• The Korean Journal of Food And Nutrition
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• v.19 no.4
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• pp.526-531
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• 2006

Minimum inhibition concentration(MIC), growth inhibition activity, and colony forming inhibitory activity of grapefruit seed extract against Bacillus cereus, Bacillus subtilis, Listeria monocytogenes, Escherichia coli, Salmonella enterifidis and Serratia marcescens were tested. MIC of grapefruit seed extract against Bacillus cereus, Bacillus subtilis, Listeria monocytogenes, Escherichia coli, Salmonella enteritidis and Serratia marcescens was 12.5, 12.5, 12.5, 50, 50, 100ppm, respectively. Growth inhibition concentration of grapefruit seed extract against Bacillus cereus, Bacillus subtilis, Listeria monocytogenes, Escherichia coli, Salmonella enteritidis and Serratia marcescens was below 1.0, 6.25, below 1.0, 6.25, 25, 25ppm, respectively. Colony forming inhibitory activity of grapefruit seed extract against Bacillus cereus, Bacillus subtilis, Listeria monocytogenes, Escherichia coli, Salmonella enteritidis and Serratia marcescens was 93.9, 94.0, 99.9, 4.4, 82.7, 86.4%, respectively. Colony forming inhibitory activities of grapefruit seed extract against Gram positive bacteria were higher than that against Gram negative bacteria.

• Journal of Microbiology and Biotechnology
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• v.20 no.5
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• pp.950-957
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• 2010

Serratiopeptidase (SRP), a 50 kDa metalloprotease produced from Serratia marcescens species, is a drug with potent anti-inflammatory property. In this study, a powerful statistical design, evolutionary operation (EVOP), was applied to optimize the media composition for SRP production in shake-flask culture of Serratia marcescens NRRL B-23112. Initially, factors such as inoculum size, initial pH, carbon source, and organic nitrogen source were optimized using one factor at a time. The most significant medium components affecting the production of SRP were identified as maltose, soybean meal, and $K_2HPO_4$. The SRP so produced was not found to be dependent on whey protein, but rather was notably induced by most of the organic nitrogen sources used in the study and free from other concomitant protease contaminant, as revealed by protease inhibition study. In addition, experiments were performed using different sets of EVOP design with each factor varied at three levels. The experimental data were analyzed with a standard set of statistical formula. The EVOP-optimized medium, with maltose 4.5%, soybean meal 6.5%, $K_2HPO_4$ 0.8%, and NaCl 0.5% (w/v), gave a SRP production of 7,333 EU/ml, which was 17-fold higher than the unoptimized media. The application of EVOP resulted in significant enhancement of SRP production.

• Proceedings of the Korean Journal of Food and Nutrition Conference
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• 2001.12a
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• pp.121-121
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• 2001

최소 배지에 여러 아미노산과 대사 산물을 첨가하여 배양시킨 Serratia marcescens ATCC 25419 세포추출물에서여 biodegradative threonine dehydratase (BDTD), biosynthetic threonine dehydratase (BSTD)와 acetolactate syntase (ALS)의 비활성도를 조사하였다. S. marcescens BDTD와 ALS는 낮은 농도 (0.5-2 mM)의 cAMP에 의해 촉진적 조절을 받으며, 비교적 낮은 농도의 isoleucine (1-4 mM)에 의해서는 S. marcescens BSTD의 생합성이 증가되고 높은 농도의 isoleucine (10-30 mM)에서는 감소되고 비교적 낮은 농도의 valine (2-4 mM)에 의해서 S. marcescens ALS의 생합성이 증가되는 것으로 보아 S. marcescens ATCC 25419에서 branched chain 아미노산 생합성 과정의 조절 양상은 Escherichia coli K-12와는 달리, isoleucine의 생합성 과정은 BSTD에 의해 조절되고, valine의 생합성 과정은 ALS에 의해 조절되는 것으로 사료된다.

• The Korean Journal of Pesticide Science
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• v.20 no.2
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• pp.152-158
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• 2016

The cause of death was investigated with several dead cabbage moth larvae in breeding box. Bacterial strains were isolated and selected from the dead larvae by bioassay. One of them was identified as Serratia marcescens used by morphological characteristics and gene sequencing. S. marcescens were cultured by Luria Bertani (LB) media broth for bioassay. When 100-fold dilution of culture broth to third larvae of diamondback moth, Plutella xylostella, it was showed a 100% mortality at 2 days after treatment, and only 10-fold dilution of supernatant liquid was showed 86.6% mortality. When the culture broth of S. marcescens was applied to the larvae of beet armyworm, Spodoptera exigua, contact and feeding toxicity were 20 and 8% of mortality, respectively. Otherwise, when the culture broth of S. marcescens was applied to 5 major plant pathogens, antibacterial activities against Fusarium oxysporum, Rhizoctonia solani, Colletotrichum gloeosporioides, Phytophthora capsici and Sclerotinias clerotiorum were 4.7, 11.3, 20, 15.7 and 42.6%, respectively. Also, degradation ability of S. marcescens against protein and chitin were examined.

