• 미생물학회지
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• 제49권3호
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• pp.297-300
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• 2013

인삼근계(근권, 근면, 근내부) 내 EPS 생성세균의 밀도를 측정한 결과, 근권토양 내에는 $2.4{\times}10^6$ CFU/g, 근면에는 $9.1{\times}10^6$ CFU/g, 그리고 근내부에는 $2.0{\times}10^4$ CFU/g로 확인되어 다수의 EPS 생성세균이 분포하고 있음이 확인되었다. 인삼 근계로부터 EPS 생성 우수 균주 24균주를 순수분리하고 계통학적 특성을 확인한 결과, 근권(RS)으로부터 분리된 EPS 생성세균은 Arthrobacter 속 6균주, 그리고 Rhizobium 속 1균주로 나타났다. 근면(RP)으로 부터 분리된 EPS 생성세균은 Arthrobacter 속 6균주, Rhodococcus 속 1균주, Pseudomonas 속 1균주로 나타났다. 근내부(IR)에서 분리된 EPS 생성세균은 Rhizobium 속 6균주, Bacillus 속 1균주 그리고 Rhodococcus 속 1균주, Pseudomonas 속 1균주로 나타났다. 근권과 근면에서 분리된 EPS 세균 중 Arthrobacter 속에 속하는 균주는 가장 특징적인 세균으로 밝혀졌으며, Rhizobium 속은 근내부에서 분리된 가장 특징적인 EPS 생성세균으로 나타났다. EPS 생성 우수균주 Rhizobium sp. 1NP2 (KACC 17637)는 10 g/L 그리고 Arthrobacter sp. 5MP1 (KACC 17636)는 4.9 g/L의 다당을 생성하였으며, 당단백질의 구성당 성분을 확인한 결과, galactose, glucose, mannose를 구성하고 있었으며, glucosamine의 아미노당이 나타났다. 특히, glucose는 72.7-84.9%로 주요 구성당임이 확인되었다.

• 한국연초학회지
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• 제2권2호
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• pp.20-37
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• 1980

앞의 실험에서 선별된 34菌株의 니코틴 분해세균 중에서 Pseudomonas putida로 동정된 Strain NCT 27과 Arthrobacter oxydans biotype xanthum으로 동정된 strain NCT30에 대해서 이들의 니코틴 분해를 위한 최적 배지조건 및 그 밖의 생장특성을 조사하여 다음과 같은 결과를 얻었다. 니코틴 분해를 위한 최적배지조성은, $KH_2PO_4 2.Ogr$, KCI 5.Ogr, $MgSO_4\cdot7H_2O$ 20mg, $MnSO_46H_2O$ 0.2mg, $FeSO_4\cdot7H_2O$ 1.0mg, Co (Cobalt Acetate) 2.0$r$Ni (NiSO4.6H2O) 0.5${\gamma}$, yeast extract 80mg/1iter 이고 최적 초기 니코틴 농도는 Pseudomonas가 0.4%, Arthrobacter는 0.1%이었다. 그리고 최적생장온도는 두 경우 모두 3$0^{\circ}C$, pH는 7.0이며 배 양중의 pH변화는, Pseudomonas는 대수생장기에서 산성으로 기울었다가 24~40시간 후에 염기성으로 변화하는데 비해 Arthrobacter는 전 기간 중 pH가 거의 일정하게 유지되었다. 니코틴에 대한 저항성은 Arthrobacter가 0. 7%이상의 농도에서 생장이 완전히 저해됨에 비해 Pseudomonas는 1.0%까지 생장 가능하며 또한 담배추출물에서나, Nicotine 외의 다른 탄소, 질소 영양원이 포함되어 있는 배지에서도 니코틴을 효과적으로 분해할 수 있다. 그리고 최적배지조건에 서 최대 니코틴 분해도는 각각 1.22g/hr/1iter 및 0.186g/hr/1iter이었다.

