• Title/Summary/Keyword: Bacterial Enzyme

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Seroprevalence of Q-fever in Korean native cattle (국내 서식 한우에서 큐열 항체 양성율 조사)

  • Kim, Ji-Yeon;Sung, So-Ra;Pyun, Ji-In;Her, Moon;Kang, Sung-Il;Lee, Hyang-Keun;Jung, Suk Chan
    • Korean Journal of Veterinary Research
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    • v.54 no.3
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    • pp.147-150
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    • 2014
  • Q-fever is a vector-borne (Coxiella [C.] burnetii) zoonotic disease that is an increasing public health concern. To date, some research about Q-fever prevalence in dairy herds and human patients has been reported in Korea, but information about Korean native cattle is scarce. To measure the prevalence rates of C. burnetii in Korean native cattle, a total of 1,095 bovine serum samples collected during 2010~2013 were analyzed with an enzyme-linked immunosorbent assay. Sixty-eight heads of cattle were diagnosed as positive and while 19 heads were suspected (positive rate = 6.2%). Interestingly, Jeju province had a seropositivity rate six times greater than that of other provinces (18.9% vs. 3.2%). High seroprevalence might be caused by wide distribution of ticks in Jeju province compared to other regions. Based on these data, extensive monitoring of C. burnetii infection in cattle, tick distribution, and climate changes is required.

Studies on the scouring of raw silk by the application of bacterial enzyme of sericinase -(Part 1.) Isolation and selection of proper bacteria and some studies of properties of this bacterial enzyme- (세균성(細菌性) Sericin 분해(分解) 효소(酵素)에 의(依)한 생사정련(生絲精練)에 관(關)한 연구(硏究) -(제1보(第1報)) 유용세균(有用細菌)의 분리(分離) 세정(選定) 및 생성(生成) Sericinase 의 효소학적(酵素學的) 성질(性質)에 대(對)하여-)

  • Ki, Woo-Kyung;Seu, Jung-Hwn
    • Applied Biological Chemistry
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    • v.12
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    • pp.75-81
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    • 1969
  • In order to obtain a method of scouring of raw silk and degumming of cocoon by the appling of bacterial enzyme of sericinase, a strain of proper bacteria was isolated and some properties of the enzyme produced by the isolated bacteria were studied and the following results were obtained. 1) Optimum pH and temperature were indicating 7.5 and $50^{\circ}C$. and on these conditions, the silk fibroin will get no modification at all. 2) Sericinase activity was inhibited by calcium ion in the free incubation but same ions reacted as an activator in the reaction with substrate. So, degumming of Tussah cocoon which contains calcium oxalate in the cocoon layer will be possible by the treatment of this enzyme. 3) This bacterial sericinase never gives any affection to the fibroin layer of the silk. 4) The factors of smooth-surface condition, damage of fibroin layer, touching, luster and degumming effect of the silk resulting by the enzyme treatment were more appropriate than the results of other scouring methods, saponin, alkali and saponin-alkali using methods. We expect to get the same scouring result that compared with the papain or pancreatin were applied.

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Enzyme Profiles of Alga-Lytic Bacterial Strain AK-13 Related with Elimination of Cyanobacterium Anabaena cylindrica

  • Kim, Jeong-Dong;Han, Myung-Soo
    • Korean Journal of Environmental Biology
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    • v.22 no.1
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    • pp.184-191
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    • 2004
  • To investigate bacteria with algalytic activities against Anabaena cylindrica when water blooming occurs and to study enzyme profiles associated with alga-lytic activity, various bacterial strains were isolated from surface waters and sediments in eutrophic lakes or reservoirs in Korea. Among 178 isolates, only nine isolates exhibited lytic abilities against A cylindrica on the agar plates, and then the isolate AK-13 was selected as the strongest in lysing the cyanobacterium A. cytindrica. The strain AK-13 was characterized and identified as Sinorhizobium sp. based on fatty acid methyl ether profiles and 16S rDNA sequence. According to the results of the enzyme assays, in the strain An-13 of Sinorhizobium sp., alginase, amylase, proteinase (caseinase and gelatinase), carboxymethyl-cellulase (CMCase), laminarinase, and lipase was produced, namely CMCase, laminarinase and protease were highly active. None of glycosidase was produced. Therefore, enzyme systems of Sinorhizobium sp. AK-13 were very complex to degrade cell walls of A. cylindrica. The peptidoglycans of A. cylindrica mat be hydrolyzed and metabolized to a range of easily utilizable monosaccharides or other low molecular weight organic substances by Sinorhizobium sp. AK-13.

