• BMB Reports
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• 제31권1호
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• pp.37-43
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• 1998

The catabolic ${\alpha}$-acetolactate synthase was purified to homogeneity from Serratia marcescens ATCC 25419 using ammonium sulfate fractionation, DEAE-Sepharose, Phenyl-Sepharose, and Hydroxylapatite column chromatography. The native molecular weight of the enzyme was approximately 150 kDa and composed of two identical subunits with molecular weights of 64 kDa each. The N-terminal amino acid sequence of the enzyme was determined to be Ala-Gln-Glu-Lys-Thr-Gly-Asn-Asp-Trp-Gln-His-Gly-Ala-Asp-Leu-Val-Val-Lys-Asn-Leu. It was not inhibited by the branched chain amino acids and sulfometuron methyl herbicide. The optimum pH of the enzyme was around pH 5.5 and the pI value was 6.1. The catabolic ${\alpha}$-acetolactate synthase showed weak immunological relationships with recombinant tobacco ALS, barley ALS, and the valine-sensitive ALS isozyme from Serratia marcescens.

• Biotechnology and Bioprocess Engineering:BBE
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• 제7권2호
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• pp.100-104
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• 2002

Serratia marcescens biovar A2/A6, isolated from an Indonesian freshwater source, was identified based on extensive morphological, biochemical and genetic characterization. Formation of pigment was found to be strongly influenced by environmental conditions. Placket-Burman design was used to analyze the effect of carbon and nitrogen sources. Based on results of physiological and biochemical studies, the optimum conditions for growth and pigment formation were incubation 30$^{\circ}C$ in a neutral to slightly alkaline medium containing lactic acid and beef extract.

• 한국미생물·생명공학회지
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• 제51권3호
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• pp.309-313
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• 2023

Here we report essential features of the draft genome of an AmpC-β-lactamase-producing bacterial isolate obtained from farm tomatoes in South Africa. The isolate designated strain Tom1 featured a genome of 4950426 bp with a G+C% of 59.83. It was identified as Serratia marcescens by ribosomal multilocus sequence typing (rMLST), digital DNA-DNA hybridization (dDDH), average nucleotide identity (ANI), and phylogenetic analysis using reference genomes. Its genome encoded an AmpC-β-lactamase (bla_SST-1), an efflux pump providing tetracycline resistance (tet(41)), and an aminoglycoside acetyltransferase (aac(6')-Ic). Additionally, genes encoding proteins involved in prodigiosin biosynthesis and associated with adherence, biofilm formation, virulence, and pathogenicity were detected.

• Journal of Microbiology and Biotechnology
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• 제2권3호
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• pp.209-214
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• 1992

Serratia marcescens co-cultured with various phytopathogenic fungi, including Rhizopus stolonifer, Helminthosporium allii, Pyricularia oryzae, Fusarium oxysporium and Collectothricom cassiicola, in an LB- agar medium containing 1.5% swollen chitin, significantly inhibitied fungal growth. Fungal hyphae grew rapidly outward from the culture dish center, but the hyphal extensions of the pathogenic fungi were significantly inhibited in a perimetric contact area with S. marcescens. This was especially evident in pathogenic fungi which have a high chitin content in their cell walls. The extracellular chitinase activities of S. marcescens were increased seven fold by the addition of 1.5% swollen chitin to the LB-broth, compared to chitinase activities in a culture medium without chitin. The type of induction was dependent on the various forms of chitin used. When the culture supernatant of S. marcescens or the chitinases of Streptomyces griceus purchased from Sigma Chemical Co., were incubated with the mycelium of F. oxysporium, the mycelium gradually burst as cultivation time progressed and completely lysed after incubation for 2 days. On the other hand, E. coli extract did not hydrolyze the F. oxysporium mycelium at all. These data showed that the chitinolytic activities of S. marcescens play important roles in the biochemical control of phytopathogenic fungi.

• 한국응용곤충학회지
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• 제32권3호
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• pp.330-337
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• 1993

벼멸구에 강한 병원성이 있는 Serratia marcescens, biotype A2a를 분리, 동정하였다. 벼 유묘에 분무한 후 성충-계절풍을 따라 비래하는 형태-을 공시하고 병원성을 조사하여 3~5일 만에 강한 살충력을 발견하였다. 따라서, 본 세균의 곤충병원성 관련 형질 탐색을 하기 위하여 Tn5로써 돌연변이를 시도한 후, Chitinase, Protease, DNase indicator media에서 돌연변이 계통을 분리하였다. 이들을 공시충에 병원성을 검정한 결과 Pro-Strain중에서 병원력이 현저히 떨어지는 현상을 관찰하였다. 공시충을 전자현미경(SEM, TEM)으로 관찰하여, abdomen의 전장부위와 표피사이에 다수의 세균이 증식하였음을 발견하였다. 곤충복부표피조직 중 cuticle층은 intact한 상태였다. 따라서, 이에 관련된 유전자를 분리하기 위해 genomic library 실험을 진행하고 있다.

