• Title, Summary, Keyword: Serratia marcescens

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Optimal Conditions for Chitinase Production by Serratia marcescens

  • Cha, Jin-Myeong;Cheong, Kyung-Hoon;Cha, Wol-Suk;Choi, Du-Bok;Roh, Sung-Hee;Kim, Sun-Il
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.9 no.4
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    • pp.297-302
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    • 2004
  • A chitinase-producing bacterium was isolated from seashore mud around Beobseongpo in Chunmam province through the use of a selective enrichment culture. The best chitinase producing strain was isolated and identified as Serratia marcescens KY from its characteristics. For effective production of chitinase, optimum pH, temperature, and agitation speed were investigated in flask cultures. The optimum pH using Serratia marcescens KY was between pH 6 and 7 and the chitinase produced was 37.9 unit/mL. On the other hand, the optimal pH of the Serratia marcescens ATCC 27117 was 7.5, and the produced amount of chitinase was 35.2 unit/mL. The optimal temperature for chitinase production for Serratia marcescens KY and Serratia marcescens ATCC 27117 was $30^{\circ}$. The cell growth pattern at different temperature was almost identical to the chitinase production. To investigate the optimal shaking speed under optimal culture, speeds were varied in the range of 0∼300 rpm. The maximum production of chitinase was carried at 200 rpm although the cell growth was the highest at 150 rpm. It indicates that oxygen adjustment is required for the maximum chitinase production. Using optimal conditions, batch cultures for comparing Serratia marcescens KY and Serratia marcescens ATCC 27117 were carried out in a 5 L fermentor. The oxygen consumption was increased with the increase of culture. Especially, at 120 h of culture Serratia marcescens KY and Serratia marcescens ATCC 27117 produced 38.3 unit/mL, and 33.5 unit/mL, respectively.

Optimization of Culture Conditions for toe Production of Chitinase (Chitinase 생성을 위한 배did 조건 최적화)

  • 차진명;석근영;차월석
    • KSBB Journal
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    • v.16 no.4
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    • pp.365-369
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    • 2001
  • Chitinase producing microorganism, Serratia marcescens KY, was isolated from seashore mud around Beobseongpo in Chunnam province by selective enrichment culture. As the colloidal chitin concentration increased, chitinase production was increased. But chitinase production with addition of other carbon sources (glucose, fructose, galactose, maltose, sucrose, starch) was decreased. The effect of nitrogen sources on the chitinase production with serratia marcescens KY was as fellows. The opitimum mineral concentration for chitinase production was K$_2$HPO$_4$ 0.2 g/L and MgSO$_4$ 0.20 ∼ 0.25 g/L, respectively. The effect of nitrogen sources on chitinase production by Serratia marcescens KY was increased as follows, tryptone > yeast extract > beef extract > asparagine.

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Isolation and Identification of Serratia marcescens strain US50-3 Producing Water-Soluble Red Pigment (수용성 적색 색소를 생산하는 Serratia marcescens US50-3 균주의 분리 및 동정)

  • 양인영;황순욱
    • Microbiology and Biotechnology Letters
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    • v.23 no.6
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    • pp.777-780
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    • 1995
  • A strain US50-3 producing water-soluble red pigment was isolated from the pond separating oil from water near the oil storage tanks. The strain US50-3 was identified as a strain of Serratia marcescens considering its morphological and physiological characteristics, and DNA G+C contents. It showed a little difference comparing to the Type strain and was considered to be another biotype strain.

