• Journal of the Korean Applied Science and Technology
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• v.33 no.4
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• pp.751-761
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• 2016

In order to reduce the bitter taste of red ginseng extract(RGE), inclusion complexes(RGE-CD) of the extract with ${\alpha}$-, ${\beta}$-, ${\gamma}$-cyclodextine after acetic acid treatment at the steam process were prepared and studied for their taste by an electronic tongue. By complexation, the bitter taster- reducing efficacies of ${\alpha}$-CD and ${\beta}$-CD were much lower than that of ${\gamma}$-CD. This study suggested that by processing red ginseng with acetic acid it is possible to enhance the yield of both ginsenoside $Rg_3$ and nonpolar ginsenosides. Taste such as bitterness, sourness, saltiness, umami and sweetness of the red ginseng extract with different amounts of ${\alpha}$-CD, ${\beta}$-CD and ${\gamma}$-CD were checked using an electronic tongue. As a result, REG-${\gamma}$-CD10, prepared using 10%(w/w), showed significantly lower bitter taste than those of the other samples.

• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.148-153
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• 1989

A strain of alkalophilic Bacillus sp. YC-335 has been isolated from soil. The strain was capable of producing large amount of cyclodextrin glycosyl transferase (CGTase) in the culture broth. The preferable medium composition has been determined to be as follows : 1.5% soluble starch, 5% corn steep liquor, 0.1% $K_2$HPO$_4$, 0.02%mgSO$_4$.7$H_2O$, 1% CaCO$_3$and 1% Na$_2$CO$_3$(pH 10.3). The highest enzyme production was observed after 48 hours of cultivation at 31$^{\circ}C$. The optimum pH and temperature for the activity of crude enzyme were 6.0 and 5$0^{\circ}C$, respectively. The enzyme was stable between pH 5 and 9, and upto 5$0^{\circ}C$. The enzyme converted starch into $\alpha$-, $\beta$- and ${\gamma}$-CD in the relative amounts of 1:10:1.5, respectively.

• Korean Journal of Food Science and Technology
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• v.26 no.4
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• pp.375-381
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• 1994

A bacterial strain No. KY-126, which produced extracellular cyclodextrin glycosyltransferase(CGTase), was isolated from soil and identified as Bacillus stearothermophilus KY-126. The enzyme was purified by the treatments of ammonium sulfate precipitation, DEAF-Sephadex, Sephadex G-100 column chromatography. The optimal pH and temperature for the enzyme activity were pH 5.5 and $65^{\circ}C$, respectively. And the enzyme was stable at pH values from 6.0 to 11.0 at $55^{\circ}C$ for 30 min and stable up to $60^{\circ}C$ for 30 min.. The enzyme was inhibited by $HgCl_{2}$. The molecular weight of the enzyme was estimated to be 67,000 by using SDS-PAGE. The maximum conversion from starch to cyclodextrin (CD) by CGTase was 43% and obtained at 6 hr reaction and the ratio of ${\alpha}-,\;{\beta}-,\;{\gamma}-$, CD production at this time was 2.9 : 2.1 : 1.0.

• Bulletin of the Korean Chemical Society
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• v.21 no.2
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• pp.245-250
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• 2000

• Food Science and Biotechnology
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• v.17 no.4
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• pp.700-704
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• 2008

Anti-obesity effects of $\beta$-cyclodextrin in obese C57BL/6J mice induced by a high fat diet (HD) were observed. The administration of $\beta$-cyclodextrin reduced the gain of body weight, abdominal fat, liver weight, the lipid deposits of hepatocytes and the size of adipocytes in the HD group. In serum analysis, the total and low-density lipoprotein-cholesterols were significantly decreased in the $\beta$-cyclodextrin-supplemented HD group than in the HD group. However, high-density lipoprotein-cholesterol was not changed in these groups. In hypothalamic homogenates, the decrease of neuropeptide Y and increase of $\alpha$-melanocyte stimulating hormone were detected in the $\beta$-cyclodextrin-supplemented HD group compared to that in the HD group. These effects of $\beta$-cyclodextrin were similar to those of Garcinia cambogia, which is widely used as a natural anti-obesity product. These results suggest that $\beta$-cyclodextrin has anti-obesity effects through the lowering of the abdominal fat pad and inhibits the central effects of hunger.

• Journal of Microbiology and Biotechnology
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• v.1 no.1
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• pp.54-62
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• 1991

Cyclodextrin glucanotransferase(CGTase) derived from Bacillus macerans was immobilized by (1) covalent linkage on chitosan and chitin with glutaraldehyde, (2) adsorption on DEAE-cellulose and Amberite IRA 900 after succinylation, and (3) entrapment on alginate and polyacrylamide by cross linking. Adsorption on Amberite IRA 900 and covalent linking on chitosan were identified to be the most suitable immobilization methods considering the yield of activity and stability of immobilized CGTase. The enzymatic properties of immobilized CGTase were investigated and compared with those of the soluble CGTase. Thermal stability of CGTase immobilized on chitosan was increased from 50 to $55^{\circ}C$, and the optimum temperature of CGTase immobilized on Amberite IRA 900 was shifted from 55 to $50^{\circ}C$. The effect of molecular size of soluble starch (substrate) on immobilized CGTase investigated using partially liquefied substrates with different dextrose equivalent(DE). Cyclodextrin(CD) conversion yield augmented according to the increase of DE level for immobilized CGTase on Amberite IRA 900. CD conversion yield of partially cyclized starch with soluble CGTase was higher compared with liquefied one with ${\alpha}-amylase$.

