• Journal of Microbiology and Biotechnology
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• v.10 no.4
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• pp.551-553
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• 2000

A strong constitutive $P_{JH}$ promoter from Bacillus was applied to overexpress the endoxylanase gene in B. subtilis. The expression plasmid, pHJKJ4, was designed to contain the $P_{JH}$ promoter and endoxylanase promoter ($P_B$), and introduced into B. subtilis DB104. Through batch fermentation of the trasformant cell on a maltose medium, endoxylanase was produced in a growth-associated manner as the predominant protein. The total activity reached about 600 unit/ml at the end of the cultivation, which corresponded to 698 mg endoxylanase protein/l with a specific activity of 860 unit/mg protein. It was also found that the segregational plasmid instability was less than 30% and most of the endoxylanase activity was detected in the culture medium. This result suggests that the secretory production of endoxylanase can be significantly enhanced with the use of the $P_{JH}$ promoter and high-cell density culture techniques, quantitatively as well as qualitatively.

• Journal of Microbiology and Biotechnology
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• v.12 no.3
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• pp.411-416
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• 2002

Bacillus macerans cyclodextrin glucanotransferase (CGTase) was expressed on the cell surface of Saccharomyces cerevisiae by fusing with Aga2p linked to the membrane-anchored protein, Aga1p. The surface display of CGTase was confirmed by immunofluorescence microscopy and its enzymatic ability to form ${\alpha}$-cyclodextrin from starch. The maximum surface-display of CGTase was obtained by growing recombinant S. cerevisiae at $20^{\circ}C$ and pH 6.0. S. cerevisiae cells displaying CGTase on their surface consumed glucose and maltose, inhibitory byproducts of the CGTase reaction, to enhance the purity of produced cyclodextrins. Accordingly, the experimental results described herein suggest a possibility of using the recombinant S.cerevisiae anchored with bacterial CGTase on the cell surface as a whole-cell biocatalyst for the production of cyclodextrin.

• Korean Journal of Veterinary Service
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• v.29 no.3
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• pp.297-308
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• 2006

Fowl typhoid (FT) is a septicemic disease caused by Salmonella gallinarum. The purpose of this study was to investigate the antimicrobial resistance and pulsed -field gel electrophoresis (PFGE) patterns of S gallinarum isolated from broiler. During 1999 to 2004, there was isolated a total of 26 strains in liver and spleen. The biochemical characteristics of S gallinarum isolates was nonmotile, no production of $H_2S$, glucose gas, non-fermented rhamnose, indole-negative, fermentation of dulcitol, mannitol, maltose, and ornithine decarboxylase. At antimicrobial susceptibility, all of isolates were susceptible to amoxicillin/clavulanic acid, amikacin, neomycin, kanamycin, and cephalothin. Twenty-six isolates were divided into 19 resistant patterns and 6 strains was 8-multi-drug resistance. PFGE of Xba I restriction fragments of S gallinarum isolates was 22 patterns.

• KSBB Journal
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• v.26 no.1
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• pp.19-26
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• 2011

Of the 500 Actinomycetes isolates obtained from soil, one isolate grown on maltose as the sole carbon source produced compound BHK-P19, which inhibited the growth of multiple drug resistant P. aeruginosa 0245. Ultraviolet radiation mutagenesis curtailed production of BHK-P19. Mutation of the BHK-P19 producer using N-methyl-N'-nitro-N-nitroso-guanidine obviated the antibacterial activity to P. aeruginosa 0245, but not towards P. aeruginosa 0225. The mixing of BHK-P19 and BHK-S5 culture extracts inhibited P. aeruginosa 0254, 0225 and 1113. The combined application of BHK-P19 culture extract and Schizandra chinensis Baillon extract inhibited P. aeruginosa 0254, 0225, 0826, 1113, 1378, 1731 and 2492. Use of various concentrations of BHK-P19 culture extract and ampicillin markedly increased antibacterial activity against multi-drug resistant P. aeruginose 1113.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.1
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• pp.126-130
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• 2006

The purpose of this research was to study the effect of freeze drying on the microorganisms in kefir. Influences of lyoprotectants and rehydrated media (water at $4^{\circ}C$, $25^{\circ}C$; 10% reconstituted milk at $4^{\circ}C$, $25^{\circ}C$) on the viability of lactic acid bacteria and yeasts in freeze-dried kefir were investigated. Kefir was made from cow milk which was inoculated with 5% kefir grains, and incubated at $20^{\circ}C$ for 20 h. Lyoprotectants (galactose, lactose, maltose, sucrose and trehalose) were added independently before dehydration of kefir by freeze drying. Results indicated significant loss in viability of microorganisms in kefir after freeze-drying. Addition of 10% galactose or 10% sucrose as lyoprotectants significantly increased the survival rates of both lactic acid bacteria and yeasts (p<0.05). The $4^{\circ}C$ rehydration temperature showed the best viabilities for yeasts, however, viability was not significantly affected by rehydration media (p>0.05).