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Enzymatic Properties of Serratia marcescens Pretense (Serratia marcescens Protease의 효소학적 특성)

  • 최병범
    • The Korean Journal of Food And Nutrition
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    • v.16 no.2
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    • pp.152-157
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    • 2003
  • Serratia marcescens ATCC 25419 protease was purified to homogeneity by ammonium sulfate treatment, and DEAE-cellulose anion exchange chromatography. The specific activity of the enzyme was increased 448-fold during purification with an overall yield of 43.0%. Metal reactivation on the purified protease from S. marcescens was studied. S. marcescens protease was a metalloenzyme to be completely inhibited its activity by EDTA and the enzyme outstandingly inhibited by Hg, Fe, Cu, but the activity was increased approximately 20% by Co. The reactivation of the apoenzyme was effective with Mn, Co, Zn in pH range from 6 to 8. Among metalloenzymes prepared to the addition of Mn, Co, Zn to restore the degree of activity of native enzyme, Zn-enzyme was similar to the native enzyme in respects with enzyme activity, alkali-inactivation, thermo-stability.

Red Pigment Producing Serratia marcescens Isolated from Abalone (Haliotis discus) (전복(Haliotis discus)에서 분리한 Serratia marcescens가 생산하는 적색 색소의 항균활성)

  • Shin, YuJin;Kang, Chang-Ho;So, Jae-Seong
    • KSBB Journal
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    • v.31 no.4
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    • pp.214-218
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    • 2016
  • Serratia marcescens characterized by the ability to produce red pigments inhabits various ecological niches. A strain Serratia marcescens PYU was isolated from abalone (Haliotis discus) collected at the West Sea in Korea. The isolated strain was gram-negative, motile, rods like coccus, oxidase-negative, and catalase-positive; and formed red pigment. S. marcescens PYU was grown in the presence of 0~10% (w/v) NaCl, at pH 4~9, and at $10{\sim}40^{\circ}C$. The strain PYU produced red pigment, and the extracted pigment showed antibacterial activity against Streptococcus iniae and Lactococcus garviae which has been known as an important fish pathogens. Further studies are underway to elucidate the direct relationship between the red pigment and antibacterial activity.

Molecular Cloning of Serratia rnarcescens Metalloprotease Gene into Escherichia coli (Serratia marcescens Metalloprotease 유전자의 대장균에로의 클로닝)

  • 김기석;이창원;이상열;이병룡;신용철
    • Microbiology and Biotechnology Letters
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    • v.20 no.3
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    • pp.280-288
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    • 1992
  • Molecular cloning of metalloprotease gene from Serratia marcescens ATCC 21074 into Escherichia coli JM109 was carried out. Chromosomal DNA of S. marcescens was completely digested with Hind111 and southern hybridization with a synthetic oligonucleotide probe revealed that a 50 KD metalloprotease gene was contained in 4.0 Kb chromosomal DNA fragment, 4.0 Kb chromosomal DNA fragments eluted from agarose gel were ligated with pUC19 and transformed into E. coli JM109. Nine positive clones were obtained from about $1\times 10^3$ transformants by colony hybridization. Their recombinant plasmids, pSPl and pSP2 have same chromosomal DNA fragments in pUC19 in opposite-orientations. When cloned metalloprotease gene was expressed in E. coli, about 52 KD precursor protein of metalloprotease was detected by western blot analysis from E. coli harboring a recombinant plasmid pSP2. Plasmid pSP2 showed no protease activities in E. coli but overproduced the active metalloprotease in S. rnarcescens ATCC 27117.

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Secretion of the cloned serratia marcescens nuclease in escherichia coli (Serratia marcescens nuclease의 escherichia coli에서의 분비)

  • 신용철;이상열;김기석
    • Korean Journal of Microbiology
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    • v.28 no.4
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    • pp.297-303
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    • 1990
  • Secretion of Serratia marcescens nuclease by E. coli harboring pNUC4 was investigated. 29.2, 54.2 and 16.6% of total nuclease were observed in culture medium, periplasm, and cytoplasm of E. coli, respectively. To investigate the secretion mechanism of Serratia nuclease by E. coli, secretion kinetics of nuclease was examined in the presences of sodium azide, and energy metabolism inhibitor; procaine, an exoprotein processing inhibitor; and chloramphenicol, a protein synthesis inhibitor. In the presence of sodium azide, periplasmic unclease was gradually decreased and the extracellular nyclease was linearly increased according to the incubation time. Similar results were obtained in presences of procaine and chloramphenicol. From these results, we concluded that two transport processes are involved in nuclease secretion: secretion of nuclease through the inner membrane is occurred by an energy-dependent process and probably requiring precusor processing: secretion of nuclease through outer membrane does not require energy, de novo protein synthesis, and precursor processing.

