• Journal of Applied Biological Chemistry
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• v.43 no.4
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• pp.264-268
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• 2000

High activity of acidic ethylacetate extract from the culture supernatant of ginseng growth-promoting bacterium Pseudomonas fluorescens KGPP 207 and its fractions were demonstrated through wheat coleoptile bioassay. The following auxins and auxin-like compounds were identified in these fractions by combined gas chromatography-mass spectrometry: indole-3-acetic acid, indole-3-acetic acid methyl and ethyl ester, indole-3-butyric acid, indole-3-lactic acid and its methyl ester, indole-3-propionic acid, indole-3-pyruvic acid, p-hydroxyphenyl acetic acid, p-hydroxyphenyl acetic acid methyl and ethyl ester, phenyl acetic acid and its methyl ester. The bacterium KGPP 207 belongs to the strain of P. fluorescens which produces plant growth regulators and its beneficial effect on the ginseng growth may be due to the formation of the identified compounds.

• Archives of Pharmacal Research
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• v.15 no.2
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• pp.138-141
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• 1992

The new N-aryl-benz[f]-indole-4, 9-dione derivatives were synthesized via in tramolecular cyclization when triethylamine was employed as a base for the reaction of 2-chloro-3-$(\alpha$-cyano-$\alpha$-ethoxycarbonyl-methyl)-1, 4-naphthoquinone and arylamines.

• Applied Chemistry for Engineering
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• v.21 no.2
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• pp.238-241
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• 2010

The purification of indole from 54.3wt% indole fraction (temperature range of distillate: $250{\sim}255^{\circ}C$) recovered by extraction-distillation combination of coal tar fraction (temperature range of distillate: $240{\sim}265^{\circ}C$) was examined by solute crystallization. The feed consists of eight components such as quinoline, iso-quinoline, indole, quinaldine, 1-methylnaphthalene, 2-methylnaphthalene, biphenyl and phenyl ether. Hexane and an aqueous solution of methanol (50 : 50 vol%) were used as the crystallization solvent and the coolant, respectively. A batch stirred tank of glass material was used as a crystallization apparatus. By increasing the operation temperature and the volume ratio of solvent to feed at initial, the purity of indole increas ed, but yields of indole showed a decreasing tendency. Solute crystallization method using hexane as a solvent was excellent because the purity of 99.3 wt% indole was recovered at the yield of 50% without washing operation.

• Journal of Korean Society of Environmental Engineers
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• v.30 no.3
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• pp.286-292
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• 2008

This study was conducted to analyze and determine the formation potential of chlorination DBPs from seven urinary compounds with or without Br$^-$. Three of seven components were kynurenine, indole and uracil that were relatively shown high the formation potential of chlorination DBPs concentrations. The reported results of THMs/DOC with or without Br$^-$ in kynurenine showed that THMs/DOC was detected 86.9 $\mu$g/mg when Br$^-$ was not added, and THMs/DOC was detected 100.8 $\mu$g/mg when Br$^-$ was presented. In indole, THMs/DOC was increased from 6.58 $\mu$g/mg to 31.4 $\mu$g/mg when Br$^-$ was added. Moreover, among them, the highest, second-highest and third-highest HAAs/DOC were shown in kynurenine, uracil and indole respectively. Specially, HAAs/DOC was significantly deceased in kynurenine and indole when Br$^-$ was presented. This was a totally different phenomenon for THMs/DOC. TCAA was dominated in HAAs for kynurenine and indole, and DCAA was also dominated in HAAs for uracil. The highest formation of HANs/DOC was shown in kynurenine whether or not Br$^-$ presented, and DCAN was predominant in HANs. HANs was not formed by chlorination in uracil. In addition, the formation of CH/DOC was relatively low in kynurenine and indole. The formation of CH/DOC was specially high(1,270 $\mu$g/mg) in uracil when Br$^-$ was not added. The formation of CH/DOC was 1,027 $\mu$g/mg in uracil when Br$^-$ was added. The formations of THMs and HAAs were also investigated in kynurenine, indole and uracil when Br$^-$ was presented or not. The formation of THMs/DOC was higher in kynurenine and indole when Br$^-$ was presented. The formation of HAAs/DOC was reduced in kynurenine when Br$^-$ was added. The result could be attributed to higher formation of THMs/DOC in kynurenine when Br$^-$ was added. The formation of HAAs/DOC was also reduced in indole when Br$^-$ was added. To the contrary, this result was not attributed to higher formation of THMs/DOC in indole when Br$^-$ was added.