• Journal of Life Science
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• 제9권1호
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• pp.54-57
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• 1999

We have got several clones from Serratia marcescens which stimulated the cells to use maltose as a carbon source in E. coli TP2139 (${\Delta}$lac, ${\Delta}$crp). One of the cloned genes, pCKB13, was further analyzed. In order to find whether the increased expression of the gene under the direction of maltose metabolism, we constructed several recombinant subclones. We have confirmed that the clone, pCKB13 codes Coenzyme A transferase gene by partial nucleotide sequencing in the terminal region. The enzyme activity of Coenzyme A transferase increased after introduction of the multicopy of the cloned gene in E. coli. The recombinant proteins expressed by multicopy and induction with IPTG, two polypeptide of 26-and 28-kDa, were confirmed by SDS-PAGE. Southern hybridization analysis confirmed that the cloned DNA fragment was originated from S. marcescens chromosomal DNA.

• Journal of Microbiology and Biotechnology
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• 제17권10호
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• pp.1622-1628
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• 2007

We characterized the efficacy of an electrostatic precipitator (ESP) air-cleaner in reducing the concentration of Serratia marcescens in an enclosed space. We used an experimental room ($4.5{\times}3{\times}2.9\;m$) in which electrostatic air-cleaners were located. Two air-cleaners enhanced the equivalent ventilation rates in the chamber by about 3.3 air changes per hour (ACH) over the 2 ACH provided by the mechanical ventilation system. Natural die-off of the organisms provided an additional equivalent of 3 ACH, so that the total ventilation rate with the ESP air-ccleaners was 8.3 ACH. We also examined whether the ESP air-cleaners altered the deposition of Serratia marcescens aerosols on the experimental room surfaces. We did not find any significant differences in the number of colony forming units recovered from surfaces with and without the air-cleaners. We installed UV lights inside the ESPs and determined if UV light, in addition to electrical fields, increased the efficacy of the ESPs. The presence of UV light inside the ESP reduced S. marcescens aerosols by approximately 2 ACH. Finally, a box model indicates that the efficiency of the air-cleaner increases for both biological and nonbiological particles at ventilation rates of 0.2-1, which are typical for residential settings.

• 미생물학회지
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• 제30권6호
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• pp.507-513
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• 1992

Serratia marecescens RH1 isolated from soil samples produced large amount of extracellular proteases. One of the genes encoding an extracellular protease form S. marcescens RH1 was cloned in Escherichia coli by shot gun cloning method. The cloned protease, SSP, was stably expressed by its own promoter and excreted into the extracellular medium from E. coli host (ORF) of 3.135 nucleotides corresponding to 1.045 amino acids (112 kDa). The nucleotide and deduced amino acid sequence of SSP showed high overall homology (88%) to one of the S. marcescens protease (27), but low homology to other serine protease families. The optimal pH and temperature of the enzyme were pH 9.0 and 45.deg.C respectively. The activity of protease was inhibited by phenylmethylsulfonyl fluoride (PMSF), which suggests that the enzyme is a serine protease.

• Biotechnology and Bioprocess Engineering:BBE
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• 제7권1호
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• pp.38-42
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• 2002

A chitinase gene (pCHi58) encoding a 58 kDa chitinase was isolated from the Serratia marcescens KCTC 2172 cosmid library. The chitinase gene consisted of a 1686 bp open reading frame that encoded 562 amino acids. Escherichia coil harboring the pChi58 gene secreted a 58 kDa chitinase into the culture supernatant. The 58 kDa chitinase was purified using a chitin affinity column and mono-S column. A nucleotide and N-terminal amino acid sequence analysis showed that the 58 kDa chitinase had a leader peptide consisting of 23 amino acids which was cleaved prior to the 24th alanine. The 58 KDa chitinase exhibited a $98\%$ similarity to that of S. marcescens OMB 1466 in its nuclotide sequence. The chitinolytic patterns of the 58 kDa chitinase released N,N'-diacetyl chitobiose (NAG2) as the major hydrolysis end-product with a trace amount of N-acetylglucosamine. When a 4-methylumbellyferyl-N-acetylglucosamin monomer, dimmer, and tetramer were used as substrates, the 58 kDa chitinase did not digest the 4-Mu-NAG monomer $(analogue\;of\;NAG_2)$, thereby indicating that the 58 kDa chitinase was likely an endochitinase. The optimum reaction temperature and pH of the enzyme were $50^{\circ}C$ and 5.0, respectively.

• BMB Reports
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• 제32권2호
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• pp.210-213
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• 1999

In Serratia marcescens, acetolactate produced by the catabolic acetolactate synthase (ALS) is converted into acetoin, its physiological role of which is to maintain intracellular pH homeostasis. In this study, the expression mode of catabolic ALS by aeration and branched-chain amino acids was examined by the ELISA method. The amount of catabolic ALS decreased approximately 93% under aerobic conditions. We also showed that the expression of catabolic ALS decreased approximately 34 % and 65 % in the presence of 2.5 mM and 10 mM leucine, respectively. The repression of catabolic ALS by leucine has not been reported previously. In contrast to leucine, catabolic ALS levels increased approximately 13% and 38% by treatment with 2.5 mM and 10 mM isoleucine, respectively, while valine alone did not have any significant effect on the synthesis of catabolic ALS. The amount of catabolic ALS was also reduced to approximately 32% and 45% in the presence of 10 mM Leu+Ile and Leu+Ile+Val, respectively. The regulatory mode of the Serratia catabolic ALS suggests that catabolic ALS may also have a role in supplying acetolactate as an intermediate of valine and leucine biosynthesis in addition to the maintenance of internal pH.