Hongch’ŏn, South Korea
Hongch’ŏn, South Korea

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Han Y.R.,Seoul National University | Youn S.Y.,Seoul National University | Ji G.E.,Seoul National University | Ji G.E.,BIFIDO Co. | Park M.S.,Anyang University, South Korea
Journal of Microbiology and Biotechnology | Year: 2014

Approximately 50% of people in the world experience abdominal flatulence after the intake of foods containing galactosides such as lactose or soybean oligosaccharides. The galactoside hydrolyzing enzymes of α- and β-galactosidases have been shown to reduce the levels of galactosides in both the food matrix and the human gastrointestinal tract. This study aimed to optimize the production of α- and β-galactosidases of Bifidobacterium longum subsp. longum RD47 with a basal medium containing whey and corn steep liquor. The activities of both enzymes were determined after culturing at 37°C at pH 6.0 for 30 h. The optimal production of α- and β-galactosidases was obtained with soybean oligosaccharides as a carbon source and proteose peptone no. 3 as a nitrogen source. The optimum pH for both α- and β-galactosidases was 6.0. The optimum temperatures were 35°C for α-galactosidase and 37°C for β- galactosidase. They showed temperature stability up to 37°C. At a 1 mM concentration of metal ions, CuSO4 inhibited the activities of α- and β-galactosidases by 35% and 50%, respectively. On the basis of the results obtained in this study, B. longum RD47 may be used for the production of α- and β-galactosidases, which may reduce the levels of flatulence factors. © 2014 by The Korean Society for Microbiology and Biotechnology.


Wang Y.,Seoul National University | Kim J.Y.,Seoul National University | Park M.S.,Anyang University, South Korea | Park M.S.,BIFIDO Co. | And 2 more authors.
Journal of Microbiology | Year: 2012

For the development of a food-grade expression system for Bifidobacterium, a strong promoter leading to high-level expression of cloned gene is a prerequisite. For this purpose, a promoter screening host-vector system for Bifidobacterium has been established using β-glucosidase from Bifidobacterium lactis as a reporter and Bifidobacterium bifidum BGN4 as a host, which is β-glucosidase negative strain. Seven putative promoters showing constitutive high-level expression were selected through microarray analysis based on the genome sequence of B. bifidum BGN4. They were cloned into upstream of β-glucosidase gene and transformed into Escherichia coli DH5α and B. bifidum BGN4. Promoter activities were analyzed both in E. coli and B. bifidum BGN4 by measuring β-glucosidase activity. β-Glucosidase activities in all of the transformants showed growth-associated characteristics. Among them, P919 was the strongest in B. bifidum BGN4 and showed maximum activity at 18 h, while P895 was the strongest in E. coli DH5α at 7 h. This study shows that novel strong promoters such as P919 can be used for high-level expression of foreign genes in Bifidobacterium and will be useful for the construction of an efficient food-grade expression system. © 2012 The Microbiological Society of Korea and Springer-Verlag Berlin Heidelberg.


Youn S.Y.,Seoul National University | Park M.S.,Anyang University, South Korea | Park M.S.,BIFIDO Co. | Ji G.E.,Seoul National University | Ji G.E.,BIFIDO Co.
Journal of Microbiology and Biotechnology | Year: 2012

β-Glucosidase is necessary for the bioconversion of glycosidic phytochemicals in food. Two Bifidobacterium strains (Bifidobacterium animalis subsp. lactis SH5 and B. animalis subsp. lactis RD68) with relatively high β- glucosidase activities were selected among 46 lactic acid bacteria. A β-glucosidase gene (bbg572) from B. lactis was shotgun cloned, fully sequenced, and analyzed for its transcription start site, structural gene, and deduced transcriptional terminator. The structural gene of bbg572 was 1,383 bp. Based on amino sequence similarities, bbg572 was assigned to family 1 of the glycosyl hydrolases. To overexpress bbg572 in Bifidobacterium, several bifidobacteria expression vectors were constructed by combining several promoters and a terminator sequence from different bifidobacteria. The maximum activity of recombinant Bbg572 was achieved when it was expressed under its own promoter and terminator. Its enzyme activity increased 31-fold compared with those of its parental strains. The optimal pH for Bbg572 was pH 6.0. Bbg572 was stable at 37-40°C. It hydrolyzed isoflavones, quercetins, and disaccharides with various β-glucoside linkages. Bbg572 also converted the ginsenosides Rb1 and Rb2. These results suggest that this new β-glucosidase-positive Bifidobacterium transformant can be utilized for the production of specific aglycone products. © The Korean Society for Microbiology and Biotechnology.


Park S.J.,Seoul National University | Youn S.Y.,Seoul National University | Ji G.E.,Seoul National University | Ji G.E.,BIFIDO Co. | And 2 more authors.
Food Science and Biotechnology | Year: 2012

Various strains of Lactobacillus and Leuconostoc species were evaluated to select the most promising strain to carry out transforming major ginsenosides into minor ginsenosides. Among the experimental lactic acid bacteria (LAB), Leuconostoc mesenteroides KFRI 690, Leuconostoc paramesenteroides KFRI 159, and Lactobacillus delbrueckii KCCM 35486 produced compound K from major ginsenosides precursors (Rbl, Rc, Rd, and F2). KFRI 690 showed the best transforming activity among them. Furthermore, these LABs could biotransform ginsenosides without disrupting the cell to release enzyme activity. The conversion ratio of Rbl to compound K using KFRI 690 has been enhanced up to 97.8% by adding 2% sucrose into the culture medium. This is the first report on the production of compound K using whole cells of Leu. mesenteroides, Leu. paramesenteroides, and Lb. delbrueckii, which are food grade lactic acid bacteria.


