• Microbiology and Biotechnology Letters
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• v.14 no.5
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• pp.365-369
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• 1986

The activity of glucoamylase and pullulanase, properties of glucoamylase and ethanol productivities of fusants were studied. Glucoamylase and pullulanase activity of fusants were higher than parents. The optimal pH and temperature of glucoamylase of fusants were very similar to the those produced by S. diastaticus. In alcohol fermentation. fermenting ability and fermentation rate of fusants were higher and faster than either of its parental strain. The maximum of alcohol yield in 15% of liquefied potato starch was 7.8% (v/v)

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.287-290
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• 2000

To examine effects of agitation and aeration as well as adding of glucose and yeast extract on cell growth and polysaccharide production by Paecilomyces japonica, batch culture was carried out at 5L jar fermenter at $27^{\circ}C$ with the initial pH 7 for 7 days cultivation(innoculum size 2%, working volume 3L). Media compositions(g/L) were 30 glucose, 20 yeast extract, 0.5 $KH_2PO_4$, $0.1\;CuCl_2\;{\cdot}\;2H_2O$. Optimum culture conditions of agitation and aeration in batch culture were 400 rpm and 1.0 vvm, resulting in 23.1 g/L biomass and 2.5 g/L polysaccharide. Additional feeding of glucose and yeast extract with a pulse mode conferred an advantage on cell growth and polysaccharide production with showing the results of 29.2 g/L and 3.3 g/L, respectively.

• Journal of Ginseng Research
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• v.40 no.2
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• pp.121-126
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• 2016

Background: Ginsenoside F1, a pharmaceutical component of ginseng, is known to have antiaging, antioxidant, anticancer, and keratinocyte protective effects. However, the usage of ginsenoside F1 is restricted owing to the small amount found in Korean ginseng. Methods: To enhance the production of ginsenoside F1 as a 10 g unit with high specificity, yield, and purity, an enzymatic bioconversion method was developed to adopt the commercial enzyme Cellulase KN from Aspergillus niger with food grade, which has ginsenoside-transforming ability. The proposed optimum reaction conditions of Cellulase KN were pH 5.0 and $50^{\circ}C$. Results: Cellulase KN could effectively transform the ginsenosides Re and Rg1 into F1. A scaled-up biotransformation reaction was performed in a 10 L jar fermenter at pH 5.0 and $50^{\circ}C$ for 48 h with protopanaxatriol-type ginsenoside mixture (at a concentration of 10 mg/mL) from ginseng roots. Finally, 13.0 g of F1 was produced from 50 g of protopanaxatriol-type ginsenoside mixture with $91.5{\pm}1.1%$ chromatographic purity. Conclusion: The results suggest that this enzymatic method could be exploited usefully for the preparation of ginsenoside F1 to be used in cosmetic, functional food, and pharmaceutical industries.

• Korean Chemical Engineering Research
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• v.44 no.1
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• pp.52-57
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• 2006

Bacterial cellulose (BC) was produced by Gluconacetobacter hansenii PJK (KCTC 10505 BP) strains using the waste of beer fermentation broth. It contained more C and N than a basal medium with a small amount of S and more than 4％ ethanol. The amount of BC produced in a shaking culture using the waste of beer fermentation broth was nearly the same as that of a basal medium. The production of BC decreased in a shear stress field in a jar fermenter although the conversion of cellulose producing ($Cel^+$) cells to non-cellulose producing ($Cel^-$) mutants was not severe. This study showed that the waste of beer fermentation broth is an inexpensive carbon, nitrogen source with ethanol and thus a worthy substitute for the conventional medium for BC production.

• Journal of the Korea Organic Resources Recycling Association
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• v.9 no.1
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• pp.49-55
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• 2001

For the production of probiotic feed enriched with viable yeasts, aerobic liquid culture of Kluyveromyces marxianus was attempted in pulverized residual food wastes. After the preliminary shaking culture result, the liquid food wastes was added with urea($0.5g/{\ell}$), o-phosphate($0.4g/{\ell}$ ), molasses($4g/{\ell}$), and yeast extract($1g/{\ell}$), and the fermentation was carried out in 2-litre jar fermenter. In 12 hours of aerobic mixed culture with Aspersillus oryzae, viable cell count of the yeast reached to the number of $1.4{\times}10^{10}/{\ell}$ in the cultured medium.

