• 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.

• 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.

• Korean Journal of Food Science and Technology
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• v.33 no.3
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• pp.361-365
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• 2001

The effects of purine catabolites in growth media on the biosynthesis of Serratia marcescens and Lactobacillus plantarum purine nucleoside phosphorylase (PNP) activity were examined. Serratia PNP activity was decreased approximately by 30% in the presence of high concentrations of inosine $(5{\sim}15\;mM)$, but was not affected at low concentrations of inosine $(0.1{\sim}1\;mM)$. However, Lactobacillus PNP activity was increased above 60% by inosine among the range from 5 to 15 mM. Serratia PNP activity was decreased approximately by 45% in the presence of high concentrations of hypoxanthine $(5{\sim}15\;mM)$, but was not affected at low concentrations of hypoxanthine $(0.1{\sim}0.5\;mM)$. Lactobacillus PNP activity was increased approximately by 20% in the presence of low concentrations of hypoxanthine $(0.1{\sim}0.5\;mM)$, and increased approximately by $50{\sim}65%$ in the presence of concentrations of hypoxanthine $(1{\sim}15\;mM)$. Serratia and Lactobacillus PNP activity was increased 20% by low concentrations of uric acid (0.5 mM), but was decreased $40{\sim}80%$ at high concentrations of same purine catabolite $(10{\sim}15\;mM)$. These data suggest that purine nucleoside phosphorylase in Serratia marcescens ATCC 25419 and Lactobacillus plantarum ATCC 8014 is positively regulated by a low uric acid concentration, and then may play a regulatory role in a purine nucleotide catabolic pathway.

• Microbiology and Biotechnology Letters
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• v.19 no.5
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• pp.450-455
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• 1991

A protease hyperproducer, ampicillin resistant mutant, Serratia sp. SMNT-1 was selected from Serratia marcescens ATCC 21074 by mutagenesis. The protease productivity of this strain was about 11 times as much as that of the parental strain. The enzyme showed maximal activity at pH 9.0 and $40^{\circ}C$ and was stable over the pH range from 6.0 to 10.0 at $4^{\circ}C$, whereas it was unstable at $37^{\circ}C$ in alkaline condition. the enzyme was inactivated by heating at $60^{\circ}C$ for 10 min. The enzyme was inactivated by EDTA and reactivated by $Zn^{2+}, Co^{2+},\; and \; Mn^{2+}$, but the proteoiytic activity of the enzyme was not affected by DFP. From the above results, the protease produced by Serratia sp. SMNT-1 was classified as a metalloprotese.

• 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.

• 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.

• Applied Biological Chemistry
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• v.42 no.3
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• pp.181-187
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• 1999

For the selection of an effective antagonistic biocontrol agent, we have isolated an antagonistic bacterium which produced extracellular chitinase, from a local soil of Kyongju, Korea. The selected strain was identified as Serratia proteamaculans 3095. The chitinase produced from Serratia sp. 3095 showed antifungal activity which can attack the hypha surface of Fusarium oxysporum and F. solani. The carbon and nitrogen sources for chitinase production were 0.15% colloidal chitin and 0.1% ammonium sulfate, respectively. Glucose in the chitinase production medium might inhibit the production of chitinase by feed back repression. The antagonistic Serratia sp. 3095 also showed a powerful biocontrol activity against F. oxysporum through in vitro test and in vivo pot test.

• 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.

• 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.

• 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.