• The Korean Journal of Food And Nutrition
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• v.10 no.4
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• pp.475-479
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• 1997

The effects of amino acids and metabolites in growth media on the biosynthesis of prodigiosin from Serratia marcescens ATCC 25419 were examined. The prodigiosin synthesis was decreased approximately by 50 to 80% by several amino acids and metabolites tested. The prodigiosin synthesis was increased approximately by 20 to 40% by a low concentration of glyoxylate(1 to 3mM) and outstandingly increased by 122% at 5mM concentration under anaerobic condition. However, the prodigiosin synthesis was decreased approximately by 50 to 90% at a high concentration(20 to 30mM) under anaerobic condition. The prodigiosin was not synthesized by pyruvate and $\alpha$-ketobutyrate under aerobic and anaerobic condition, with addition to glyoxylate under aerobic condition, among the range from 0.5 to 30mM, while the cell growth under anaerobic condition was decreased distinctly by a high concentration(20mM above) of glyoxylate. These data suggest that the growth and prodigiosin of S. marcescens is positively regulated by a low concentration of glyoxylate (1-5mM), but repressed by a high concentration of glyoxylate(20mM above) unlike pyruvate and $\alpha$-ketobutyrate.

• Microbiology and Biotechnology Letters
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• v.20 no.5
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• pp.511-518
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• 1992

We subcloned a 58 KD chitinase gene of Serratia marcescens into Escherichia coli and investigated the expression and secretion of the chitinase. Chitinase was produced in E. coli by using its own promoter but the levels of enzyme were very low, less than 5 mU/m$\ell$. However, by the combined action of the chitinase and lac promoters, the chitinase activity increased up to about 80 mU/m$\ell$. The most of the chitinase produced in E. coli was localized in periplasm and the small amounts were observed in cytosol and culture medium. Intracellular chitinase activities increased in proportion to the growth of E. coli up to the early stationary phase but rapidly decreased thereafter, which was assumed to be degradation of the chitinase by E. coli proteolytic enzymes.

• Korean Journal of Agricultural Science
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• v.40 no.3
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• pp.221-226
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• 2013

Degrees of hydrolysis by alkaline protease produced from Serratia marcescens S3-R1 is 3.95-6.30% of whey proteins during 5, 15, 30, 60, 90, 120,180, 240 min incubation at $40^{\circ}C$. Proteolytic pattern of the whey proteins showed that various low molecular weight peptides were generated during the incubation periods. The biological function of in Raw 264.7 cells treated with whey protein hydrolytic peptides, anti-inflammatory effect showed exhibit in the expression of pro-inflammatory cytokines such as TNF-${\alpha}$, IL-6, COX-2 and iNOS by PCR analysis. COX-2 and iNOS gene expression inhibited in Raw 264.7 cells on whey protein hydrolysates below 3,000 dalton. The protease from Serratia marcescens S3-R1 showed a potential in production of low molecular weight whey protein hydrolysates which could be used for industrial application.

• Journal of Microbiology and Biotechnology
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• v.10 no.5
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• pp.670-676
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• 2000

Several clones obtained from Serratia marcescens stimulated E. coli TP2139 (${\Delta}lac, \;{\Delta} crp$) cells to use maltose as a carbon source. The crp gene clone, pCKB12, was confirmed to stimulate the $\beta$-galactosidase activity, by Southern hybridization [31]. The nucleotide sequence of the crp region consisting of 1,979 bp was determined. The sequencing of the fragment led to the identification of two open reading frames: One of these, the crp gene, encoded 210 amino acid and the other encoded a truncated protein. The S. marcescens and E. coli crp genes showed a higher degree of divergence in their nucleotide sequence with 120 changes, however, the corresponding amino acid sequences showed only two amino acid differences. Yet, an analysis of the amino acid divergence revealed that the catabolite gene activator protein, the crp gene product, was the most conserved protein observed so far. Using a crp-lac protein fusion, it was demonstrated that S. marcescens CRP could repress its own expression, probably via a mechanism similar to that previously described for the E. coli crp gene.

• Korean Journal of Organic Agriculture
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• v.22 no.4
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• pp.855-868
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• 2014

Synthetic agro-chemicals have been widely used to control diseases on paprika but these days negative attention has been increasing to use of them because of several adverse effects. This research was conducted to isolate and to characterize the antagonistic microorganism to control major paprika diseases, gray mold rot, fruit and stem rot, phytophthora blight, sclerotium rot, and wilt disease. Analysis of the fatty acid and analysis of the 16S rDNA gene sequence revealed that YKJ1 isolated in this research belongs to a group of Serratia marcescens. Specially, 16S rDNA gene sequence of YKJ1 showed 99% of sequence similarity with S. marcescens. Observation through the optical microscope revealed that YKJ1 suppressed the spore germination and the hyphal growth of pathogens. YKJ1 treatment on pathogens induced marked morphological changes like hyphal swelling and degradation of cell wall. In the case of phytophthora blight, the zoosporangium formation was restrained. S. marcescens found in this study call as S. marcescens-YKJ1 and it may be valuable as one of biological control agents against major diseases of paprika in the future even though it is require to be tested with more study on field test.

• Journal of Life Science
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• v.10 no.4
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• pp.397-402
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• 2000

Polyphosphate kinase catalyzes the formation of polyphosphate from ATP. To understand the mechanism of phosphate accumulation, the Serratia marcescens gene encoding ppk was cloned from the genomic library by the method of Southern hybridization. The hybridization positive DNA fragment region from pDH3 was subcloned into the expression vector. The ppk gene product, a polypeptide of 75 kDa, was confirmed by SDS-PAGE. Expression of the Serratia marcescens ppk is regulated by the catabolite repression system. The enzyme activity polyphosphate kinase was increased in the E. coli strain harboring plasmid pMH4 with ppk gene.