• Microbiology and Biotechnology Letters
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• v.22 no.5
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• pp.515-521
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• 1994

A bacterial strain, which showed the high protease activity at low temperature and the high tolerance for the surfactant, was isolated from soil and identified as Xanthomonas sp. YL-37. The optimal temperature, initial pH, and cultivation time for the production of the alkaline protease by Xanthomonas sp. YL-37 were 20$\circC , 11.0, and 84 hours, respectively. In the jar fermenter culture of Xanthomonas sp. YL-37, the alkaline protease activity was about 15,000 DU/ml/-broth after cultivating for 108 hours. The optimal pH and temperature for the protease activity were 70$\circC and 11.0, respectively. The protease was relatively stable at the pH range of 7.0~12.0 and at the temperatures below 50$\circC . The protease activity at 20$\circC was about the level of 40% of its activity at 70$\circC . The enzyme was suggested as a serine protease because the enzyme activity was inhibited by phenylmethane sulfonyl fluoride, a serine modifier.

• KSBB Journal
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• v.26 no.5
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• pp.439-442
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• 2011

1,2-propanediol (1,2-PD) is a commodity chemical that is currently produced from petrochemical derivatives. Saccharomyces cerevisiae is well characterized and a successful industrial microorganism to enable the improvement of the 1,2-propanediol production by metabolic engineering. A recombinant S. cerevisiae M3G3 was used to produce 1,2-propanediol. S. cerevisiae M3G3 is the diploid strain that contains 3 copies of mgs (methylglyoxal synthase) and gldA (glycerol dehydrogenase). S. cerevisiae M3G3 was cultivated at various culture conditions by changing culture temperature, glucose concentration, and inducer concentration. Also the effect of induction time was studied to optimize the production of 1,2-propanediol. Batch and fed-batch cultivation of S. cerevisiae M3G3 was performed by using a 5 L jar fermenter. The highest concentration of 1,2-propanediol in batch cultivation was 0.86 g/L and it was further improved to 1.33 g/L in fed-batch cultivation.

• Journal of Microbiology and Biotechnology
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• v.9 no.5
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• pp.613-618
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• 1999

L-Proline-producing mutant strains were developed by exposing L-glutamic acid-producing bacteria to N-metyl-N-nitro-nitrosoguanidine and UV irradiation. A L-histidine auxotroph of Corynebacterium acetoacidophilum RYU3161(KCTC 0616BP), which was resistant to sulfaguanidine and proline analogs (DHP, AZC, TAC), was isolated. The activity of the mutant strain's $\gamma$-glutamyl kinase was 45% higher than that of the parent strain. The optimum level of L-histidine for production of L-proline was 0.16 g/l. In a 5-1 jar fermenter, the mutant strain produced L-proline at a high concentration (35 g/l) level within 48 h of cultivation.

• Journal of Microbiology
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• v.37 no.4
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• pp.200-205
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• 1999

7-Aminocephalosporanic acid (7-ACA) is the initial compound in preparation of cephalosporin antibiotics widely used in clinical treatment. Bacteria producing glutaryl 7-ACA acylase, which convert cephalosporin C to 7-ACA, has been screened in soil samples. A bacterial strain exhibiting high glutaryl 7-ACA acylase activity, designated KAC-1, was isolated and identified as a strain of Pseudomonas diminuta by characterizing its morphological and physiological properties. The screening procedures include culturing on enrichment media containing glutaric acid, glutamate, and glutaryl 7-aminocephalosporanic acid as selective carbon sources. To enhance enzyme production, optimal cultivation conditions were investigated. This strain grew optimally at pH 7 to 9 and in temperatures of 20 to 40 C, but acylase production was higher when the strain was grown at 25 C. Glutaric acid, glutamate and glucos also acted as inducers for acylase production. In a jar fermenter culture, P. diminuta KAC-1 produce acylase in a growth-associated manner. The substrate specificity of KAC-1 acylase by cell extract showed that this enzyme had specificity toward glutaryl 7-ACA, glutaryl 7-ADCA, but not cephalosporin C.

• KSBB Journal
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• v.14 no.5
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• pp.543-549
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• 1999

For development of an integrated calorimetric bio-reactor to measure the metabolic heat dissipated during cell growth, a 5 liter jar fermenter was modified to measure the pulse length of automatic temperature control signals to set heater on and off, and the to send them to computer to calculate the cumulative heat supplied. Cumulative heats for the calorimetric reactor in the absence of cell growth, were measured with varying conditions. The heat loss by the aeration was 30.9 kJ/vvm and the loss to ambient air was 10.5 kJ/L/hr/$^{\circ}C$. Cumulative heat was measued within $\pm$0.2% when testing with a small electri heater submerged in the reactor. Metabolic heat was measured to be 0.76 and 0.76 and 11.4kJ per g consumption of glucose during cultivation of S. cerevisiae and E. coli, respectively.