Lee E.-J.,Sookmyung Womens University | Ji G.-E.,Seoul National University | Ji G.-E.,BIFIDO Co. | Sung M.-K.,Sookmyung Womens University
Inflammation Research | Year: 2010

Objective: We investigated the inhibitory effects of quercetin and kaempferol treatment on the suppression of immunoglobulin E (IgE)-mediated allergic responses in relation to intestinal epithelium barrier function in RBL-2H3 and Caco-2 cells. Methods: RBL-2H3 cells as a model of intestinal mucosa mast cells were treated with flavonols followed by IgE-anti-dinitrophenyl sensitization. The extent of degranulation and the release of pro-inflammatory cytokines were measured. Caco-2 cells were stimulated with interleukin (IL)-4 or IgE-allergen with or without flavonol pretreatment and changes in the expression of CD23 mRNA and mitogen-activated protein kinase (MAPK), and chemokine release were determined. Results: Flavonols inhibited the secretion of allergic mediators in RBL-2H3 cells and suppressed the CD23 mRNA expression and p38 MAPK activation in IL-4 stimulated Caco-2 cells. Flavonols also suppressed IgE-OVA induced extra signal-regulated protein kinase (ERK) activation and chemokine release. Conclusions: Quercetin and kaempferol effectively suppressed the development of IgE-mediated allergic inflammation of intestinal cell models. © 2010 Springer Basel AG.


Ju You H.,Seoul National University | Jin Ahn H.,Seoul National University | Ji G.E.,Seoul National University | Ji G.E.,BIFIDO Co.
Journal of Agricultural and Food Chemistry | Year: 2010

The flavonol quercetin in plants and foods occurs predominantly in the form of glycoside whose sugar moiety affects the bioavailability and the mechanism of its biological activities. The antiproliferative activities of quercetin derivatives such as quercetin aglycone, quercetin-3-ß-D-glucoside (Q3G), and rutin were compared using six different cancer cell lines including colon, breast, hepatocellular, and lung cancer. The IC50 value of Q3G ranged between 15 and 25 μM in HT-29, HCT 116, MCF-7, HepG2, and A549 cells. In these five cell lines, Q3G showed the most potent growth inhibition, whereas rutin showed the least potency. Transformation of rutin to Q3G was conducted by controlling R-L-rhamnosidase and ß-D-glucosidase activities from crude enzyme extract of Aspergillus niger. Carbon sources during culture and transformation conditions such as pH, temperature, and heatstability were optimized. After 4 h biotransformation, 99% of rutin was transformed to Q3G and no quercetin was detected. This study presented an efficient biotransformation for the conversion of rutin to Q3G which was newly shown to have more potent antiproliferative effect than quercetin and rutin. ©2010 American Chemical Society.


Lee K.J.,Seoul National University | Ji G.E.,Seoul National University | Ji G.E.,BIFIDO Co.
Journal of Ginseng Research | Year: 2014

Background: Understanding what causes changes in the flux of free fatty acids (FFA) is important to elucidate the etiology of metabolic syndrome. The first aim of this study was to test whether or not hormones and the autonomic nervous system influence blood FFA levels. A secondary aim was to test by means of a multiple group path analysis whether the consumption of fermented red ginseng (FRG; Panax ginseng) would influence those causal relationships. Methods: Ninety-three postmenopausal women (age 50-73 yr) were randomly divided into two groups. One group (44 women; age, 58.4±5.9 yr; body mass index, 23.6±2.5 kg/m2) was supplied placebo capsules and the other group (49 women, age 58.4±5.5 yr; body mass index, 22.9±2.4 kg/m2) was supplied FRG capsules. Both prior to and after the study (2 wk), blood samples were collected from the participants and several blood variables were measured and analyzed. Results: Squared multiple correlations of FFA were 0.699 in the placebo group and 0.707 in the FRG group. The unstandardized estimate of estradiol (E2) for FFA was 0.824 in both groups. Conclusion: The path coefficients of cortisol and the branchial pulse for FFA were significantly different between the FRG group and the placebo group. © 2014, The Korean Society of Ginseng, Published by Elsevier.


Trademark
Bifido Co. | Date: 2016-01-25

Bifidus probiotics containing B. Bifidum for medical purposes; powder form bifidus probiotics containing B. Bifidum for medical purposes.


Trademark
Bifido Co. | Date: 2016-01-25

Bifidus probiotics for medical purposes; powder form bifidus probiotics for medical purposes.


Trademark
Bifido Co. | Date: 2016-01-11

Cosmetics; make-up; functional cosmetics; cosmetics for scalp; cosmetic preparations for bath and shower; cosmetics using biotechnology; cosmetic preparations for skin care and skin treatment. Bifidus probiotics for medical purposes; bifidus probiotics in powder form for medical purposes; vitamins and vitamin preparations; dietary supplements consisting primarily of iron; nutritional supplements consisting primarily of iron; ginseng capsules for medical purposes; diet capsules; vitamin and mineral preparations. Fermented milk products using bifidobacteria; milk with bifidobacteria; yogurt with bifidobacteria; cheese with bifidobacteria; processed red ginseng products; ginseng processed food products.

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