• 한국생물공학회:학술대회논문집
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• 2002.04a
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• pp.473-476
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• 2002

A lignin degradation bacteria, symbiotic bacteria was isolated from the gut of Sympetrum depressiusculum and tested for its lignin degrading activity using lignin model compounds and related aromatic compounds. The strain was identified as Serratia marcescens HY-5 based on the 165 rDNA, cellular fatty acid composition, biochemical and physiological characteristics. S. marcescens showed 40-50% lignin degrading activity in the media that contained vaillin, guaiacol and dealkaline lignin. S. marcescens showed three ligninase activities [Jaccase, lignin peroxidase(LiP) and Manganase peroxidase(MnP)]. Addition of dealkaline lignin to the basal media increased about 6fold of laccase activity. Vanillic acid or vanillin increase 1.3fold of MnP activity and p-coumaric acid increased 12fold of LiP activity which added to the basal medium.

• The Korean Journal of Food And Nutrition
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• v.9 no.4
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• pp.372-378
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• 1996

The effects of branched chain amino acids and metabolites in growth media on the biosynthesis of Serratia marcescens threonine dehydratase activity were examined. The enzyme activity was decreased above 60% by leucine among the range from 1 to 20 mM, and the enzyme activity was decreased approximately 20% by a low concentration of valine (1 to 4 mM), but not affected at high concentration (20 mM). However, the enzyme activity was increased approximately 100 to 140% by a low concentration of isoleucine (1 to 4 mM), but decreased approximately 25 to 80% at high concentration (15 to 30 mM). The enzyme activity was decreased by 25 and 58% by the simultaneous addition of all three branched chain amino acids at 2 and 10 mM concentration, respectively, but increased by 75 and 50% by the combination addition of isoleucine plus valine and isoleucine plus leucine at 2 mM, respectively. cAMP was decreased the enzyme activity approximately 10 to 40% by a low concentration (1 to 2 mM), but increased by 80% at high concentration (10 mM). These data suggest that S. marcescens threonine dehydratase should be multivalently repressed by branched chain amino acids, but positively regulated by a low isoleucine concentration and may play a regulatory role in an isoleucine biosynthetic pathway unlike the E. coli K-12 enzyme.

• BMB Reports
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• v.30 no.1
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• pp.13-17
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• 1997

The inhibitory effect of herbicides such as sulfonylurea derivatives, imidazolinones and pyrimidylsalicylate has been examined on the purified valine sensitive acetolactate synthase (ALS) from Serratia marcescens. The concentration of sulfometuron methyl which inhibits 50% of the ALS activity was 2.5 mM. The required concentrations of triasulfuron, primisulfuron methyl and imazaquin for the 50% inhibition of the ALS activity were 1 mM. The resistance of Serratia ALS to sulfometuron methyl, imazapyr and imazaquin is similar to that of E. coli ALS 1. However, pyrimidylsalicylate showed a potent inhibitory effect on the Serratia ALS almost 13 times more potent than on E. coli ALS II, which is known as herbicide-sensitive isozyme. The inhibitory mode was competitive against pyruvate. 150 value was determined to be $17{\mu}M$ in an assay mixture containing 20 mM pyruvate, and the $K_1$, value was calculated to be $0.4{\mu}m$ from the modified double reciprocal plot of 1/V versus $1/S^2$.

• The Plant Pathology Journal
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• v.25 no.4
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• pp.369-375
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• 2009

The potential antiviral effects of the culture filtrates (CF) from Serratia marcescens strain Gsm01 against yellow strain of Cucumber mosaic virus (CMV-Y) were investigated. The culture filtrate of S. marcescens strain Gsm01 applied on Chenopodium amaranticolor showed high inhibitory activity, likewise no necrosis appeared when applied on the tobacco plants 2 days before CMV-Y inoculation. When plants were challenge inoculated with CMV-Y for eighteen days, the disease incidence in plants with culture filtrate of S. marcescens Gsm01 did not exceed 59%, whereas 100% of control plants were severely infected. The results of double antibody sandwich-enzyme linked immunosorbent assay (DAS-ELISA), reverse transcriptase polymerase chain reaction (RT-PCR), dot blotting, and western blotting showed that culture filtrate treatment highly affected the accumulation of CMV-Y or its CP protein gene in the treated plant leaves. It was also observed that the culture filtrate had no RNase activity on genomic RNAs of CMV-Y, suggesting that culture filtrate may not contain ribosome inactivating proteins (RIPs) or proteins with RNase activity. These data shows that culture filtrate of S. marcescens strain Gsm01 seems to be a promising source of antiviral substance for the practical use.

• KSBB Journal
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• v.11 no.1
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• pp.92-98
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• 1996

A chitinase-producing bacterium was isolated from seashore mud around Beobseongpo in Chunnam province by selective enrichment culture, and among it, one isolate which was the best in producing of chitinase was selected. Nutrient or MacConkey medium was confirmed with secreting of prodigiosin pigment by Serratia sp. JM, and it was performed by the production of clear zone on medium containing chitin. Serratia sp. JM was almost same compared with Serratia marcescens ATCC 27117 in respect of its morphological, physiological and biochemical characteristics except succinic, urea and pyruvic acid. Serratia sp. JM was resistant to tetracycline but was not resistant to kanamycin and chloramphenicol. The optimal temperature and pH for the production of chitinase from Serratia sp. JM were $30^{\circ}C$ and 7.5, respectively. Production of chitinase and pH in the medium increased until the cultivation of 120 hours, but after 120 hours, they were decreased due to the acetic acid accumulated from degradation of chitin by Serratia sp. JM.