• Bulletin of the Korean Chemical Society
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• v.35 no.5
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• pp.1409-1412
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• 2014

Sex hormones are important metabolites in vertebrates' development and reproduction. For rapid screening sex hormones, matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is one of the promising analytical platforms, but MALDI MS faces many challenges in detecting steroids such as low ionization efficiency and matrix background interference. One potential strategy to overcome matrix interference in the low m/z region is using a cyclodextrin (CD)-supported matrix for steroid analysis since CD-supported matrixes are known to effectively suppress matrix-related ion signals. In this study, we aimed to find the optimal CD-supported matrix for the analysis of the nonderivatized sex steroids. Our results showed that the ${\alpha}CD$-supported 2,5-dihydroxybenzoic acid (DHB) matrix efficiently ionized all three major classes of sex hormones, estrogens, androgens, and progestagens, with low or no matrix background and also with high sensitivity. In addition, the ${\alpha}CD$-supported DHB matrix mainly generated molecular ions or protonated ions of sex hormones, and this enabled us to obtain information-rich tandem mass spectra which potentially lead to unambiguous identification of steroid species from complex metabolite mixtures.

• Microbiology and Biotechnology Letters
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• v.20 no.4
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• pp.422-429
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• 1992

The effect of various water-activity depressors, such as pol yo Is, sugars, and polymers, on the conversion yields of the enzymatic synthesis of maltosyl-$\beta$-cyclodextrin from $\beta$-cyc1odextrin and maltose through reverse reaction of pullulanase was investigated. PEG 6000 of concentration of 10% (w/w) was found to be the most acceptable water-activity depressor resulting for increment of conversion yield from 43.0% to 55.9%, corresponding maltosyl-$\beta$-cyc1odextrin concentration of 3.02 g/100 ml H20. Water activity was changed from initial 0.966 to 0.914 upon addition of 20% (w/w) of PEG 6000. The conversion yields were inversely proportional to the water activities, and the increased conversion yield was caused by water activity depression which inhibited the hydrolysis reaction of maltosyl-$\beta$-CD to maltose and $\beta$-cyc1odextrin. The changes of enthalpy ($\Delta$H), entropy ($\Delta$S), and Gibbs free energy ($\Delta$G) were calculated to be 36.788 kJ/mole, 0.067 kJ/mole K. and 14.433 kJ/mole, respectively. The synthesis of maltosyl-$\beta$-CD could be increased substantially by the intermittent feeding of $\beta$-cyclodextrin. PEG 6000 could be separated effectively from reaction mixture using ultrafiltration membrane for reutilization.

• Proceedings of the Microbiological Society of Korea Conference
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• 2003.05a
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• pp.122-124
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• 2003

Cyclodextrin glucanotransferase (CGTase) and endoxylanase genes of Bacillus sp. were subcloned down-stream of yeast ADH1 promoter and expressed in S. cerevisiae. Most of the CGTase and endoxylanase expressed were detected in the extracellular medium with activity of 0.6 and 7-8 unit/ml, respectively. The recombinant enzymes were secreted as N-linked-glycosylated forms, resulting an enhanced thermal stability. CGTase predominantly produced $\alpha-cyclodextrin$ from starch and endoxylanase produced xylobiose and xylotriose from xylan.

• Microbiology and Biotechnology Letters
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• v.29 no.1
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• pp.31-36
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• 2001

Paenibacillus sp. JB-13 producing the cyclodextrin glucan-otransferase(CGTase) [EC 2.4.1.19] that glucosylated ascorbic acid(AA) at the C-2 position was isolated form soil and the optimal conditions for the production of 2-O-$\alpha$-D- Glucopyranosl L-Ascorbic acid(AA-2G) with CGTase were investigated. CGTase produced AA-2G efficiently using dextrin as a substrate and AA as an aceptor. Several AA-2-oilgosaccharides(AA-2Gs) were also produced in this reaction mixture, and these were efficiently hydro-lyzed to AA-2G and glucose by the treatment with glucoamylase. The optimal temperature for AA-2G production was $37^{\circ}C$ and the optimal pH was around 6.5. CGTase also utilized $\alpha$-,$\beta$-,${\gamma}$-CDs, soluble starch, com statch, dia-static solution from rice and diastatic solution from malt as substrate, but not glucose. The reaction mixture for the maximal production of AA-2G was following; 15% total substrate concentration, 2,500 units/ml of CGTase and a mixing ration of 3:2(g of AA: g of dextrin). Under this condition, 56 mM of AA-2G ,which corresponded to 12.4% yield based on AA. was produced after incubation for 44 hrs at $37^{\circ}C$ and pH 6.5.