• Journal of Microbiology and Biotechnology
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• v.30 no.10
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• pp.1559-1566
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• 2020

Compound K (C-K) is one of the most pharmaceutically effective ginsenosides, but it is absent in natural ginseng. However, C-K can be obtained through the hydrolysis of protopanaxadiol-type ginsenosides (PPDGs) in natural ginseng. The aim of this study was to obtain the high concentration of food-available C-K using PPDGs in Korean ginseng extract by an extracellular enzyme from Aspergillus niger KACC 46495. A. niger was cultivated in the culture medium containing the inducer carboxymethyl cellulose (CMC) for 6 days. The extracellular enzyme extracted from A. niger was prepared from the culture broth by filtration, ammonium sulfate, and dialysis. The extracellular enzyme was used for C-K production using PPDGs. The glycoside-hydrolyzing pathways for converting PPDGs into C-K by the extracellular enzyme were Rb1 → Rd → F2 → C-K, Rb2 → Rd or compound O → F2 or compound Y → C-K, and Rc → Rd or compound Mc1 → F2 or compound Mc → C-K. The extracellular enzyme from A. niger at 8.0 mg/ml, which was obtained by the induction of CMC during the cultivation, converted 6.0 mg/ml (5.6 mM) PPDGs in Korean ginseng extract into 2.8 mg/ml (4.5 mM) food-available C-K in 9 h, with a productivity of 313 mg/l/h and a molar conversion of 80%. To the best of our knowledge, the productivity and concentration of C-K of the extracellular enzyme are the highest among those by crude enzymes from wild-type microorganisms.

• Journal of Life Science
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• v.16 no.1
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• pp.6-11
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• 2006

The waste water from a milk factory was investigated for possibility of use to the production of citric acid by cells of Aspegillus niger ATCC 9142. The addition of $Mn^{2+},\;Fe^{2+}\;and\;Cu^{2+}$ ions to waste increased citric acid production steadily, but addition of metal ion $Mg^{2+}$ decreased the citric acid production. The amount of produced citric acid by Aspegillus niger ATCC 9142 with addition 50 g/1 and 100 g/1 of reducing sugar in milk factory waste water were 7.2 g/1 and 16.5 g/1 respectively. Mathematical model was simulated for their predictability of cell growth, citric acid production and substrate consumption rate and coincided with experimental data.

• Korean Journal of Microbiology
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• v.9 no.4
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• pp.155-162
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• 1971

A comparison of dextrinogenic amylase activities in the Asp. niger group was made with their crude and ethanol dialized enzymes before and after heating at high temperature (60-$65^{\circ}C$). The results obtained are as follows ; 1. THe dextrinogenic amylase activity of crude enzymes of Asp. kawachii and Asp. foetidus was strong, but Asp. phoernicis, Asp. carbonarius and Asp.japonicus showed weak activity. The others showed medial grades of activity. 2. The ethanol dialized enzymes of Asp. kawachii, Asp. foetidus and Asp. japonicus was very sesitive to high temperature (60 or $65^{\circ}C$) and their enzymatic activities were diminished greatly. The others did not show diminution of enzymatic activity at 60 or 65.deg.C, but diminished greatly at 70 or $75^{\circ}C$. 3. The ethanol dialized enzymes of the Asp.niger group heated to 65.deg.C was more sensitive at pH 6.0 and 6.5 than at pH 4.5, 5.0 and 5.5. 4. Tested strains in the Asp.niger group were subdivided into 4 subgroups by their dextrinogenic amylase activities before and after heating at 60 or $65^{\circ}C$. The first group showed a medial grade of activity before heating and no diminution of their enzymatic activities after heating. Asp. niger, Asp.pulverulentus, Asp. awamori and Asp. usmii were included in this group. The second group had strong enzymatic activity before heating, but diminished greatly after heating. Asp rawachii and Asp. phoenicis were included in this group. The fourth group showed very weak enzymatic activity before heating, and was inactivated easily by heating. Asp.oryzae of the Asp. flavus group showed a very strong dextrinogenic amylase activity before heating. After the heat treatment, however, its enzymatic activity was diminished greatly.

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.648-651
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• 2001

Kinetic resolution of various racemic aromatic epoxides by newly isolated Aspergillus niger LK has been investigated, and enantioselectivity of whole-cell biocatalyst was analyzed. The epoxide hydrolase (EHase) of A. niger LK was cloned using RT-PCR. The sequence homology was compared with that of other microbial EHase and the gene for EHase was characterized at molecular level.