• Microbiology and Biotechnology Letters
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• v.37 no.3
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• pp.197-203
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• 2009

An indole oxygenase originated from Rhodococcus sp. RHA1 was cloned into the expression vector, pTrc99A, in Escherichia coli, and designated pTCAN1. The pTCAN2 was constructed from pTCAN1 by the deletion of $lacI^q$ for the constitutive expression of indole oxygenase without adding IPTG in the medium. The complete open reading frame of indole oxygenase was 1,224 bp long, which encodes a protein of 407amino acids. Crude extracts of E. coli $DH5{\alpha}$/pTCAN1 and pTCAN2, respectively, were prepared and subjected to SDS-PAGE analysis. A band corresponding to molecular mass of about 43 kDa was appeared and this result correlated with the predicted molecular mass of cloned indole oxygenase. The E. coli harboring pTCAN1 and pTCAN2, respectively, showed blue color colony in LB plate. The pigment showing blue color was prepared from E. coli $DH5{\alpha}$/pTCAN2, and identified as indigo by experiments using spectrophotometer, HPLC, and TLC. The indigo-forming activity of indole oxygenases from the whole cell of E. coli $DH5{\alpha}/pTCAN1$ cultured at LB medium added 1mM of IPTG and that of E. coli/pTCAN2 showed about 1.75nmol/min/mg DCW (dry cell weight) and 3.85 nmol/min/mg DCW, respectively. Also, the E. coli $DH5{\alpha}$/pTCAN2 produced about $236{\mu}M$ of indigo after 48 hours incubation in TB medium supplemented with 2.5 mM of tryptophan.

• YAKHAK HOEJI
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• v.35 no.3
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• pp.231-235
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• 1991

Compounds of the structure of -4,9-dione are known to have an antibacterial activity against Gram-positive bacteria. New kinds of 2-amino-$\alpha$-cyano-$\alpha$-ethoxycarbonyl-niethyl)-1,4-naphthoquino ne was reacted with some alkylamines(methylamine, ethylamine, ethanolarnine, isopropylamine, cyclohexylamine, benzylamine) to yield 2-amino-3-ethoxycarbonyl-N-alkyl-4,9-diones.

• Applied Chemistry for Engineering
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• v.18 no.2
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• pp.168-172
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• 2007

The separation of indole from a model mixture comprising four kinds of nitrogen heterocyclic compounds [indole (In), quinoline (Q), iso-quinoline (iQ), quinaldine (Qu)], three kinds of bicyclic aromatic compounds [1-methylnaphthalene (1MN), 2-methylnaphthalene (2MN), dimethylnaphthalene (DMN)], biphenyl (Bp) and phenyl ether (Pe) was examined by batch cocurrent 4 stages equilibrium extraction. The model mixture used as a raw material in this work was prepared according to the components and compositions contained in coal tar fraction (the temperature ranges of fraction: $240{\sim}265^{\circ}C$). An aqueous solution of formamide was used as a solvent. Indole was recovered more than 99% through 4 stages of the equilibrium extraction. The range of selectivity of indole in reference to DMN obtained through the 5 stages equilibrium extraction was found to be 63~118. The process for separation and recovery of indole contained in coal tar was studied by using the experimental results obtained from this work and the previous work.

• Journal of Microbiology and Biotechnology
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• v.23 no.12
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• pp.1726-1736
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• 2013