• Journal of Microbiology and Biotechnology
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• 제6권6호
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• pp.402-406
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• 1996

Inulin fructotransferase (depolymerizing) (EC 2.4.1.93) was purified 34-fold from the culture broth of Arthrobacter sp. A-6 by using a combination of ammonium sulfate fractionation, DEAE-Sepharose CL-6B chromatography and Sephacryl S-200 gel filtration. The purified enzyme converts inulin into di-D-fructofuranose dianhydride III(DFA III) and small quantities of fructo-oligosaccharides. The temperature and pH optima of the enzyme were $70^{\circ}C$ and 6.0, respectively. Molecular weight of the enzyme was determined to be 49 kDa by 12$%$ SDS-polyacrylamide gel electrophoresis, and 145 kDa by Sephacryl S-200gel filtration. This indicates that the functional inulin fructotransferase of Arthrobacter sp. A-6 has a homomeric trimer structure. The enzyme had an isoelectric point of pH 4.6. The N-terminal amino acid sequence of the purified enzyme subunit was Ala-Asp-Asn-Pro-Asp-Gly(\ulcorner)-Ser-Asn-Met(or Glu)-Tyr-Asp-Val.

• 한국미생물·생명공학회지
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• 제27권6호
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• pp.471-476
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• 1999

Inulin fructotransferase(depolymerizing)(EC 2.4.1.93)(inulaseII) which converts inulin into di-D-fructofuranose-1,2':2,3'-dianhydride (DFAIII) was purified from Arthrobacter ureafaciens KCTC 3387 using column chromatography on DEAE-Toyopearl 650M and gel filtration of Sephadex G-200. The enzyme was purified 7-fold with a yield of 11% from a culture supernatant. The purified enzyme gave a single band on polyacrylamide gel electrophoresis, and the molecular weight of the enzyme was estimated to be 45,000 by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for the enzyme reaction were pH6.5~7.0 and $55{\circ}C$, respectively. The enzyme was stable within a pH range of 5.0 to 10.6 and up to $60^{\circ}C$. The Km of this enzyme for DFAIII production was 11.9mM. The enzyme was inactivated by $Hg^{2+}$ and after exhaustive digestion of inulin by this enzyme, 1-kestose and nystose were produced in addition of DFAIII.

• 한국미생물·생명공학회지
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• 제28권4호
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• pp.214-218
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• 2000

The inulinase producing microorganism was isolated from soil and tentatively identified as Arthrobacter protophormiae/ramosus. Inulinase was pruified by ethanol precipitation, DEAE-Sephadex ion exchange chromatography and Sephadex gel filtration chromatography. The molecular weight of the purified enzyme was 34 kDa. The specific activity, yield and purity were 31.5 Unit/mg, 19.5% and 18.5 fold, respectively. Optimal pH and temperature for reaction of the purified inulinase were 8.5 and $55^{\circ}C$, respectively. The enzyme was stable at pH 7.5, below$ 55^{\circ}C$, and the activity was stimulated Mg2+.

• Journal of Microbiology and Biotechnology
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• 제10권2호
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• pp.275-280
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• 2000

The inulin fructotransferse (depolymerizing) (IFTase, EC 2.4.1.93) gene of Arthrobacter sp. A-6 was cloned and expressed in Escherichia coli and Bacillus subtilis. The IFTase gene consisted of an ORF of 1.311 nucleotides encoding a polypeptide of 436 amino acids containing a signal peptide of 31 amino acids in the N-terminus. The molecular mass of the IFTase based on the nucleotide sequence was calculated to be 46.116 Da. The recombinant E. coli $DH5{\alpha}$ cells expressing the Arthrobacter sp. A-6 IFTase gene produced most of the IFTase intracelularly. In contrast, the recombinant B. subtilis DB 104 carrying the IFTas gene on a B. subtilis-E. Coli expression vector secreted the IFTase into the culture fluid efficiently.

