• Korean Journal of Microbiology
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• v.54 no.3
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• pp.244-253
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• 2018

This study was carried out to evaluate effects of antimicrobial substances produced by isolated soil bacteria. Among two thousands of bacterial isolates Paenibacillus elgii DS381 exhibited high antimicrobial activities against several microbial residents on human skin and pathogenic bacteria. DS381 showed 15.3~26.0 mm inhibition zone diameter against all target bacteria and yeast in agar well diffusion test. Antimicrobial peptide produced by DS381 indicated low minimum inhibitory concentration (0.039-5.000 mg/ml). DS381 produced biosurfactant such as lipopeptide, and surface tension of culture supernatant of DS381 reduced from 60.0 to 40.3 mN/m. DS381 also showed $1.56{\pm}0.13U/ml$ of chitinase activity. These results suggest that Paenibacillus elgii DS381 may be utilized as an efficient biocontrol agent against some important human skin microbes and pathogenic bacteria.

• Korean Journal of Food Science and Technology
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• v.34 no.3
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• pp.444-448
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• 2002

The waste brine gained from successively reused brine during kimchi manufacturing can cause serious water pollution. We investigated the filtration effects on the physicochemical characteristics and microbial counts of the waste brine. Chinese cabbage was salted for five times successively, and the waste brines were filtered through sand and active carbon column. While original values of salinity and soluble solid contents of waste brine were 15.4% and $18.0^{\circ}$Brix$, respectively, we observed decrease of them to 0.1% and $0.0^{\circ}$Brix$, respectively, after filtration of the waste brine through sand followed by active carbon column. The filtration also recover pH value of the waste brine to its original value, which was decreased by successive salting from 8.3 to 6.0. We also observed that COD of waste brine increased to 63.2 ppm after five times of salting but decreased to 5.1 ppm after active carbon filtration. Total viable count was also increased with successive 5 steps of salting and was not detected after active carbon-filtration.

• Korean Journal of Microbiology
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• v.27 no.3
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• pp.216-220
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• 1989

As the bsic study about protoplast fusion of amylolytic fungus Aspergillus oryze and nonamyloytic sugar fermenter, Saccaromyces cerevsisae, the intraspecific protoplast fusion of A. oryzae was carried out and the properties of the obtained fusants were investigated. For protoplast fomation from mycellia of auxotrophs, Novozyme 234 as lytic enzyme was the most effective and optimal pH was determined to be pH 5.5-6.0. When the two types of protoplasts were treated with a fusogen including 30% PEG4000, they fused effectively and most of fusants were heterokaryons. Protoplasts aggregated with 30% PEG4000 after fusion treatment were observed by the microscope. Protoplast regeneration frequency was 1.46 to 13.8% and complementation frequency of fusion was 0.12 to 0.16. Fusant strains had a 1.5-fold DNA content compared to that of parent strain. And amylase activity was intermediate between those of parent strains.

• Korean Journal of Microbiology
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• v.47 no.2
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• pp.143-150
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• 2011

Lactic fermented dongchimi naengmyeun broth which has enhanced antioxidative activity was developed. During lactic fermentation of dongchimi naengmyeun broth at $25^{\circ}C$, changes of total lactic acid bacteria, pH, acidity, soluble phenolics, and anthocyanins were investigated. After 72 h of fermentation, the stronger antioxidant activities were observed in dongchimi naengmyeun broth supplemented with purple sweet potato than those of control dongchimi naengmyeun broth which showing 96.80% in DPPH radical scavenging activity, 100.82% in $ABTs^{+{\cdot}}$ scavenging activity, 7.77 in reducing power, and 6.89 in ferric reducing/antioxidant power, respectively. These high antioxidant activities related with higher contents of soluble phenolics and anthocyanins in dongchimi naengmyeun broth supplemented with purple sweet potato. The results suggest that the making of functional dongchimi naengmyeun broth by using high soluble phenolics and anthocyanins supplements such as purple sweet potato powder was possible.

• Microbiology and Biotechnology Letters
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• v.8 no.4
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• pp.229-235
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• 1980

Pectin transeliminase (PTE) was produced by Saccharomyces cerevisiae, Schizosaccharomyces pombe 4683, and Aspergillus niger in the media containing 2% pectin and examined for its characteristics. The Production of the enzyme was higher by Asp. niger than by the two yeast strains, showing that the PTE activity was proportional to reducing power. The enzyme was proved to reduce pectin and produce 4, 5- unsaturated galacturonic acid. The optimum activity of the PTE was found to be at pH 6.0 and $50^{\circ}C$. The activities of these enzyme were stable below $50^{\circ}C$ but decreased at the higher temperature. Substrate inhibition of the PTE activities was appeared at high concentrations of pectin. Those PTE activities were increased under 0.6M of KCI and NaCI, but that maximal activities at the concentration of 0.2M MgC $l_2$.

