• Journal of Microbiology and Biotechnology
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• v.21 no.1
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• pp.71-80
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• 2011

Four diazinon-degrading bacteria were isolated from agricultural soil by using an enrichment technique. The biochemical analysis and molecular method including RFLP indicated that these isolates were identical, and one strain designated DI101 was selected for further study. Phylogenetic analysis based on 16S rDNA sequencing indicated that the strain DI101 clearly belongs to the Serratia marcescens group. The ability of the strain to utilize diazinon as a source of carbon and phosphorus was investigated under different culture conditions. The DI101 strain was able to completely degrade 50 mg/l diazinon in MSM within 11 days with a degradation rate of 0.226 $day^{-1}$. The inoculation of sterilized soil treated with 100 mg/kg of diazinon with $10^6$ CFU/g DI101 resulted in a faster degradation rate than was recorded in non-sterilized soil. The diazinon degradation rate by DI101 was efficient at temperatures from 25 to $30^{\circ}C$ and at pHs from 7.0 to 8.0. The degradation rate of diazinon was not affected by the absence of a phosphorus supplement, and addition of other carbon sources (glucose or succinate) resulted in the slowing down of the degradation rate. The maximum degradation rate ($V_{max}$) of diazinon was 0.292 $day^{-1}$ and its saturation constant ($K_s$) was 11 mg/l, as determined by a Michaelis-Menten curve. The strain was able to degrade diethylthiophosphate-containing organophosphates such as chlorpyrifos, coumaphos, parathion, and isazofos when provided as a source of carbon and phosphorus, but not ethoprophos, cadusafos, and fenamiphos. These results propose useful information for the potential application of the DI101 strain in bioremediation of pesticide-contaminated environments.

• Microbiology and Biotechnology Letters
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• v.47 no.2
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• pp.259-268
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• 2019

In this study, the extracellular metalloprotease from Serratia marcescens PPB-26 was purified to homogeneity via ethanol fractionation and DEAE-cellulose column chromatography. Thus, a 3.8-fold purification was achieved with a 20% yield and specific activity of 76.2 U/mg. The purified protease was a 50-kDa monomer whose optimum pH and temperature for activity were 7.5 and $30^{\circ}C$ respectively; however, it was found to remain active in the 5-9 pH range and up to $40^{\circ}C$ for 6 h. The protease had a half-life of 15 days at $4^{\circ}C$, an optimum reaction time of 10 min, and an optimum substrate (casein) concentration of 0.25%. Furthermore, the Michaelis constant ($K_m$) and reaction velocity ($V_{max}$) of the protease were calculated to be 0.28% and $111.11{\mu}moles/(min{\cdot}mg)^{-1}$, respectively. The protease was stable when subjected to metal ions (2 mM), showing increased activity with most (especially $CoCl_2$ and $MgSO_4$ (30.54% increase)). It was also stable when exposed to oxidizing agents, bleaching agents, and detergents (5% v/v for 60 min). It retained 93% of its activity in non-ionic detergents (Tween-20, Tween-80, and Triton X-100). Moreover, wash performance analysis in commercial detergents (Ariel and Tide) showed that not only was the protease capable of protein stain removal, but also reduced cleaning time by 80% when added to detergents. Thus, the Serratia marcescens PPB-26 metalloprotease appears to be a promising new candidate as a laundry additive in the detergent industry.

• Korean Journal of Microbiology
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• v.18 no.1
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• pp.15-19
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• 1980

In order to study on the pigment and protease of Serratia marcescens, the correlation between protease activity and pigment formation was investigated. The results are as follows ; (1) The protease activity exhibitied two pH optima 6.0 and 7.5, respectively. (2) The optimal temeprature of proteolytic activity was $45^{\circ}C$. With these-results, it is suggested that the proteolytic enzymes of Serratia masrecescens is stable at neutral pH range and more active at the high temeprature than lthat of otehr proteolytic enzymes.

• Research in Plant Disease
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• v.9 no.4
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• pp.229-236
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• 2003

The 1080 epiphytic bacteria obtained from 370 samples of pome and stone fruits including apple, pear, peach, grape, apricot and Chinese quince were screened for antagonistic activity against postharvest pathogens, Penicillium expansum, Alternaria alternata and Botrytis cinerea. Among tested antagonistic bacteria, eight bacterial isolates inhibited mycelial growth of the postharvest pathogens and were identified as Bacillus amyloliquefaciens (three strains), B. megaterium, B. subtilis var. gladioli, B. licheniformis, B. pumilus and Serratia marcescens based on biochemical characteristics and utility of carbon and nitrogen compounds (Biolog system). Eight carbohydrates were evaluated for their effect on mycelial growth and germination of the postharvest pathogen, P. expansum to select nutrients for enhancing bio-control efficacy. The growth of four selected antagonists, B. amyloliquefaciens P43-2, B. amyloliquefaciens A71-2, B. licheniformis P94-1, and S. marcescens P76-9 were also tested. As a result, 1% glucose (w/v) strongly stimulated growth of the antagonists, suppressed mycelial growth of the postharvest pathogen, and had a little comparatively stimulatory effect on germination of the the postharvest pathogen. It was confirmed that the addition of 1% glucose (w/v) greatly enhanced biocontrol effect of B. amyloliquefaciens P43-2, B. licheniformis P94-1, and S. marcescens P76-9. Application of B. amyloliquefaciens P43-2, B. licheniformis P94-1, and S. marcescens P76-9 with the addition of 1% glucose (w/v) increased the control efficacy up to 48%, 46%, 14% compared with those of the antagonists without glucose, respectively. When the antagonists were applied to control postharvest disease caused by P. expansum in apple wounds, the population of B. amyloliquefaciens P43-2 and B. licheniformis P94-1 increased until 4 days after inoculation (DAI) of the antagonists and then decreased from 10 DAI. Meanwhile the population of S. marcescens P76-9 decreased at early stage (4 DAI), but increased from 7 DAI, and finally maintained constantly until 10 DAI in apple wounds.

