• Food Science and Biotechnology
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• v.17 no.5
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• pp.895-898
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• 2008

The mobility of water in set yogurt during fermentation was studied using nuclear magnetic resonance (NMR) relaxometry. The spin-spin relaxation was analyzed using a 2-fraction model, resulting in 2 spin-spin relaxation time constants $T_{21}$ and $T_{22}$. Both $T_{21}$ and $T_{22}$ exhibited rapid changes between 2 and 4 hr of fermentation, coinciding with the drop in pH and the rise in lactic acid bacteria count. The spin-lattice relaxation time $T_1$ increased over the fermentation period. Both $T_1$ and $T_2$ showed an increase in the mobility of water upon gel formation during fermentation. Water redistribution within the gel matrix due to casein aggregation and structure forming may be responsible for the changes in mobility.

• BMB Reports
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• v.28 no.1
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• pp.46-50
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• 1995

Three kinds of mouse tumor necrosis factor (TNF), which have molecular weights of 35 kDa, 45 kDa, and 18 kDa on SDS-PAGE, were partially purified from serum-free culture supernatants of mouse peritoneal macrophages induced with lipopolysaccharide. Analysis of the native molecular weights by gel filtration indicated that the 18 kDa and 45 kDa TNFs aggregate into 50 kDa and 100 kDa molecules, respectively, while the 35 kDa TNF is contained in high molecular weight aggregates of approximately 200 kDa. The three kinds of cytotoxic factors all elicited tumor reducing responses.

• Journal of Microbiology and Biotechnology
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• v.9 no.5
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• pp.683-686
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• 1999

Four mutants of Acetobacter xylinum BRC5 defective in gluconic acid production were isolated from UV-irradiated cells. The gluconic acid-negative mutants did not show glucose oxidase activity. The mutants were also defective in cellulose production. A randomly selected mutant grown in the Hestrin-Schramm medium (pH 6.0) supplemented with gluconic acid, however, was found to synthesize cellulose. The mutant grown in Hestrin-Schramm medium whose pH was adjusted to 5.0 with HC1 and contained no gluconic acid also produced cellulose. Wild-type cells grown under the same condition synthesized cellulose more rapidly than those grown in the pH 6.0 medium.

• Journal of Microbiology and Biotechnology
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• v.11 no.3
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• pp.376-383
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• 2001

Lactobacillus casei YIT 9018 was microencapsulated within alginate or alginate/chitosan double membrane using an air atomizer. Microbiological analysis revealed that the viability of encapsulated L. casei in gastric juice, hydrogen peroxide, and pepsin was 2-3 log cycle higher than that of the nonencapsulated cell. However, the encapsulated cells did not show a signifciant increase in survival when subjected to in virto high acid and 0.6% bile salt condition. Alginate-encapsulated, alginate/chitosan-encapsulated, and nonencapsulated cells were stored at different temperatures eencapsulated cells showed similar stability at $4^{\circ}C$. However, at $22^{\circ}C$, the alginate/chitosan-encapsulted cell was the most stable.

• Journal of Microbiology and Biotechnology
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• v.11 no.5
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• pp.858-862
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• 2001

The purpose of this research was to investigate the effects of nondigestible oligosaccharides (NDO) from red ginseng marc on the growth of Bifidobacterium spp. Red ginseng marc, a fibrous byproduct of ginseng extract from processing, was destarched by ${\alpha}$-amylase and amyloglucosidase treatment, and then treated with a commercial pectinase to produce NDO. The bifidogenic effects of NDO on B. adolescentis, B. animalis, B. breve, and B. longum were investigated in vitro. NDO significantly promoted the growth of Bifidobacterium spp. The growth, decrease of pH, and organic acid formation (acetate, lactate, formate) were markedly different among the species. B. adolescentis showed the best growth and produced the greatest amount of organic acids. When NDO was used as a carbon source in the cocultivation of Bifidobacterium spp. and Clostridium perfringens, the growth of Bifidobacterium spp. was not influenced by the existence of Cl. perfringens. The result strongly suggested that NDO from red ginseng marc could be used as a potential bifidogenic source.

• Journal of Microbiology and Biotechnology
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• v.27 no.3
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• pp.460-470
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• 2017

Mussels are major fouling organisms causing serious technical and economic problems. In this study, antifouling activity towards mussel was found in three compounds isolated from a marine bacterium associated with the sea anemone Haliplanella sp. This bacterial strain, called PE2, was identified as Vibrio alginolyticus using morphology, biochemical tests, and phylogenetic analysis based on sequences of 16S rRNA and four housekeeping genes (rpoD, gyrB, rctB, and toxR). Three small-molecule compounds (indole, 3-formylindole, and cyclo (Pro-Leu)) were purified from the ethyl acetate extract of V. alginolyticus PE2 using column chromatography techniques. They all significantly inhibited byssal thread production of the green mussel Perna viridis, with $EC_{50}$ values of $24.45{\mu}g/ml$ for indole, $50.07{\mu}g/ml$ for 3-formylindole, and $49.24{\mu}g/ml$ for cyclo (Pro-Leu). Previous research on the antifouling activity of metabolites from marine bacteria towards mussels is scarce. Indole, 3-formylindole and cyclo (Pro-Leu) also exhibited antifouling activity against settlement of the barnacle Balanus albicostatus ($EC_{50}$ values of 8.84, 0.43, and $11.35{\mu}g/ml$, respectively) and the marine bacterium Pseudomonas sp. ($EC_{50}$ values of 42.68, 69.68, and $39.05{\mu}g/ml$, respectively). These results suggested that the three compounds are potentially useful for environmentally friendly mussel control and/or the development of new antifouling additives that are effective against several biofoulers.

• Journal of Microbiology
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• v.37 no.2
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• pp.97-101
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• 1999

Random hexapeptide library on the surface of filamentous bacteriophage was constructed using the SurfZAP vector. The size of the library was approximately 105. The peptide insert was flanked by two cysteines to constrain the peptide structure with a disulfide bond. This library was screened for the topoisomerase II binding peptide. Dramatic enrichment of the fusion phage over the VCS M13 helper phage was demonstrated by bio-panning affinity selection.

• BMB Reports
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• v.32 no.3
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• pp.306-310
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• 1999

The partial cDNA of the MT-c clone encoding snake venom metalloprotease was subcloned and expressed in E. coli. The expressed metalloprotease was purified by affinity chromatography in the presence of urea, and then successfully refolded into its functional form, retaining metalloprotease activity that hydrolyzes fibrinogen. The simple and convenient refolding strategy established in this work was highly efficient in recovering the recombinant enzyme activity. Experimental evidence suggests that the C-terminal amino acid stretch of 16 residues is a critical sequence for proper folding of the metalloprotease domain.

• BMB Reports
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• v.28 no.2
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• pp.107-111
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• 1995

In malonate grown Pseudomonas fluorescens, malonate decarboxylase and acetyl-CoA synthetase were induced, whereas in Acinetobacter calcoaceticus malonate decarboxylase, acetate kinase, and phosphate acetyltransferase were induced. In both bacteria malonate decarboxylase was the first, key enzyme catalyzing the decarboxylation of malonate to acetate, and it was localized in the periplasmic space. Acetate thus formed was metabolized to acetyl-CoA directly by acetyl-CoA synthetase in Pseudomonas, and to acetyl-CoA via acetyl phosphate by acetate kinase and phosphate acetyltransferase in Acinetobacter.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2001.06b
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• pp.21-22
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• 2001