• KSBB Journal
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• v.13 no.4
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• pp.352-356
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• 1998

Addition of cyclodextrin in the biotransformation of digitoxin into digoxin by Digitalis lanata cell suspension cultures enhanced the conversion yield. Presence of cyclodextrin also supported good stability of the intermediate product, digoxin, for long time. Among several kinds of cyclodextrins, ${\beta}$-cyclodextrin provided the best results. It was found that the optimum form of cyclodextrin utilization was the external addition of iclusion complexes between digitoxin and ${\beta}$-cyclodextrin at 1: 2 molar ratio from the beginning of biotransformation. With the optimized conditions, addition of ${\beta}$-cyclodextrin enhanced the production of digoxin up to 1.55 fold. In this case, not only digitoxin consumption was increased, but also the production of by-product was reduced.

• Microbiology and Biotechnology Letters
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• v.14 no.6
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• pp.461-466
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• 1986

A highly cyclodextrin glucanotransferase producing strain of Bacillus sp. was isolated from soil, and basic studies on the characteristics of the strain and its enzyme, conditions for the enzyme production, and the enzyme utilization were carried out. The isolated strain was aerobic, motile, endospore-forming and rod-shaped bacterium. Optimum pH and temperature for the enzyme action were 6.0 and 45$^{\circ}C$, and the enzyme was stable within 5$0^{\circ}C$, and between pH 6.0 and 10.0. The highest yield of the enzyme was obtained using the medium containing 2% corn starch as a carbon source, and 5% corn steep liquor, 0.1% urea and 0.25% ammonium sulfate as nitrogen sources. The fermentation conditions for the enzyme production in a jar fermentor were cetermined to be 3$0^{\circ}C$, 200rpm, 0.6vvm and 60hr cultural period. Stevioside transglycosylation catalyzed by this enzyme was identified by high performance liquid chromatography.

• The Korean Journal of Food And Nutrition
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• v.16 no.4
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• pp.334-339
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• 2003

To increase the utilization of citron, citron juice that is by-product of citron tea was spray dried and freeze dried. Cyclodextrin(CD) was used as wall material to stabilize during drying. The physiochemical properties of citron juice were as follows: water content of 82.3%, pH of 2.45, and there were little different in two kinds of drying or CD added in different ratio. Citric acid, malic acid, succinic acid and lactic acid were detected in all of the samples. Spray and freeze-drying increased markedly yellowness compared to that of citron juice. Heat stability was reduced by both of two kinds of drying, and CD 15% was more decreased than CD 10%. Water uptake by freeze-drying was somewhat higher than that of spray-drying. When sensory properties of original citron juice was compared with those of spray and freeze dried, freeze drying with 10% of cyclodextrin was evaluated as superior to citron juice or other drying conditions.

• Clean Technology
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• v.19 no.3
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• pp.212-218
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• 2013

The microparticles of 2-hydroxypropyl-${\beta}$-cyclodextrin (HP-${\beta}$-CD) were prepared using aerosol solvent extraction system (ASES) by employing supercritical carbon dioxide as an antisolvent, The effects of various process parameters such as temperature, pressure, solution concentration and solution flow rate on the formation of HP-${\beta}$-CD microparticles were investigated. The HP-${\beta}$-CD microparticles prepared by the ASES process were observed to consist of agglomerates of nano-sized (50-200 nm) particles. When an aqueous solution of ethanol was used as a solvent for HP-${\beta}$-CD, the HP-${\beta}$-CD particles were found to be spherical in shape and to become larger as the water content increased. It was confirmed that the micronization of HP-${\beta}$-CD using the ASES process could enhance the inclusion efficiency of ibuprofen/HP-${\beta}$-CD complexes significantly.

• Journal of Microbiology
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• v.42 no.4
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• pp.319-327
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• 2004

An additional amylase, besides the typical $\alpha-amylase,$ was detected for the first time in the cytoplasm of B. subtilis SUH4-2, an isolate from Korean soil. The corresponding gene (bbmA) encoded a malto­genic amylase (MAase) and its sequence was almost identical to the yvdF gene of B. subtilis 168, whose function was unknown. Southern blot analysis using bbmA as the probe indicated that this gene was ubiquitous among various B. subtilis strains. In an effort to understand the physiological function of the bbmA gene in B. subtilis, the expression pattern of the gene was monitored by measuring the $\beta-galactosidase$ activity produced from the bbmA promoter fused to the amino terminus of the lacZ struc­tural gene, which was then integrated into the amyE locus on the B. subtilis 168 chromosome. The pro­moter was induced during the mid-log phase and fully expressed at the early stationary phase in defined media containing $\beta--cyclodextrin\;(\beta-CD),$ maltose, or starch. On the other hand, it was kept repressed in the presence of glucose, fructose, sucrose, or glycerol, suggesting that catabolite repression might be involved in the expression of the gene. Production of the $\beta-CD$ hydrolyzing activity was impaired by the spo0A mutation in B. subtilis 168, indicating the involvement of an additional regu­latory system exerting control on the promoter. Inactivation of yvdF resulted in a significant decrease of the $\beta-CD$ hydrolyzing activity, if not all. This result implied the presence of an additional enzyme(s) that is capable of hydrolyzing $\beta-CD$ in B. subtilis 168. Based on the results, MAase encoded by bbmA is likely to be involved in maltose and $\beta-CD$ utilization when other sugars, which are readily usable as an energy source, are not available during the stationary phase.