Purification and Characterization of the Bacillus sp. KK-l $\beta$-Xylosidase from a Recombinant Escherichia coli

  • Jung, Kyung-Hwa;Chun, Yong-Chin;Lee, Jae-Chan;Park, Seung-Hwan;Yoon, Ki-Hong
    • Journal of Microbiology and Biotechnology
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    • v.8 no.3
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    • pp.258-263
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    • 1998
  • ${\beta}$-Xylosidase was purified from the recombinant Escherichia coli carrying the Bacillus sp. KK-1 ${\beta}$-xylosidase gene (xylB). The molecular mass of the purified enzyme was estimated to be 62 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. However, the apparent molecular mass of the ${\beta}$-xylosidase was 140 kDa, indicating that the native ${\beta}$-xylosidase has an oligomeric structure composed of two identical subunits. The isoelectric point was determined to be pH 5.5. The enzyme was highly active on p-nitrophenyl-$\beta$-D-xylopyranoside but it barely hydrolyzed xylan substrates, and did not exhibit activity towards carboxymethylcellulose and p-nitrophenyl-${\beta}$-D- glucopyranoside. The enzyme had a pH optimum for its activity at pH 6.5 and a temperature optimum at $40^{\circ}C$. The enzyme activity was completely inhibited by the presence of $Hg^{++}$, and also markedly inhibited by D-xylose and D-glucose.

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Screening of Antimicrobial Activity and Proteolytic Enzyme Stability of Extract of the Blue Mussel Mytilus edulis (진주담치(Mytilus edulis) 추출물의 항균활성 및 단백질 분해효소에 대한 안정성 탐색)

  • Lee, Ji-Eun;Seo, Jung-Kil
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.54 no.3
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    • pp.280-286
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    • 2021
  • This study was performed to screen the antimicrobial activities and proteolytic enzyme stability of the acidified extract of the Blue mussel Mytilus edulis. The acidified extract showed potent antimicrobial activities against Gram-positive bacteria, Bacillus subtilis, and Gram-negative bacteria, Escherichia coli D31, but had no activity against Candida albicans. Treatment of extract with trypsin completely abolished all or significant antibacterial activity against the tested bacteria, but slightly decreased antimicrobial activity against B. subtilis, and treatment of extract with chymotrypsin retained almost antibacterial activity against the tested bacteria except for E. coli D31. To confirm the additional enzyme stability of the extract, antimicrobial activity of the extract was tested after treated with several enzymes. Enzymes treated extract showed potent antimicrobial activity against B. subtilis and its activity was also retained for 5 h after trypsin treatments. Non-proteinaceous materials in the acidified extract also showed strong DNA-binding ability but did not show bacterial membrane permeabilizing ability. All our results indicate that mussel extract might contain the proteinaceous or non-proteinaceous antibacterial materials target not bacterial membrane but intracellular components. These results could be used to develop mussel extract as an additive for the improvement of stability or antimicrobial activity of antibiotics against specific bacteria.

Immunomodulatory and Therapeutic Potential of Enrofloxacin in Bovine Sub Clinical Mastitis

  • Mukherjee, Reena;Dash, P.K.
    • Asian-Australasian Journal of Animal Sciences
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    • v.16 no.6
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    • pp.889-893
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    • 2003
  • Immunomodulatory and therapeutic potential of Enrofloxacin was studied in bovine sub clinical mastitis (SCM). The therapeutic efficacy was adjudged by Somatic cell count and Total bacterial count of the milk, whereas, the immuno modulatory potential of the drug was assessed by measuring myeloperoxidase (MPO) and acid phosphates (ACP) enzyme level in the milk leukocytes. Forty-five cows were divided into three equal groups. Gr I consisting 15 cows served as healthy control, whereas, 30 cows (SCM), Gr II and Gr III, selected on the basis of California Mastitis Test (CMT) positive reaction. Gr II cows received 150 mg of Enrofloxacin, once a day for three days and Gr.III received sterile 5 ml PBS (pH 7.4) for 7days, both the treatment were given by intramammary route. The observation was made up to 30 days post-treatment (PT). The CMT of the healthy milk was negative (0), whereas, it ranged between 1 point score and 2 point score in SCM. The Somatic cell count (SCC) and Total bacterial count (TBC) decreased significantly (p<0.05) on day 3 PT in GrII cows in Enrofloxacin treated group, however, such changes were insignificant in PBS treated group. Traces of MPO and ACP enzyme were found in the healthy milk. The mean ACP level enhanced by 70% on day 3 PT in GrII and only 18.7% in Gr. III cows. The mean MPO level enhanced to 32% in Gr. II and 18 % in Gr. III cows on day 3 PT. Concomitant use of Enrofloxacin in SCM at sub optimal dose was found to reduce the bacterial load by increasing the bactericidal enzyme level in the milk polymorphonuclear cells (PMNs) in bovine SCM, which indicates its immunomodulatory potential in mastitis.