• Korean Journal of Veterinary Service
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• v.32 no.2
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• pp.155-163
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• 2009

Fowl typhoid (FT) is a septicemic disease caused by Salmonella Gallinarum. The purpose of this study was to investigate the antimicrobial resistance and pulsed-field gel electrophoresis (PFGE) patterns of S. Gallinarum isolated from chicken. During 1999 to 2004, there was isolated a total of 100 strains in liver and spleen. The biochemical characteristics of S. Gallinarum isolates was nonmotile, no production of H$_2$S, glucose gas, non-fermented rhamnose, indole-negative, fermentation of dulcitol, mannitol, maltose, and ornithine decarboxylase. At antimicrobial susceptibility, all of isolates were susceptible to amoxicillin/clavulanic acid, amikacin, neomycin, kanamycin, norfloxacin and enrofloxacin. One hundred isolates were divided into 54 resistant patterns and 37 strains was 6-multi drug resistance. PFGE of Xba I restriction fragments of S. Gallinarum isolates was 20 patterns.

• Korean Journal of Veterinary Service
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• v.33 no.1
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• pp.51-57
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• 2010

Salmonella Typhimurium is a virulent pathogen for human and animal. We studied serotypes, biochemical characteristics, and antimicrobial resistance of S. Typhimurium isolated from diseased pigs in Gyeongbuk province over 1998 to 2008. One hundred sixteen isolates were identified as S. Typhimurium by biochemical characteristics and serotypes from 90 farms. The biochemical characteristics of S. Typhimurium isolates was production of $H_2S$, indole-negative, fermentation of mannitol, dulcitol, sorbitol, inositol, rhamnose, and maltose, and ornithine decarboxylase. At antimicrobial susceptibility test, the majority of isolates were highly susceptible to amoxicillin/clavulanic acid, cefepime, ciprofloxacin, while were highly resistant streptomycin, cephalothin, enrofloxacin, nalidixic acid, apramycin, chloramphenicol, tetracycline. The isolates were divided into 65 resistant patterns and 47 of the isolates were shown as a DT104 ASSSuT resistant phenotype.

• Korean journal of food and cookery science
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• v.27 no.5
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• pp.577-587
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• 2011

In this study, lotus leaf was added to a Takju (Korean milky rice wine) preparation to evaluate its effects on physicochemical and fermentation properties. For rapid saccharification Takju was stored at 25$^{\circ}C$ for 2 days and then temperature was switched to 18$^{\circ}C$ to mature the wine for 21 days. From the start of fermentation to 2-days, the pH of Takju decreased rapidly and acidity increased. Maltose, a byproduct of starch saccharification, increased for 2 days then rapidly decreased. Glucose fluctuated for 7 days and of the 21-days fermentation. The ethanol production rate was highest during the first 7 days, then slowed. Total viable yeast and lactic acid bacterial counts increased rapidly for 2 days and then decreased gradually thereafter. Leuconostoc spp. grew rapidly for 1 day and sharply disappeared with decreasing pH. DPPH radical scavenging activity was significantly higher for Takju prepared with lotus leaf than without. The overall acceptance of Takju tended to increase when it was prepared with lotus leaf.

• Korean Journal of Microbiology
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• v.26 no.1
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• pp.37-43
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• 1988

This research was focused on investigation of the condition for protoplast formation and regeneration of protoplast fusion between Saccharomyces cerevisiae which has fermentation ability and Candida cariosilignicola which can grow at high temperature and utilize methanol. The results obtained were as follows; The highest production was collected in exponential growth phase. Ninety-nine% protoplast formation of C. cariosilignicola was obtained in glycin-NaOH buffer (pH10.0) containing Zymolyase 0.5mg/ml at $35^{\circ}C$ for 1hr incubation. The highest regeneration was produced when protoplast wuwpension containing 0.5% soft agar in buffered 50mM $CaCl_{2}$ was poured as a soft overlay onto 2% agar plates. Equal amuont of protoplast suspension of two strains was mixed and centrifuged. The subsequent pellet was added to 2ml of 35% polyethylene glycol (MW 4,000) containing 50mM $CaCl_{2}$, and incubated at $30^{\circ}C$ for 10min. Then 0.1ml of the suspension of aggregated protoplast was immediately covered with minimal medium and incubated at $40^{\circ}C$ for 5-7 days. As results, $SC_{1}$, $SC_{2}$, and $SC_{3}$ fusants were obtained. The physiological characteristics of fusants produced by protoplast fusion were; $SC_{1}$, and $SC_{2}$ utilized maltose, galactose, methanol, potassium nitrate. $SC_{3}$ utilized all the above materials except galactose.

• Journal of Microbiology and Biotechnology
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• v.11 no.4
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• pp.636-643
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• 2001

Bacillus sp. AIR-5, a strain from soil, produced an extracellular maltopentaose-forming amylase from amylose and soluble starch. This bacterium produced 8.9 g/l of maltopentaose from 40 g/l of soluble starch in a batch fermentation and the maltopentaose made up 90 % of the maltooligosaccharides produced (from maltose to maltoheptaose). The culture supernatant was concentrated using a 30 K molecular weight cut-off membrane and purified by DEAE-Cellulose and Sephadex G-150 column chromatographies. The purified protein showed one band on a native-PAGE and its molecular mass was estimated as 250 kDa. The 250-kDa protein was composed of tetramers of a 63-kDa protein. the isoelectric point of the purified protein was pH 6.9, and the optimum temperature for the enzyme activity was $45^{\circ}C$. The enzyme was quickly inactivated above $55^{\circ}C$, and showed a maximum activity at pH 8.5 and over 90% stability between a pH of 6 to 10. The putative N-terminal amino acid sequence of AIR-5 amylase, ATINNGTLMQYFEWYVPNDG, showed a 96% sequence similarity with that of BLA, a general liquefying amylase.