorobenzoate(4CBA), 4-iodobenzoate, and 4-bromobenzoate completely under aerobic conditions. During. the degradation of 4CBA by Pseudomonas sp. DJ-12, chloride ions were released by dechlorination and 4-hydroxybenzoate was produced as an intermediate metabolite. The NotI-KNA fragments of pKC157 containing dechlorination genes hybridized with the gene encoding 4CBA:CoA dehalogenase of Pseudomonas sp. CBS3 which is responsible for the hydrolytic dechlorination of 4CBA. These results imply that Pseudomonas sp. DJ-12 degrades 4CBA to 40hydroxybenzoate via dechlorination as the initial step of its degradativ pathway. The genes responsible for dechlorination of 4CBA were found to be blcated on the chromosomal DNA of Pseudomonas sp. DJ-12.

Characteristics of Catechol 2,3-dioxygenase Produced by 4-Chlorobenzoate-degrading Pseudomonas sp. S-47: Kim, Ki Pil , Seo, Dong In , Min, Kyung Hee , Ka, Jong Ok , Park, Yong Keun , Kim, Chi Kyung; J. Microbiol. 1997;35(4):295-299.

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Abstract: Pseudomonas sp. S-47 is capable of transforming 4-chlorobenzoate to 4-chlorocatechol which is subsequently oxidized bty meta-cleavage dioxygenase to prodyce 5-chloro-2-hydroxymuconic semialdehyde. Catechol 2,3-dioxygenase (C23O) produced by Pseudomonas sp. S-47 was purified and characterized in this study. The C23O enzyme was maximally produced in the late logarithmic growth phase, and the temperature and pH for maximunm enzyme activity were 30~35℃ and 7.0, respectively. The enzyme was purified and concentrated 5 fold from the crude cell extracts through Q Sepharose chromatography and Sephadex G-100 gel filtration after acetone precipitation. The enzyme was identified as consisting of 35 kDa subunits when analyzed by SDS-PAGE. The C23O produced by Pseudomonas sp. S-47 was similar to Xy1E of Pseudomonas putida with respect to substrate specificity for several catecholic compounds.

Production of Stress-shock Proteins in Pseudomonas sp. DJ-12 Treated with 4-Hydroxybenzoate: Park, Sang Ho , Oh, Kye Heon , Lee, Kil Jae , Kim, Chi Kyung; J. Microbiol. 1998;36(4):273-279.

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Abstract: Pseudomonas sp. DJ-12 can grow on 4-hydroxybenzoate (4HBA) at concentration of 5 mM or lower by degrading 4HBA for carbon and energy sources. The organisms were found to produce DnaK stress-shock protein when treated with several aromatic hydrocarbons including 4HBA. Those cells treated with 5 mM 4HBA exhibited increased tolerance to 10 mM concentration. In this study, the production of other stress-shock kproteins besides KnaK was examined in Pseudomonas sp. DJ-12 exposed to various concentrations of 4HBA, compraing the production of the proteins with their survival and degradation of 4HBA. The organisms could degrade 4HBA at 0.5 to 5 mM concentrations after 60 to 90 minutes of incubation. The survival rate of the organism decreased when treated with 4HBA at 10 mM or higher concentrations. The stress-shock proteins of DnaK, GroEL, and GroES were produced in the cells which were treated with 4HBA at 0.5 mM or higher concentrations for 10 minutes. Fifteen additional stress-shock proteins were produced in the cells which were treated with 5 mM 4HBA for 40 minutes. The DnaK and GroEL proteins in the cells gradually decreased upto 6 hours after the stress was removed from the culture.

Cellular Response of Pseudomonas sp. DJ-12 to the Stresses of Several Aromatic Pollutants: Park, Sang Ho , Ko, Yeon Ja , Oh, Kye Heon , Kim, Chi Kyung; J. Microbiol. 1998;36(2):93-98.

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Abstract: Pseudomonas sp. DJ-12 is capable of degrading biphenyl, 4-chlorobiphenyl (4CB), and 4-hydroxybenzoate (4HBA) at relatively low concentrations. The degradability and cellular responses of the organism to the aromatic pollutants at higher concentrations have not been studied. In this study, the survival of the cells, production of stress proteins, and induction of tolerance were examined by exposing cells to various concentrations of the aromatics. The survival rates of the organism were reversely proportional to the concentration of each aromatic during incubation for 6 hs. Stress protein specifically reacting with anti-DnaK monoclonal antibody was commonly produced when cells were treated with each aromatic. Those cells pretreated with each aromatic at lower concentrations exhibited a certain degree of tolerance to higher concentrations of the aromatics. Such cellular responses of the organism to water-soluble 4HBA were more clearly distinguished than those to insoluble 3CB and biphenyl. Therefor, induction of DnaK stress protein in the cells by exposure to the aromatiocs could be used to develop an indicator for pollution by the aromatics.

Cloning and Expression in E. coli of the Genes Responsible for Degradation of 4-Chlorobenzoate and 4-Chlorocatechol drom Pseudomonas sp. Strain S-47: Kim, Ki Pil , Seo, Dong In , Lee, Dong Hun , Kim, Young Soo , Kim, Chi Kyung; J. Microbiol. 1998;36(2):99-105.

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Abstract: Pseudomonas sp. strain S-47 can grow on 4-chlorobenzoate (4CBA) and transform 4CBA to 4-chlorocatechol (4CC) under aerobic conditions, which is subsequently degraded to produce 2-hydroxypent-2, 4-dienoate (2H-2,4DA). The upper steps for conversion of 4CBA to 4CC are recognized to be conducted by the benzoate-1,2-dioxygenase (B12O) system encoded by benABC and benD. The ensving meta-cleabage reaction of 4CC is catalyzed by catechol 2,3-dioxygenase(C23O) encoded by the xylE gene. The benABCD and the xylE genes were cloned from the chromosome of Pseudomonas sP. S-47 into pCS1(48.7kb), pCS101(24.4kb), pCS201(17.7kb), and pCS202(6.7kb) recombinant plasmids, and were well ecpressed in E. coli XL1-Blue host cells. The PstI-insert (4.0kb) of pC202 was found to contain the benABCD and cylE genes and to have 2 EcoRV, 1 SphI, and 3 SacII restriction sites.

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