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Resistance of Some Metal Ions on Growth of Serratia marcescens Strain P (Serratia marcescens Strain P 성장에 미치는 중금속 내성)

  • 유관희;이호용
    • Microbiology and Biotechnology Letters
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    • v.20 no.6
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    • pp.693-698
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    • 1992
  • The resistant effect of several heavy metal ions to Serratia marcescens strain P was studied by the method of minimal inhibitory concentration(MIC), and testing for their metal biosorption. S. marcescens strain P showed a good survival in the presence of high concentrations of some metal ions, namely cadmium, lead, iron, magnesium, and manganese. Copper had the most inhibitory effect among tested. The MIC value was ranged from 0.79 to 1.58 mM. Cells of S. marcescens strain P exhibit an abnormally long lag phase when incubated in high concentrations of zinc and cadmium. Pigment production was reduced by zinc and cadmium, but enhanced by lead and iron. S. marcescens strain P was resistant to ampicillin, tetracycline, cefamandole and chloramphenicol with minimal inhibitory concentration of 128 $\mu$g/ml, 32 $\mu$g/ml, 256 $\mu$g/ml, and 8 $\mu$g/ml, respectively. The kinetics study of biosorptive uptake by S. marcescens strain P revealed that 16.59% of cadmium and 35.38% of lead were eliminated from the media.

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Study upon the Red Pigments Exracted from the Serratia Marcescens (Serratia marcescens로부터 추출한 적색 색소의 정제와 특성에 관한 연구)

  • Min, Seul-Ki;Park, Hee-Aurk
    • Journal of the Korean Applied Science and Technology
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    • v.33 no.3
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    • pp.599-605
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    • 2016
  • Serratia marcescens, a Gram-negative bacterium characterized by production of a nondiffusible red pigment. Serratia marcescens 2354 (ATCC 25419) was production and purification a high concentration of red pigments when growing on Cang's soytone (CS) culture broth with soytone and ethanol. The optimal temperature and intial pH range for the production of the red pigments were $28^{\circ}C$ and pH 7.5, respectively. The red pigments was separated and purified through organic solvents extraction. Characterization of the red pigments is studied by UV-spectrophotometer at ${\lambda}_{max}$ 537 nm. The HPLC-Mass analysis of the partially purified compounds showed two major peaks with the molecular masses of 537 and 565 g. The red pigments were stable at room temperature under the acidic pH (up to pH 6) but were unstable at the strong alkaline condition. And red pigments were stable at sun light.

Purification and Properties of Serratia marcescens Purine Nucleoside Phosphorylase. (Serratia marcescens Purine Nucleoside Phosphorylase의 정제 및 특성)

  • 방성권;신종란;최병범
    • Microbiology and Biotechnology Letters
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    • v.28 no.5
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    • pp.251-257
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    • 2000
  • Serratia marcescens purine nucleoside phosphorylase (PNP) was purfied to homogeneity by streptomycin sulfate treatment, Sephacry HR S-200 gel filtration chromatography and AMP-agarose affinity chromatography. The specific activity of the enzyme was increased 49-fold during purification with an overall yield of 7.0%. The molecular weight was 168kD as estimated by Sephadex G-150 gel filtration chromatography. The S. marcescens enzyme was composed of six identical subunits with subunit molecular weight of 28kD, as estimated by SDS-PAGE. The Km values of S. marcescens enzyme for inosine and deoxyinsoine were 0.38 and 1.20 mM, respectively. The ph optimum was near 8.0, and the enzyme was relatively heat-stable protein. The enzyme was inactivated com-pletely by 0.5 mM of $Cu^{ 2+}$.

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