• Title/Summary/Keyword: oligosaccharides(G2∼G7)

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Effect of Chitosan Oligosaccharides on Cholesterol Level and Antioxidant Enzyme Activities in Hypercholesterolemic Rat (고콜레스테롤 식이에 있어 키토산 올리고당이 체내 콜레스테롤농도 및 항산화효소 활성에 미치는 영향)

  • Kim, Kil-Nam;Joo, Eun-Sook;Kim, Kyu-Il;Kim, Se-Kwon;Yang, Hyun-Pyl;Jeon, You-Jin
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.34 no.1
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    • pp.36-41
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    • 2005
  • Effect of chitosan oligo saccharides (COS) on the level of serum lipids, antioxidant enzyme activities and lipid peroxidation was investigated in rats fed with high cholesterol diet for 4 weeks, The rats were divided into three experimental groups that is, high cholesterol diet group (0.5% cholesterol; control). high cholesterol diet and 1.0% or 2.0% COS-supplemented groups (COS I , COS II). Serum total cholesterol, LDL-cholesterol and triglyceride level were significantly decreased and relative HDL-cholesterol level in total cholesterol significantly increased in COS II group. Liver TBARS level and activities of SOD and catalase of COS I were also significantly reduced. These results suggest that supplement of chitosan oligosaccharides reduce levels of serum cholesterol and reduce oxidative damage by activating hepatic antioxidative defense system in rats fed with high cholesterol diets.

Improving Effects of Fructooligosaccharide and Isomaltooligosaccharide Contained in Sponge Cakes on the Constipation of Female College Students (스폰지 케이크에 함유된 프락토올리고당과 이소말토올리고당이 여대생의 변비개선에 미치는 효과)

  • 이미라;이경애;이선영
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.32 no.4
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    • pp.621-626
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    • 2003
  • The aim of this study was to evaluate the effects of 40% sucrose replacement with oligosaccharides (fructo- orisomalto-) in sponge cakes. The 18 female college students were divided into two groups; fructooligosaccharide sponge cake group (FOS) and isomaltooligosaccharide sponge cake group (IMOS). In each group, the subjects received 50 g/d of sponge cake which contained about 8 g oligosaccharides for 2 weeks. The results were as follows: (1) Frequency of stool evacuation tended to increase after 1 week and significantly increased after 2 weeks in both groups. (2) Shape and color of stool did not change in FOS group but the IMOS group showed significant improvement. (3) The stool amounts per defecation were not significantly different in both groups. (4) The time of defecation decreased 50% after 1 week in FOS group and tended to decrease gradually in IMOS group. (5) Consistency of stool was significantly decreased after 1 week in both groups and continuously decreased until 2 weeks. (6) Effort for evacuation and comfort feeling after evacuation were significantly improved only in IMOS group after 2 weeks. (7) Gastrointestinal complaints concerning diarrhea, abdominal pains, nausea, flatulence, loss of appetite and weight and bloating were apparent. The symptoms such as abdominal pains, flatulence, and bloating in FOS group lasted for 2 weeks. However, the complaints appeared only during two or three days in IMOS group. In conclusion, our results suggest that isomaltooligosaccharide was more effective than fructooligosaccharide for preventing constipation because isomaltooligosaccharide worked safely in gastrointestinal lumen.

A Simple Enzymatic Method for Quantitation of 2'-Fucosyllactose

  • Seydametova, Emine;Shin, Jonghyeok;Yu, Jiwon;Kweon, Dae-Hyuk
    • Journal of Microbiology and Biotechnology
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    • v.28 no.7
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    • pp.1141-1146
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    • 2018
  • 2'-Fucosyllactose (2'-FL) is one of the most important human milk oligosaccharides and has several health benefits for infants. The levels of 2'-FL in breast milk or samples from other sources can be quantified by high-performance liquid chromatography. However, this method cannot be used for simultaneous detection of the target compound in numerous samples. Here, we developed a simple method for quantifying 2'-FL in a microplate format. The method involves two steps: (i) release of $\text\tiny{L}$-fucose from 2'-FL by ${\alpha}$-(1-2,3,4,6)-$\text\tiny{L}$-fucosidase and (ii) measurement of NADPH formed during the oxidation of $\text\tiny{L}$-fucose by $\text\tiny{L}$-fucose dehydrogenase. This method enables measurement of up to 5 g/l 2'-FL in 50 min using a 96-well microplate. The efficiency and simplicity of the proposed method make it suitable for the analyses of a large number of samples simultaneously.