• Journal of Microbiology and Biotechnology
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• v.10 no.4
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• pp.518-521
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• 2000

Aspergillus niger is capable of metabolizing dimethyphthalate. The maximum weight of mycelium wa observed afterabout 6-8 dys of incubation. A TLC analysis revealed the accumulation of metabolites in the resting cell culture. Monomethylphthalate, phthalate, and protocatechuate were shown to be the intermediates by thin layer chromatographic and spectrophotometric analyses. The fungus metabolized dimethylphthalate through monomethylphthalate, phthalate, and protocatechuate as evidenced by the oxygen uptake and an enzymatic analysis. The terminal aromatic metabolite, protocatechuate, is metabolized via the ortho-cleavage pathway.

• Korean Chemical Engineering Research
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• v.50 no.5
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• pp.874-878
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• 2012

In the submerged fermentation of fungi, it was known pH had significant effect on the citric acid production. Various growth conditions were applied with different buffer on citric acid production by Aspergillus niger NRRL 567 grown on peat moss to find the optimum pH and most effective buffer solution. The initial pHs of different buffer solutions significantly influenced on the citric acid production and A. niger NRRL 567 produced citric acid more efficiently at high pHs. A phosphate buffer and a carbonate buffer with pH 8.6 and pH 10.0 were identified as suitable buffer solutions for citric acid production. The maximal citric acid production of 564.3 g/kg solid substrate was achieved employing carbonate buffer at pH 10.0.

• Microbiology and Biotechnology Letters
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• v.6 no.4
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• pp.167-171
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• 1978

When Asp. niger was shaked at 3$0^{\circ}C$ in 500 mι Erlenmeyer flask with 50 ml of the medium containing 14% of Korean local commercial glucose brand, 0.45% of peptone, and mineral, the citric acid was produced at the level of 37~43 gram per liter in 8 days, and the citric acid production at medium containing X glucose brand was better than that containing Y glucose brand. When the contaminated minerals were removed from the local glucose by Ambelite-IR 120 and peptone by potassium ferrocyanide followed by readjustment of ferric ion content in the medium to 10 mg per liter, the citric acid formation reached 53 gram per liter, a production level of three times higher than that with the original Sakaguchi's medium. The further physiological studies and the mutation of isolated Asp. niger will be needed.

• Microbiology and Biotechnology Letters
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• v.16 no.3
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• pp.193-198
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• 1988

Catalase from Aspergillus niger KUF-04 was purified by five steps including gel filtration. The overall purification gave 64-fold purified preparation, a yield of about nine percent. The enzyme showed its maximum absorption at 406 nm. The optimum pH and temperature for the enzyme activity were around pH 7.0 and 6$0^{\circ}C$, respectively. The catalase was found to be stable in the range of pH 4.0 to pH 8.3 and temperature 2$0^{\circ}C$ to 6$0^{\circ}C$. However, it lost nearly all of the activity by heating at 8$0^{\circ}C$ for 20 min. The activity was markedly inhibited by hydroxylamine, potassium cyanide and sodium azide.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.37 no.4 s.112
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• pp.1-7
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• 2005

This study was carried out to investigate the characteristics of extracellular cellulase and xylanase from Fusarium pallidoroseum and Aspergillus niger, such as enzyme activity and stability by various pH, temperature and metal ions, for application into enzymatic deinking system. The optimal temperature and pH for enzyme activity and stability of Fusarium pallidoroseum and Aspergillus niger were $50^{\circ}C$, pH 5.0 and $60^{\circ}C$, pH 9.0, respectively. Certain metal ions, calcium and cobalt, brought to elevate cellulase and xylanase activity from F. pallidoroseum and A. niger. With these results we suggest that enzymatic deinking system should be proceed at $50\~60^{\circ}C$ under their optimal pH condition.

• Journal of Microbiology and Biotechnology
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• v.25 no.1
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• pp.11-17
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• 2015

In an attempt to shift the optimal pH of the xylanase B (XynB) from Aspergillus niger towards alkalinity, target mutation sites were selected by alignment between Aspergillus niger xylanase B and other xylanases that have alkalophilic pH optima that highlight charged residues in the eight-residues-longer loop in the alkalophilic xylanase. Multiple engineered XynB mutants were created by site-directed mutagenesis with substitutions Q164K and Q164K+D117N. The variant XynB-117 had the highest optimum pH (at 5.5), which corresponded to a basic 0.5 pH unit shift when compared with the wild-type enzyme. However, the optimal pH of the XynB-164 mutation was not changed, similar to the wild type. These results suggest that the residues at positions 164 and 117 in the eight-residues-longer loop and the cleft's edge are important in determining the pH optima of XynB from Aspergillus niger.