• Korean Journal of Plant Tissue Culture
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• v.27 no.4
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• pp.353-358
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• 2000

• Proceedings of the Korean Society of Life Science Conference
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• 2003.05a
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• pp.83-83
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• 2003

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.281.1-281
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• 1995

No Abstract, See Full Text

• Proceedings of the Korean Society of Life Science Conference
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• 2003.10a
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• pp.55-55
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• 2003

• Proceedings of the Korean Society of Life Science Conference
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• 2002.03a
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• pp.117-117
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• 2002

• Proceedings of the PSK Conference
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• 2001.04a
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• pp.214.3-215
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• 2001

• Journal of Microbiology and Biotechnology
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• v.16 no.7
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• pp.1132-1138
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• 2006

Three types of xylanases (EC 3.2.1.8) were detected in the strain Aspergillus niger A-25, one of which, designated as XynIII, also displayed ${\beta}-(l,3-1,4)-glucanase$ (EC 3.2.1.73) activity, as determined by a zymogram analysis. XynIII was purified by ultrafiltration and ion-exchange chromatography methods. Its apparent molecular weight was about 27.9 kDa, as estimated by SDS-PAGE. The purified XynIII could hydrolyze birchwood xylan, oat spelt xylan, lichenin, and barley ${\beta}-glucan$, but not CMC, avicel cellulose, or soluble starch under the assay conditions in this study. The xylanase and ${\beta}-(l,3-1,4)-glucanase$ activities of XynIII both had a similar optimal pH and pH stability, as well as a similar optimal temperature and temperature stability. Moreover, the effects of metal ions on the two enzymatic activities were also similar. The overall hydrolytic rates of XynIII in different mixtures of xylan and lichenin coincided with those calculated using the Michaelis-Menten model when assuming the two substrates were competing for the same active site in the enzyme. Accordingly, the results indicated that XynIII is a novel bifunctional enzyme and its xylanase and ${\beta}-(l,3-1,4)-glucanase$ activities are catalyzed by the same active center.

• Journal of Microbiology and Biotechnology
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• v.21 no.12
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• pp.1312-1321
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• 2011

Enzyme extracts of cellulase [filter paper cellulase (FPase) and carboxymethyl cellulase (CMCase)], chitinase, and chitosanase produced by Aspergillus niger NRRL-567 were evaluated. The interactive effects of initial moisture and different inducers for FP cellulase and CMCase production were optimized using response surface methodology. Higher enzyme activities [FPase $79.24{\pm}4.22$ IU/gram fermented substrate (gfs) and CMCase $124.04{\pm}7.78$ IU/gfs] were achieved after 48 h fermentation in solid-state medium containing apple pomace supplemented with rice husk [1% (w/w)] under optimized conditions [pH 4.5, moisture 55% (v/w), and inducers veratryl alcohol (2 mM/kg), copper sulfate (1.5 mM/kg), and lactose 2% (w/w)] (p<0.05). Koji fermentation in trays was carried out and higher enzyme activities (FPase $96.67{\pm}4.18$ IU/gfs and CMCase $146.50{\pm}11.92$ IU/gfs) were achieved. The nonspecific chitinase and chitosanase activities of cellulase enzyme extract were analyzed using chitin and chitosan substrates with different physicochemical characteristics, such as degree of deacetylation, molecular weight, and viscosity. Higher chitinase and chitosanase activities of $70.28{\pm}3.34$ IU/gfs and $60.18{\pm}3.82$ to $64.20{\pm}4.12$ IU/gfs, respectively, were achieved. Moreover, the enzyme was stable and retained 92-94% activity even after one month. Cellulase enzyme extract obtained from A. niger with chitinolytic and chitosanolytic activities could be potentially used for making low-molecular-weight chitin and chitosan oligomers, having promising applications in biomedicine, pharmaceuticals, food, and agricultural industries, and in biocontrol formulations.

• The Korean Journal of Mycology
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• v.20 no.3
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• pp.252-258
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• 1992

Thirty three species and two species varieties belonging to 14 genera of fungi were collected from 20 cowpea cultivars on glucose Czapek's agar (11 genera and 25 species+1 var.) and glucose-Czapek's agar supplemented with 10% NaCl (7 genera and 18 species+2 var.) at $28{\pm}2^{\circ}C$. The total count of fungi were 6716 colonies/g in all cowpea cultivars. On glucose-Czapek's agar and identified; Aspergillus flavus, A. niger, A. sydowii, A. flavus var. columnaris, A. terreus, Penicillium chrysogenum, Emericella nidutans and Rhizopus stolonifer. The total count of halotolerant or halophilic fungi was 3515 colonies/g on 10% NaCl-glueose-Czapek's agar and identified; the most common species were: A. flavus, A. sydowii, A. tamarii A. flavipes, A. niger, A. flavus var. columnaris, A. ochraceus, A. oryzae and P. chrvsogenusm. Thin layer chrormatographic analysis of chloroform extracts of the different seed samples revealed that four cultivars were naturally contaminated with aflatoxins $B_1,\;B_2,\;G_1$ and $G_2$, $(45-112\;{\mu}g/kg)$.

• Korean Chemical Engineering Research
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• v.52 no.3
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• pp.302-306
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• 2014

The present study was carried out to optimize fermentation parameters for the production of cellulolytic enzymes through solid substrate fermentation of Trichoderma reesei and Aspergillus niger grown on wheat straw. A sequential optimization based on one-factor-at-a-time method was applied to optimize fermentation parameters including temperature, pH, moisture content and particle size. The results of optimization indicated that $40^{\circ}C$, pH 7, moisture content 75% and particle size between 0.25~0.5 mm were found to be the optimum condition at 96 hr fermentation. Under the optimal condition, co-culture of T. reesei and A. niger produced cellulase activities of 10.3 IU, endoglucanase activity of 100.3 IU, ${\beta}$-glucosidase activity of 22.9 IU and xylanase activity of 2261.7 IU/g dry material were obtained. Cellulolytic enzyme production with optimization showed about 72.6, 48.8, 55.2 and 51.9% increase compared to those obtained from control experiment, respectively.