Pseudomonas sp. CB-33이 생산하는 $\beta$-Xylosidase의 특성

  • Yu, Jin-Whan;Kim, Hyun-Ku;Kim, Chi-Kyung;Lim, Jai-Yun
    • Microbiology and Biotechnology Letters
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    • v.24 no.2
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    • pp.197-205
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    • 1996
  • The $\beta$-xylosidase was purified 99- fold from the culture supernatant of Pseudo onas sp. CB-33 by ammonium sulfate precipitation, PEI precipita- tion, DEAE-Sephadex column chromatography, Sephadex G-75 gel filtration chromatography and preparative disc gel electrophoresis. Molecular weight of the enzyme was estimated to be 44,000 by SDS polyacrylamide gel electrophoresis. The enzyme has a pH optimum for activity at 7.0 and is stable over pH 6.5-9.0. The optimal temperature of the enzyme was 45$\circ$C, and its enzymatic activity was completely inactivated at 55$\circ$C for 30 min. Km value of the enzyme for p-nitrophenyl-$\beta$-D-xylopyranoside was calculated to be 4.6 mM. The effect of various reagents on the $\beta$-xylosidase activity was investigated. The enzyme activity was completely inhibited by Hg$^{2+}$, Cu$^{2+}$ and Zn$^{2+}$. The $\beta$-xylosidase was inactivated by tryptophan-specific reagent, N-bromosuccinimide and tyrosine-specific reagent, iodine. The enzyme could degrade xylo-oligosaccharides to xylose and the enzyme was competitively inhibited by xylose. The $\beta$-xylosidase and endoxylanase from Psedomonas sp. CB-33 hydrolized xylan synergically. The purified enzyme also showed $\alpha$-L-arabinofuranosidase activity.

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The Effect of Oligosaccharides on Ethylene Production in Mung Bean (Vigna radiata W.) Hypocotyl Segments

  • Choy, Yoon-Hi;Lee, Dong-Hee;Lee, June-Seung
    • Journal of Plant Biology
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    • v.39 no.4
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    • pp.295-300
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    • 1996
  • The physiological effects of oligogalacturonic acid (OGA:D. P. 6-7), a product of acid hydrolysis of polygalacturonic acid (PGA), on ethylene biosynthesis in mung bean (Vigna radiata W.) hypocotyl segments was studied. Among PGA, OGA and monogalacturomic acid (MGA), only OGA stimulated ethylene production in mung bean hypocotyl segments, and the most effective concentraton of OGA was 50$\mu\textrm{g}$/mL. Time course data indicated that this stimulatiion effect of OGA appeared after 90 min incubation period and continued until 24 h. When indol-3-acetic acid (IAA) and 1-aminocyclopropane-1-carboxylic acid (ACC) were treated with OGA to investigate the mechanism of OGA on ethylene production, they did not show synergistic effects on ethylene production. The stimulation of ethylene production by OGA was due to the increase of in vivo ACC synthase activity, but OGA treatment had no effect of in vivo ACC oxidase activity. The effect of aminoethoxy vinyl glycine (AVG) and Co2+, the inhibitor of ethylene synthesis, was siminished a little by the OGA, but the treatment of Ca2+, known to increase ACC, with OGA did not increase the ethylene production, this effect seems to be specific for Ca2+ because other divalent cation, Mg2+, did not show the inhibition of OGA-indyuced ethylene production. It is possible that the OGA adopts a different signal transduction pathway to the ethylene bioxynthesis.

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Purification and characterization of the chitinase from Bacillus subtilis JK-56 (Bacillus subtilis JK-56이 생산하는 chitinase isozyme의 정제와 특성 규명)

  • 전홍기;김낙원;정영기
    • Journal of Life Science
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    • v.12 no.1
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    • pp.77-86
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    • 2002
  • Chitin, a $\beta$-1,4 polymer of N-acetyl-D-glucosamine, is one of the most abundant organic compounds in nature. Chitinase (EC 3.2.1.14) is an enzyme that degrades chitin to chito-oligosaccharides, diacetyl rhitobiose and N-acetyl-D-glucosamine. An extracellular chitinase-producing bacterial strain was isolated from soil and named to as Bacillus subtilis JK-56. Optimum culture condition of B. subtilis JK-56 for the production of chitinase was 1% chitin, 0.5% polypepton, 0.1% KCl, 0.05% MnS $O_4$.4$H_2O$, 37$^{\circ}C$, initial pH 7.0 and 40 hour culture time. When B. subtilis JK-56 was grown in the optimum medium, one major active band and two minor active bands were detected by native-PAGE and active staining of the gel. Among them, the major band was purified from the culture supernatant by 70% ammonium sulfate precipitation and native-PAGE with BIO-RAD Model 491 Prep-Cell and named as Chi-56A. Its molecular weight was estimated to be 53kDa monomer and the isoelectric point (pI) was pH 4.3. The pH and temperature for the optimum activity of Chi-56A were pH 6.0 and $65^{\circ}C$, respectively. Chi-56A was stable up to $65^{\circ}C$ and in alkaline region. Its $K_{m}$ value for colloidal chitin was 17.33g/L. HPLC analysis of the reaction products confirmed that Chi-56A was an exo type chitinase.e.