• Korean Journal of Microbiology
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• v.10 no.2
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• pp.87-92
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• 1972

In order to study on the pigment and protease of Serratia marcescens, the correlation between protease activity and pigment formation was investigated. The results are as follows ; 1) The protease activity exhibitied two pH optima 6.0 and 7.5, respectively. 2) The optimal temeprature of proteolytic activity was 45.deg.C. With these-results, it is suggested that the proteolytic enzymes of Serratia masrecescens is stable at neutral pH range and more active at the high temeprature than lthat of otehr proteolytic enzymes.

• Journal of Microbiology and Biotechnology
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• v.29 no.4
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• pp.596-606
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• 2019

N-acyl-homoserine lactone quorum sensing (AHL-QS) has been shown to regulate many physiological behaviors in Serratia marcescens MG1. In the current study, the effects of AHL-QS on the biosynthesis of acid and neutral products by S. marcescens MG1 and its isogenic ${\Delta}swrI$ with or without supplementing exogenous N-hexanoyl-L-homoserine lactone ($C_6-HSL$) were systematically investigated. The results showed that swrI disruption resulted in rapid pH drops from 7.0 to 4.8, which could be restored to wild type by supplementing $C_6-HSL$. Furthermore, fermentation product analysis indicated that ${\Delta}swrI$ could lead to obvious accumulation for acidogenesis products such as lactic acid and succinic acid, especially excess acetic acid (2.27 g/l) produced at the early stage of fermentation, whereas solventogenesis products by ${\Delta}swrI$ appeared to noticeably decrease by an approximate 30% for acetoin during 32-48 h and by an approximate 20% for 2,3-butanediol during 24-40 h, when compared to those by wild type. Interestingly, the excess acetic acid produced could be removed in an AHL-QS-independent manner. Subsequently, quantitative real-time PCR was used to determine the mRNA expression levels of genes responsible for acidogenesis and solventogenesis and showed consistent results with those of product synthesis. Finally, by close examination of promoter regions of the analyzed genes, four putative luxI box-like motifs were found upstream of genes encoding acetyl-CoA synthase, lactate dehydrogenase, ${\alpha}$-acetolactate decarboxylase, and Lys-like regulator. The information from this study provides a novel insight into the roles played by AHL-QS in switching from acidogenesis to solventogenesis in S. marcescens MG1.

• Journal of Life Science
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• v.34 no.6
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• pp.377-384
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• 2024

Prodigiosin is a red pigment characterized by a common pyrrolylpyrromethane skeleton. It is produced by Serratia marcescens, Vibrio psychroerythrus, Hahella chejuensis, etc. Prodigiosin has been reported to possess anticancer, immunosuppressant, antifungal antimalarial, and algicidal activities. However, despite prodigiosin's diverse range of activities, its production rate is significantly low and biosynthesis conditions are difficult. Consequently, the selling price is high, and its usability is limited. This study aimed to increase the efficiency of prodigiosin production according to the culture conditions of Serratia. In this study, a bacterial strain PDGS¹²⁰⁹¹⁵ producing prodigiosin was isolated from lightly contaminated stream water in Busan and identified as a strain of Serratia sp. based on 16S rDNA gene sequence analysis and physiological characteristics. The reddish pigment from PDGS¹²⁰⁹¹⁵ was directly extracted using acidified ethanol, and a characterization analysis confirmed that it was a prodigiosin compound. The optimal conditions for pigment production were 25℃, pH 7, and 0% NaCl concentration for a duration of 14 hr. Furthermore, by treating carbon and nitrogen sources, such as fructose and beef extract, respectively, prodigiosin production increased approximately six-fold and four-fold. Among the minerals tested, 0.1% KCl was found to be the most effective for prodigiosin production. Moreover, casein was identified as the most suitable source for prodigiosin production.

• Korean Journal of Microbiology
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• v.32 no.2
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• pp.147-154
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• 1994

Nuclease was secreted to the environmental media from the Escherichia coli JM107 tranformant harboring the extracellular nuclease gene of Serratia marcescens in the plasmid of pNUC4. Under the growth conditions, the amount of secreted enzyme was increased in parallel with bacterial growth conditions, the amount of secreted enzyme was increased in parallel with bacterial growth. The enzyme was purified using chromatofraphic procedures of Matrex green gel and heparin agarose affinity gel, resulted in 50-fold purification with 15% recovery of the enzyme. The apparent molecular weight of the enzyme was estimated to be 29Kda by sodium dodecylsulfate denaturing gel electrophoresis. Using the purified enzyme, polyclonal antibody was obtained from the rabbit. The specificity of the antibody was confirmed by immunoblotting and immunoprecipitaion. For the investigation of cellular distribution of the enzyme, cells were fractionated into three fractions; cytoplasm, periplasm and extracellular fluid. While more than 80% of the enzymatic activity was detected in the extracellular fluid and periplasm, a little was found in the cytoplasm, indicating that the enzyme was likely to be immediately exported to the membrane for excretion after biosynthesis. These results were confirmed again by immunocytochemistry technique using the antibody.

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2001.11a
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• pp.122-122
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• 2001

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.600-601
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• 2005