• Applied Biological Chemistry
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• v.34 no.1
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• pp.54-60
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• 1991

Serratia marcescens CK-3, decomposing chitin which is a mar component of cell wall in phyitopathogenic fungi, was isolated from the continuous cropping rhizosphere of pepper and cucumber and its enzymatic property was examined. S. marcescens CK-3 was found tn have an tagonistic effects against, Fusarium axysporum and Rhizoctonia solani and to have complex enzyme system such as chitinase, laminarinase, and proteinase. The preferable composition of the medium for production of chitinase was fond and was as follows : colloidal chitin 1.5%, tryptone 0.5%, glucose 1.0%, peptone 0.2%, $MgSO_4{\cdot}7H_2O\;0.1%,\;K_2HPO_4\;0.1%,\;and\;NaCl\;0.1%$(w/v), pH 6.8. The maximum enzyme production was observed after culture of 72 hours at $30^{\circ}C$ using a medium containing the above chemical composition. The optimal pH and temperature for in vitro activity of chitinase from S. marcescens CK-3 were pH 7.5 and $50^{\circ}C$, respectively. The enzyme activity in-creased by metal ions such as$Ag^+$ and $Mn^{++}$.

• Journal of Life Science
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• v.8 no.3
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• pp.263-271
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• 1998

One of the better-characterized transcription factor of E. coli is the cAMP receptor protein(CRP) and the CRP binds cAMP and DNA. The cAMP-CRP complex is involved in regulation of many genes at bacteria. The cAMP-CRP regulatory element represents, in some respects, a global regulatory network. The aim of this work was to study the structure and the mechanisms controlling the expression of CRP in Serratia marcescens. We have been get 5 different clones from Serratia which stimulated the cells to use maltose as a sole carbon source in E. coli TP2139. The crp gene clone, pCKB12, was confirmed by Southern hybridization with E. coli crp gene. The location of the crp gene was determined by construction subclones carrying various portions of pCKB12. To investigate the potential role of CRP in E. coli, lacZ fused plasmids were constructed and investigated the ${\beta}$-galactosidase activity of the fused plasmid. The Serratiamarcescens cAMP receptor protein can substitute the E. coli CRP in transcriptional activation at the lacZ gene. These results suggest that Serratia marcescens cAMP receptor protein complex functions to regulate several promoters in E. coli.

• Journal of fish pathology
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• v.6 no.2
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• pp.103-110
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• 1993

Total genomic DNA library of Serratia marcescens was prepared by inserting Sau3AI partial digesting fragments(above 5 kb) into the dephosphorylated BamHl site of pUC19. In primary screening, two colonies were selected by observing the halo around E. coli transformants grown on the swollen colloidal chitin media. Secondary screening was performed by soaking two colonies with a few drops of 4-methylumbelleliferryl N-acetyl-$\beta$-D-glucocosaminide(4-MuNGlcNAc). As 4-MuNGlcNAc is a specific, fluorogenic substrate for chitinase, the positive clones produce light fluorescence by the exposure under the long wave U.V. light(360 nm). From genomic DNA library derived from pUC19, we have isolated two different chitinase clones, pCH1(11.0Kb) and pCH2(7.5Kb), which show completely different restriction map to each other. The cross-hybridization of pCH1EA and pCH2 have not revealed any hybridization signals to each other.

• BMB Reports
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• v.34 no.2
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• pp.109-113
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• 2001

The Serratia marcescens metalloprotease inhibitor (SmaPI) is a proteinase inhibitor toward Serratia marcescens metalloprotease (SMP). The three-dimensional structure of SmaPI was calculated by computer modeling using the structure complex between SMP and the Erwinia chrysanthemi inhibitor as a template. Based on this model structure, the substitution of the amino acid residues, Ala4, Leu-5, Pro-6, and Thr-7, were located at the hinge region of the N-terminal segment by site-directed mutagenesis. Although the A4R and T7A mutant SmaPIs showed a nearly full inhibitory activity, the inhibitory activity of SmaPI decreased significantly when the Leu-5 was converted to Ala, Gly, Ile, or Val. Surprisingly, the L5I and L5V mutant SmaPIs showed less inhibitory activities than the L5A mutant. From these results, we suggested that the orientations and positions of respective aliphatic groups in the side-chain of position 5 mainly affected the inhibitory activity of SmaPI. The overall side-chain hydrophobicity was only slightly affected. The side-chain of the Leu-5 residue contributed approximately 0.79 kcal/mol out of 8.44 kcal/mol to the binding of SmaPI with SMP The inhibitory activities of P6A and F6G were also severely decreased. The Pro-6 may have a critical role in maintaining the strict conformation of the N-terminal portion that may be important in the inhibitory activity of SmaPI. In conclusion, Leu-5 and Pro-6 have crucial roles in the inhibitory function of SmaPI toward SMP.

• The Journal of the Korean Society for Microbiology
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• v.13 no.1
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• pp.25-30
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• 1978

Among clincal isolates, most strains of Serratia marcescens were belonged to nonpigmented form, and several attempts were undertaken for the rapid and simple identification of these strains. Prodigiosin production of non-pigmented strains was uniformly negative in many kinds of solid media as well as in nutrient agar added with various amino acids and thiamine. On blood agar, colonies of S. marcescens turned gradually to grey or dark color by the lapse of incubation period and this characteristic seems to be able to utilize as an indicator for a primary isolation, and also generally paralleled with the results of dehydration of Tween 80 and lipase activity in soy bean oil medium although these reactions were by no means specific to S. marcescens. In order to rule out these non-specific reactions, other tests such as oxidase and sucrose fermentation are required for the final confirmation of this species.