• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.1
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• pp.35-40
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• 2000

The effect of levanheptaose produced by levanase from Streptomyces sp. 366L on principle intestinal microflora was investigated. The reaction product, levanheptaose, was used as a carbon source for various intestinal microflora. As a results, Bifidobacterium adolescentis, Lactobacillus acidophilus, and Eubacterium limosum grew effectively in the in vitro experiment, whereas Clostridium perfringens, E. coli, and Staphylococcus aureus did not. Therefore levanheptaose seems to promote selectively the growth of B. adolescentis and L. acidophilus. In the in vivo experiment, the effect of levanheptaose on the growth of intestinal microflora, $\beta$-fructosidase activity, pH, and butyrate concentration were examined in rats. Apparently, the number of fecal Bifidobacteria, the amount of butyrate, and $\beta$-fructosidase activity were increased, whereas total aerobes and pH were reduced in rats fed by levanheptaose diets, compared with those of control diets. We concluded that those effects may be beneficial in improving gastrointestinal health.

• Korean Journal of Microbiology
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• v.35 no.2
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• pp.153-157
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• 1999

The effececl of levanoclaose produced by levanase Croni Pseuc/olol~~o!!n.s sp. K-52 on pnnciple inlesimal microflorawas investigated. The reaction product, levanoctaose, was used as a carbon source for various intestinalmicroflora. Especially. Bijidobacteriulolr~ adolescentis and Lnctohaciilrrs ocidophilus grew effectively in vitroexpeiiments, whereas Clostridiunz per.frilol~gerzs, Bactetvid,~ngilis, Eschericlzin. coli, and Stnplzylococcus nureirsdid not. Therefore, levanoctdose seemed to proinole selectively the growth ol" B. ndo1escenti.r and L. acidol~hi-/us. In Lhe in viva experiments, the effects of levanoctaose on inlestinal nucroflora were examined on heirgrowth. $\beta$-fri~ctosidase acliviiy. and butyrate concenuation in rats. Appuently, die number of fecal Bifidobacteria.the amount of bulyrate, and $\beta$-hctosidase activity were increased, whereas total aerobes 'and pH werereduced in rals Eed leviu~octaose diets, cornpxed with hose of the control diets. We concluded hat those effecismay be beneficial in improving gastrointestinal health.astrointestinal health.

• Proceedings of the Zoological Society Korea Conference
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• 1996.10a
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• pp.227.2-227
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• 1996

No Abstract, See Full Text

• Journal of Plant Biology
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• v.35 no.1
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• pp.91-95
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• 1992

Changes of contents of reducing sugar and sucrose and activities of sucrose-phosphate synthase, sucrose synthease and invertase from the leaves of barley (Hordeum vulgare L. cv. Chalssal) seedlings grown at $4^{\circ}C$ were investigated, and the property of acid invertase were also examined. In the seedlings grown at $4^{\circ}C$ for 3 days, the contents of reducing sugar and sucrose were increased to 1.3 and 2.4 times, respectively. Activity of acid invertase was decreased markedly by cold treatment while the activities of sucrosephosphate synthase, sucrose synthase, and alkaline invertase were not changed. In acid phosphatase purified partially by ammonium sulfate fractionation and DEAE-Sephacel column chromatography, the $K_m$ value for sucrose was 9.5 mM and the optimum pH and temperature was 5.5 and $35^{\circ}C$ respectively. This enzyme was supposed to be ${\beta}-fructosidase$ by studies on the substrate specificity and the molecular weight was estimated to be 63 Kd by Sephadex G-200 gel chromatography.graphy.

• Korean Journal of Food Science and Technology
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• v.11 no.4
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• pp.283-290
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• 1979

Partially purified ${\beta}-fructosidase$ (inulase) from Kluyveromyces fragilis was immobilized on Tygon tube and aminoethyl-cellulose, respectively and both preparations were characterized. Silanization of Tygon tube in chloroform at $65^{\circ}C$ and treatment with 10 % glutaraldehyde were critical for the immobilization of inulase on Tygon tube, while 2 % glutaraldehyde was effective for the immobilization on aminoethyl-cellulose. The derivative of Tygon tube showed 11.5 units of inulase activity per g of dried matrix with retention of 22.5 % of original activity against inulin, whereas one of aminoethyl-cellulose showed 39.3 units per g of dired matrix with 53.4 % of retention. Studies of enzyme stability, pH and temperature dependences, and $K_m$ values are presented for inulase and invertase activities of both immobilized enzymes.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.655-659
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• 2000

A 11.5-kb DNA fragment containing an endo-inulinase gene was cloned from Xanthomonas oryzae #5. It contained a single open reading frame of 3,999bp, encoding a polypeptide composed of signal peptide of 32 amino acids and mature protein of 1,301 amino acids. From the comparison of amino acids sequences with fructan hydrolases, inulinase, levanase and CFTase, the sequence of the endo-inulinase had highly homology of 72% with CFTase of B. circulans, and six highly conserved regions including the ${\beta}-fructosidase$ motif were found.