• 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.

Expression of Serratia marcescens Metalloprotease(SMP)Gene in Escherichia coli and Serratia marcescens (대장균과 Serratia marcescens에서 Serratia marcescens Metalloprotease(SMP) 유전자의 발현)

  • Kim, Ki-Seok;Jung, Jae-Yeon;Park, Kun-Sik;Kim, Tae Un;Byun, Si Myung;Shin, Yong Chul
    • Microbiology and Biotechnology Letters
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    • v.23 no.3
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    • pp.288-296
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    • 1995
  • To investigate high-level expression of Serratia marcescens metalloprotease (SMP) in Escherichia coli and S. marcescens, we constructed various recombinant plasmids: pSP2, containing SMP gene and lac promoter; pKSP2, containing SMP gene and tac promoter; pTSP2, containing SMP gene, trc99a promoter, and lacI$^{q}$. The recombinant E. coli (pKSP2) strain expressed SMP to a high-level, about 36% of total cellular proteins but accumulated inactive SMP precursors intracellularly, which indicated that E. coli does not have activation and secretion system for SMP. To overproduce active SMP, we transformed S. marcescens with the recombinant plasmids by a modified CaCl$_{2}$ method. The recombinant S. marcescens ATCC27117 (pSP2) containing lac promoter for SMP transcription produced 530 U/ml of active SMP on LB broth, which is about 5.1 times of the SMP yield, 105 U/ml of a control strain, S. marcescens ATCC27117 (pUC19). However, S. marcescens ATCC27117 (pKSP2) containing tac promoter for SMP transcription did not grow healthy and hardly produced SMP. To overcome a harmful effect of the strong tac promoter, we constructed a regulatory plasmid pTSP2 containing a strong trc99a promoter and its repressor gene lacI$^{q}$. When S. marcescens ATCC27117 (pTSP2) was induced with 1.0 mM IPTG after 9 hr cultivation, 2,200 U/ml of SMP was obtained in LB broth, which is about 21 times of that of a control strain.

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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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The Effects of Amino Acids and Metaolites on the Biosynthesis of Biodegradative Theronine Dehydratase in Serratia matcescens ATCC25419 (아미노산과 대사산물들이 Serratia marcescens Biodegradative Threonine Dehydratase의 생합성에 미치는 영향)

  • 최병범;김승수
    • Microbiology and Biotechnology Letters
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    • v.23 no.1
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    • pp.24-30
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    • 1995
  • The effects of amino acids in growth media on the biosynthesis of Serratia marcescens biodegradative threonine dehydratase activity were examined. The enzyme activity was decreased by 44 and 34% by 10 mM isoleucine and valine, respectively, whereas it was increased approximately by 20% by 10 mM threonine. Among several metabolites tested, pyruvate increased the enzyme activity by 60% at 5 mM, but decreased the enzyme activity approximately by 20 to 70% above 20 mM. The enzyme activity was increased by 64% by 5 mM glyoxylate, whereas it decreased the enzyme activity approximately by 40 to 70% above 20 mM glyoxylate. The thiamine, monopyrrole derivative, also increased the enzyme activity by 84% at 50 $\mu $g/ml, but did not affected the enzyme activity above 300 $\mu $g/ml. cAMP increased the enzyme activity by 58% at 0.5 mM, but decreased the enzyme activity by 15% at 2 mM. These data suggested that the biosynthesis of Serratia marcescens biodegradative threonine dehydratase is regulated by concentrations of pyruvate, glyoxylate and cAMP.

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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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