• Microbiology and Biotechnology Letters
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• v.44 no.3
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• pp.363-369
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• 2016

A putative cyclomaltodextrinase gene (licd) was found from the genome of Listeria innocua ATCC 33090. The licd gene is located in the gene cluster involved in maltose/maltodextrin utilization, which consists of various genes encoding maltose phosphorylase and sugar ABC transporters. The structural gene encodes 591 amino acids with a predicted molecular mass of 68.6 kDa, which shares less than 58% of amino acid sequence identity with other known CDase family enzymes. The licd gene was cloned, and the dimeric enzyme with C-terminal six-histidines was successfully produced and purified from recombinant Escherichia coli. The enzyme showed the highest activity at pH 7.0 and 37℃. licd could hydrolyze β-cyclodextrin, starch, and maltotriose to mainly maltose, and it cleaved pullulan to panose. It could also catalyze the hydrolysis of acarbose to glucose and acarviosine-glucose. In particular, it showed significantly higher activity towards β-cyclodextrin and maltotriose than towards starch and acarbose. licd also showed transglycosylation activity, producing α-(1,6)- and/or α-(1,3)-linked transfer products from the acarbose donor and α-methyl glucopyranoside acceptor.

• Korean Journal of Food Science and Technology
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• v.35 no.2
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• pp.266-271
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• 2003

Insoluble polyphenol antioxidants, quercetin and catechin, were stabilized through the complexation with cyclodextrin to increase heat and pH stabilities. Comparison of inclusion complex formabilities of quercetin and catechin with ${\alpha}-,\;{\beta}-$, and ${\gamma}-CDs$ revealed ${\beta}-CD$ to be the most suitable result. Optimal molar mixing ratio of ${\beta}-CD$ and quercetin or catechin for inclusion complex formation was found to be 1 : 1. Inclusion complexation was confirmed using differential scanning calorimetry. Solubility of ${\beta}-CD-antioxidant$ inclusion complexes increased compared with native antioxidants, Stability against temperature and pH of ${\beta}-CD-antioxidant$ inclusion complex analyzed revealed antioxidant activities of ${\beta}-CD-quercetin$ and catechin inclusion complexes have higher stabilization compare to raw quercetin and catechin. Peroxide value of linoleic acid dissolved in water decreased substantionally after using ${\beta}-CD-quercetin$ inclusion complex. ${\beta}-CD-antioxidant$ inclusion complex can be used effectively as a fresh-food preservative.

• Proceedings of the Botanical Society of Korea Conference
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• 1995.06a
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• pp.79-90
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• 1995

Production of a cardiac glycoside, digoxin, by 12$\beta$-hydroxylation from digitoxin was studied in plant cell suspension cultures of Digitalis lanata. In order to increase the conversion yield, various culture conditions including immobilization were investigated and optimized. Since digoxin was released in the medium temporarily and converted further into a glucosylated product, deacetyllanatoside C, in situ adsorption of digoxin was employed to recover the product continuously. Amberlite resin XAD-8 showed the best adsorption characteristics for digoxin among the examined resins, and an integrated process was developed to increase the productivity. In addition, it was found that the utilization of $\beta$-cyclodextrin to entrap digoxin during the culture enhanced the biotransformation yield significantly.

• Food Engineering Progress
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• v.13 no.1
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• pp.1-7
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• 2009

Fermented functional onion juice was developed using lactic acid bacteria as a fermentation starter of onion. From the preliminary studies, we selected the bacterium KC-007 (named as Pediococcus pentosaceus based on morphological and physiological characteristics, carbon utilization pattern, and molecular genetic characteristics) as a fermentation starter. The optimum recipe of functional fermented onion juice based on manufacturing process and sensory evaluation were determined as 27% of fermentation liquer, 27% of apple juice, 3.7% of HFCS, 1.86% of $\beta$-cyclodextrin, 0.9% of oligosaccharide, 0.2% of apple flavor, 0.09% of citric acid, and 39.25% of water.