• Korean Chemical Engineering Research
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• 제54권1호
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• pp.140-144
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• 2016

본 연구에서는 극지 연구소로부터 분양 받은 Arthrobacter sp. PAMC 27388 균주에서 생산되는 아밀라아제(amylase)를 물리적 요인(physical factor)들의 변화를 통하여 생산배지 최적화를 수행하였다. 한천 배지 상에서 lugol solution을 이용한 클린환의 확인을 통하여 아밀라아제가 생산됨을 확인하였으며, 16S rDNA를 이용하여 동정한 결과 Arthrobacter sp. 임을 확인할 수 있었다. 최적화 이전의 아밀라아제 생산량은 1.66 mU/L로 확인되었다. 최적화 결과, 2.49 mL의 접종부피, pH 6.85, 42.87 mL의 배지 부피의 조건에서 가장 많은 양의 아밀라아제가 생산될 것으로 예상되었으며, 생산량은 2.84 mU/L로 예상되었다. 확인 실험을 통하여 최적화 이전과 비교하여 생산량이 약 150% 증가한 2.50 mU/L의 아밀라아제가 생산됨을 확인할 수 있었다.

• Korean Chemical Engineering Research
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• 제52권6호
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• pp.834-839
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• 2014

본 논문에서는 반응표면분석법을 이용한 Arthrobacter sp. PAMC 25486의 carotenoids 생산 배지의 최적화를 수행하였다. Placket-Burman 방법을 이용하여 yeast extract, $MgSO_4$, dextrose가 carotenoids의 생산에 영향을 미치는 주요인자인 것을 확인하였다. 반응표면분석 방법을 이용하여 최대 carotenoids 생산 농도를 갖는 yeast extract, $MgSO_4$, dextrose의 농도를 계산한 결과 1 g/L yeast extract, 0.0879 g/L $MgSO_4$ and 1 g/L dextrose의 농도에서 최대 307 mg/L의 carotenoids 농도가 예측됐으며, 실제 배양 결과 288 mg/L carotenoids가 얻어졌다. 얻어진 농도 값은 최적화 이전의 값에 비하여 200% 이상 증가하였다. 이러한 결과로부터 미생물 배양에 의한 carotenoids 생산을 증가시키기 위한 배지최적화 방법으로서 반응표면분석법의 유용성을 확인할 수 있었다.

• KSBB Journal
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• 제31권1호
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• pp.58-65
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• 2016

In this study, Arthrobacter scleromae SYE-3, which was isolated from indigenous plant in a subtropical region, Neigeria, with plant growth promoting activity was evaluated to determine the optimal culture condition. A bacterial strain SYE-3 had the IAA productivity ($89.15{\pm}0.36mg/L$) and ACC deaminase activity ($0.20{\pm}0.06$ at 72 hours). Also, optimal culture conditions such as temperature and pH of strain SYE-3 were $20^{\circ}C$ and 10 in LB medium, respectively. Strain SYE-3 had up to 3% salt tolerance in the LB medium. Plant growth promoting ability of strain SYE-3 using yam (Dioscorea japonica Thunb.) was evaluated. As a result, strain SYE-3 had showed very powerful effect on the increase of the shoot length and root biomass of yam (190.0% and 282.41% increase for 112 days, respectively). These results indicated that Arthrobacter scleromae SYE-3 can serve as a promising microbial resource for the biofertilizers of subtropical crops.

• 한국지하수토양환경학회지:지하수토양환경
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• 제19권3호
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• pp.47-55
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• 2014

Arthrobacter chlorophenolicus A6 possesses several monooxygenases (CphC-I, CphC-II, and CphB) that can catalyze the transformation of 4-chlorophenol (4-CP) to hydroxylated intermediates in the initial steps of substrate metabolism. The corresponding genes of the monooxygenases were cloned, and the competent cells were transformed with these recombinant plasmids. Although CphC-II and CphB were expressed as insoluble forms, CphC-I was successfully expressed as a soluble form and isolated by purification. The specific activity of the purified CphC-I was analyzed by using 4-CP, 4-chlorocatechol (4-CC), and catechol (CAT) as substrates. The specific activities for 4-CP, 4-CC, and CAT were determined to be 0.312 U/mg, 0.462 U/mg, 0.246 U/mg, respectively. The results of this study indicated that CphC-I is able to catalyze the degradation of 4-CC and CAT in addition to 4-CP, which is a primary substrate. This research is expected to provide the fundamental information for the development of an eco-friendly biochemical degradation of aromatic hydrocarbons.