Critical Role of Glu175 on Stability and Folding of Bacterial Luciferase: Stopped-flow Fluorescence Study

  • Shirazy, Najmeh Hadizadeh;Ranjbar, Bijan;Hosseinkhani, Saman;Khalifeh, Khosrow;Madvar, Ali Riahi;Naderi-Manesh, Hossein
    • BMB Reports
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    • v.40 no.4
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    • pp.453-458
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    • 2007
  • Bacterial luciferase is a heterodimeric enzyme, which catalyzes the light emission reaction, utilizing reduced FMN (FMNH2), a long chain aliphatic aldehyde and $O_2$, to produce green-blue light. This enzyme can be readily classed as slow or fast decay based on their rate of luminescence decay in a single turnover. Mutation of Glu175 in $\alpha$ subunit to Gly converted slow decay Xenorhabdus Luminescence luciferase to fast decay one. The following studies revealed that changing the luciferase flexibility and lake of Glu-flavin interactions are responsible for the unusual kinetic properties of mutant enzyme. Optical and thermodynamics studies have caused a decrease in free energy and anisotropy of mutant enzyme. Moreover, the role of Glu175 in transition state of folding pathway by use of stopped-flow fluorescence technique has been studied which suggesting that Glu175 is not involved in transition state of folding and appears as surface residue of the nucleus or as a member of one of a few alternative folding nuclei. These results suggest that mutation of Glu175 to Gly extended the structure of Xenorhabdus Luminescence luciferase, locally.

Analysis and Characterization of Glutathione Peroxidases in an Environmental Microbiome and Isolated Bacterial Microorganisms

  • Yun-Juan Bao;Qi Zhou;Xuejing Yu;Xiaolan Yu;Francis J. Castellino
    • Journal of Microbiology and Biotechnology
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    • v.33 no.3
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    • pp.299-309
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    • 2023
  • Glutathione peroxidases (Gpx) are a group of antioxidant enzymes that protect cells or tissues against damage from reactive oxygen species (ROS). The Gpx proteins identified in mammals exhibit high catalytic activity toward glutathione (GSH). In contrast, a variety of non-mammalian Gpx proteins from diverse organisms, including fungi, plants, insects, and rodent parasites, show specificity for thioredoxin (TRX) rather than GSH and are designated as TRX-dependent peroxiredoxins. However, the study of the properties of Gpx in the environmental microbiome or isolated bacteria is limited. In this study, we analyzed the Gpx sequences, identified the characteristics of sequences and structures, and found that the environmental microbiome Gpx proteins should be classified as TRX-dependent, Gpx-like peroxiredoxins. This classification is based on the following three items of evidence: i) the conservation of the peroxidatic Cys residue; ii) the existence and conservation of the resolving Cys residue that forms the disulfide bond with the peroxidatic cysteine; and iii) the absence of dimeric and tetrameric interface domains. The conservation/divergence pattern of all known bacterial Gpx-like proteins in public databases shows that they share common characteristics with that from the environmental microbiome and are also TRX-dependent. Moreover, phylogenetic analysis shows that the bacterial Gpx-like proteins exhibit a star-like radiating phylogenetic structure forming a highly diverse genetic pool of TRX-dependent, Gpx-like peroxidases.

Efficacy of Diphenyleneiodonium Chloride (DPIC) Against Diverse Plant Pathogens

  • Jung, Boknam;Li, Taiying;Ji, Sungyeon;Lee, Jungkwan
    • Mycobiology
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    • v.47 no.1
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    • pp.105-111
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    • 2019
  • Many of the fungicides and antibiotics currently available against plant pathogens are of limited use due to the emergence of resistant strains. In this study, we examined the effects of diphenyleneiodonium chloride (DPIC), an inhibitor of the superoxide producing enzyme NADPH oxidase, against fungal and bacterial plant pathogens. We found that DPIC inhibits fungal spore germination and bacterial cell proliferation. In addition, we demonstrated the potent antibacterial activity of DPIC using rice heads infected with the bacterial pathogen Burkholderia glumae which causes bacterial panicle blight (BPB). We found that treatment with DPIC reduced BPB when applied during the initial flowering stage of the rice heads. These results suggest that DPIC could serve as a new and useful antimicrobial agent in agriculture.

Optimum culture conditions for production of extracellular cytosine deaminase by bacellus polymyxa YL 38-3 (Bacillus polymyxa YL38-3의 세포외 cytosine deaminase 생성의 최적 배양 조건)

  • 유대식;김대현;박정문;송형익;정기택
    • Korean Journal of Microbiology
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    • v.26 no.4
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    • pp.362-367
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    • 1988
  • The strain YL 38-3, which was capable of producing extracellular cytosine deaminase, was isolated and taxonomically examined. The isolated strain was identified to be Bacillus polymyxa YL 38-3. The optimal conditions for the enzyme production from Bacillus polymyxa YL 38-3 were investigated. The enzyme production was reached maximum level in the medium containing 0.5% glucose, 0.2% beef extract, 0.5% NaCl and 0.1% $KH_{2}PO_{4}$ (pH 6.0). And the enzyme showed the highest activity when the strain YL 38-3 was cultivated at $35^{\circ}C$ for 24 gours under the initial pH 6.0. By the additions of peptone the extracellular enzyme production was inhibited, meanwhile the intracellular enzyme production was highly stimulated. It was, therefore, deduced that peptone was related to the secretion mechanism of the enzyme from this bacterial cell.

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