• Microbiology and Biotechnology Letters
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• v.34 no.2
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• pp.121-128
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• 2006

The purified xylanase from Bacillus alcalophilus AX2000 was modified with various chemical modifiers to determine amino acid residues in the active site of the enzyme. Treatment of the enzyme with group-specific reagents such as carbodiimide or N-bromosuccinimide resulted in complete loss of enzyme activity. These results suggested that these reagents reacted with glutamic acid or aspartic acid and tryptophan residues located at or near the active site. In each case, inactivation was performed by pseudo first-order kinetics. Inhibition of enzyme activity by carbodiimide and N-bromosuccinimide showed non-competitive and competitive inhibition type, respectively. Addition of xylan to the enzyme solution containing N-bromosuccinimide prevented the inactivation, indicating the presence of tryptophan at the substrate binding site. Analysis of kinetics for inactivation showed that the loss of enzyme activity was due to modification of two glutamic acid or aspartic acid residues and single tryptophan residue.

• Food Science and Preservation
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• v.5 no.3
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• pp.299-304
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• 1998

Screening for antibacterial activities with microorganisms related to the food putrefaction by ethanol extract from Chrysanthemum petals widely used for the traditional wine production, and antibacterial activities of each concentration and minimum inhibitory concentration(MIC) from the ethanol extract were researched. Antibacterial activity of ehanol extract for B. subtilis was higher in C. boreale than in C. Morifolium, but that of E. coli was higher in C. molifolium than in C. boreale. C. boreale was higher than C. morifolium in the antibacterial activity of ehanol extract and MIC of ehanol extract from C. boreale was 60-70${\mu}\ell$/ml. Ethanol extract from C. boreale was higher Gram(-) than Gram(+) in the antibacterial activities, but Gram(-), Gram(+) were greatly inhibited on growth in 100${\mu}\ell$ concentration.

• The Korean Journal of Ecology
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• v.23 no.5
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• pp.353-357
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• 2000

The soil pH favored by several native plants in Korea ranges 5.33∼7.20, while a more acidic range of pH 3.95∼6.10 is acceptable to exotic plants. Ethanol extracts of native and exotic plants in Korea were investigated for antimicrobial activity against Bacillus sphiaericus 2362, Bacillus thuringiensis var. subtilis and Bacillus thuringiensis var. cereus and Actinomycetes. Higher antimicrobial activity was observed from the extract of exotic plants than those of native plants. The ethanol extract of Ambrosia artemisiifolia var. elatior was observed to have the highest antimicrobial activity against 4 species of soil microbes. Especially, antimicrobial activity of Ambrosia artemisiifolia var. elatior showed the largest clear zone of 48mm in Actinomycetes. Larger clear zone was formed in the order of caffeic acid, benzoic acid and ρ -coumaric acid among the nine chemical compounds. Accordingly, the antimicrobial activity of Ambrosia artemisiifolia var elatior against Actinomycetes was found to be due to the synergetic effect of chemical compounds.

• KSBB Journal
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• v.14 no.3
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• pp.291-296
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• 1999

Chiral epoxides are key intermediates for the production of chiral pharmaceuticals, agrochemicals, and functional food additives. Chiral epoxides can be produced by either chemical or biological method. In biocatalytic production routes, chiral epoxides can be produced via epoxidations of prochiral alkenes by monooxygenase or peroxidase. Kinetic resolution of racemic epoxides using whole cells of bacteria or fungi might be commercially useful, since it is possible to obtain chiral epoxides with high optical purities from relatively cheap and readily avaiable racemic epoxides. Some bioprocesses already are commercially developed: the biocatalytic production of chiral epichlorohydrin via microbial stereospecific dehalogenation, and lipase-catalyzed enantioselective hydrolysis in a hollow fiber membrane bioreactor for the production of chiral methyl trans-3-(4-methoxyphenyl)glycidate. the intermediate for calcium antagonist diltiazem. The importance of biocatalytic production of chiral epoxides with several examples from literature are presented.

• Korean Journal of Microbiology
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• v.35 no.3
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• pp.231-236
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• 1999

The fuugus(Penicil1ium oralicum; HCLF-34) secreted the cyanobacteria lytic enzyme which had a molecular weight of about 22 kDa, a optimum temperature of $20^{\circ}C$, a optimum pH of 3.5, and a temperature-stable up to $50^{\circ}C$. The chemical ions such as sodium, potassium, barium, magnesium. and mangan ions appeared positive activity. but calcium, iron, copper ions, EDTA, and PMSF displayed negative activity: this results were the same as the characterilics of other cell wall lytic enzymes. This extracellular enzyme showed lytic aclivily against SDS-insoluble peptidoglycan of Anabaenrr cylinrlrica. The cell wall lylic enzyme of Penicilliurn oxalicum(HCLF-34) seemed to be glycosidase-like enzyme in the fact that ihe concentration of rcducing sugar was increased when the peptidoglycan of Anabaena qlinrlricn md Micrococcus luteus reacted with this enzyme