Biosynthesis of indole-3-acetic acid (IAA) via the indole-3-pyruvic acid pathway involves three kinds of enzymes; aminotransferase encoded by aspC, indole-3-pyruvic acid decarboxylase encoded by ipdC, and indole-3-acetic acid dehydrogenase encoded by iad1. The ipdC from Enterobacter cloacae ATCC 13047, aspC from Escherichia coli, and iad1 from Ustilago maydis were cloned and expressed under the control of the tac and sod promoters in E. coli. According to SDS-PAGE and enzyme activity, IpdC and Iad1 showed good expression under the control of $P_{tac}$, whereas AspC was efficiently expressed by $P_{sod}$ originating from Corynebacterium glutamicum. The activities of IpdC, AspC, and Iad1 from the crude extracts of recombinant E. coli Top 10 were 215.6, 5.7, and 272.1 nmol/min/mg-protein, respectively. The recombinant E. coli $DH5{\alpha}$ expressing IpdC, AspC, and Iad1 produced about 1.1 g/l of IAA and 0.13 g/l of tryptophol (TOL) after 48 h of cultivation in LB medium with 2 g/l tryptophan. To improve IAA production, a tnaA gene mediating indole formation from tryptophan was deleted. As a result, E. coli IAA68 with expression of the three genes produced 1.8 g/l of IAA, which is a 1.6-fold increase compared with wild-type $DH5{\alpha}$ harboring the same plasmids. Moreover, the complete conversion of tryptophan to IAA was achieved by E. coli IAA68. Finally, E. coli IAA68 produced 3.0 g/l of IAA after 24 h cultivation in LB medium supplemented with 4 g/l of tryptophan.

• Journal of Microbiology and Biotechnology
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• v.18 no.7
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• pp.1235-1244
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• 2008

Indole-3-acetic acid (IAA) is produced commonly by plants and many bacteria, however, little is known about the genetic basis involving the key enzymes of IAA biosynthetic pathways from Bacillus spp. IAA intermediates from the Gram-positive spore-forming bacterium Paenibacillus polymyxa E681 were investigated, which showed the existence of only an indole-3-pyruvic acid (IPA) pathway for IAA biosynthesis from the bacterium. Four open reading frames (ORFs) encoding indole-3-pyruvate decarboxylase-like proteins and putative indole-3-pyruvate decarboxylase (IPDC), a key enzyme in the IPA synthetic pathway, were found on the genome sequence database of P. polymyxa and cloned in Escherichia coli DH5$\alpha$. One of the ORFs, PP2_01257, was assigned as probable indole-3-pyruvate decarboxylase. The ORF consisted of 1,743 nucleotides encoding 581 amino acids with a deduced molecular mass of 63,380 Da. Alignment studies of the deduced amino acid sequence of the ORF with known IPDC sequences revealed conservation of several amino acids in PP2_01257, essential for substrate and cofactor binding. Recombinant protein, gene product of the ORF PP2_01257 from P. polymyxa E681, was expressed in E. coli BL21 (DE3) as a glutathione S-transferase (GST)-fusion protein and purified to homogeneity using affinity chromatography. The molecular mass of the purified enzyme showed about 63 kDa, corresponding closely to the expected molecular mass of IPDC. The indole-3-pyruvate decarboxylase activity of the recombinant protein, detected by HPLC, using IPA substrate in the enzyme reaction confirmed the identity and functionality of the enzyme IPDC from the E681 strain.

• YAKHAK HOEJI
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• v.34 no.1
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• pp.15-21
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• 1990

-4,9-dione derivatives were prepared from $2-chloro-3-({\alpha}-accetyl-{\alpha}-ethoxycarbonyl-methyl)-1,4-naphthoquinone$ and 2-chloro-3-N-phenylamino-1,4-naphthoquinone. $2-Chloro-3-({\alpha}-acetyl-{\alpha}-ethoxycarbonyl-methyl)-1,4-naphthoquinone$ was reacted with amines to give $2-amino-3-({\alpha}-acetyl-{\alpha}-ethoxycarbonyl-methyl)-1,4-naphthoquinone$ derivatives. Subsequent treatment of $2-amino-3-({\alpha}-acetyl-{\alpha}-ethoxycarbonyl-methyl)-1,4-naphthoquinone$ with sodium ethoxide gave -4,9-dione derivatives. When 2-chloro-3-N-phenylamino-1,4-naphthoquinone reacted with sodium ${\alpha}-cyano$ ethyl acetate, 2-amino-3-ethoxycarbonyl-N-phenyl--4,9-dione was obtained. However, with sodium diethyl malonate, not -4,9-dione but 2-chloro-3-bis-(methoxycarbonyl)-methyl-2H-3-N-phenylamino-1,4-naphthoquinone was obtained.