Differential Induction of Protein Expression and Benzophenanthridine Alkaloid Accumulation in Eschscholtzia californica Suspension Cultures by Methyl Jasmonate and Yeast Extract

  • Cho, Hwa-Young;Rhee, Hong-Soon;H. Yoon, Sung-Yong;Park, Jong-Moon
    • Journal of Microbiology and Biotechnology
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    • v.18 no.2
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    • pp.255-262
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    • 2008
  • Methyl jasmonate (MJ) and yeast extract (YE) induce protein expression and benzophenanthridine alkaloid accumulation in Eschscholtzia californica suspension cell cultures. One hundred ${\mu}M$ MJ primarily induced dihydrosanguinarine $(509.0{\pm}7.4mg/l)$ ; 0.2g/l YE induced sanguinarine $(146.8{\pm}3.8mg/l)$ and an unknown compound. These results occur because dihydrobenzophenanthridine oxidase (DHBO) is induced by YE and not by MJ. YE and chitin (CHI) had similar effects on sanguinarine production and DHBO expression. Differential induction of secondary metabolites was shown in E. californica suspension cultures and the expression of proteins confirmed the metabolite results. Furthermore, treatment by various oligosaccharides helped us to understand the elicitation effect of YE in signal transduction pathways.

Agronomic Traits of Soybean Breeding Lines with Low Stachyose and Raffinose Contents (Stachyose 및 Raffinose 저함량 콩 선발계통의 농업적 형질)

  • Ha, Do Su;Moon, Jin Young;Choi, Sang Woo;Shim, Sang In;Kim, Min Chul;Chung, Jong Il
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.62 no.2
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    • pp.143-148
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    • 2017
  • Soybean [Glycine max (L.) Merr.] seed is an important dietary source of protein, oil, carbohydrates, isoflavones, and other nutrients for humans and animals. Raffinose and stachyose are the main antinutritional factors in soybean seed. They are carbohydrates belonging to the raffinose family of oligosaccharides, which are not readily digested in humans and cause flatulence or diarrhea. The genetic reduction of the raffinose and stachyose contents in mature soybean seeds will improve the nutritional value of soybean. The objective of this research was to evaluate agronomic traits with 10 $F_6$ strains selected from breeding populations derived from a cross among seven parents. The contents of raffinose and stachyose in mature seeds were detected by high-performance liquid chromatography. Agronomic traits such as flower color, flowering date, harvesting date, lodging, plant height, seed coat color, hilum color, 100 seed weight, and yield were evaluated. Ten intermediate parents showed low raffinose and stachyose contents. The intermediate parent 883-1 had a small seed size, six intermediate parents (15A1, 15D1, RS-5, RS-33, RS-64, and RS-70) had a medium seed size, and two intermediate parents (14G20 and RS-21) had a large seed size. The intermediate parent RS-21 had a black seed coat and a green cotyledon. Four intermediate parents (883-1, 14G20, RS-5, and RS-21) had elite agronomic traits. The new intermediate parents developed through this study will be used to develop improved soybean cultivars with low contents of raffinose and stachyose.

Isolation and Cultivation of Microorganism Producing Levanheptaose from Levan (Levan으로부터 Levanheptaose를 생산하는 미생물의 분리 및 배양)

  • Lim, Young Soon;kang, Soo Kyung;Kang, Eun Jung;Lee, Tae Ho
    • Korean Journal of Microbiology
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    • v.34 no.1_2
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    • pp.37-42
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    • 1998
  • The microorganisms degrading levan were screened from soil. The isolated strain produced levanase releasing single oligosacchride from levan. The optimum cultural medium for levanase production (g/l) was composed of 0.5% levan, 0.1% $K_2HPO_4$, 0.05% NaCl, 0.3% $NaNO_3$, 0.3% yeast extract (pH 8.0). The cultivation for levanase production was carried out in 500 ml shaking flask containing 50 ml of the optimum medium at $30^{\circ}C$ on a reciprocal shaker, and the highest levanase production was observed after 54 hours of cultivation. The levanase hydrolyzed levan into single oligosaccharide. The product purified by chilled EtOH precipitation and gel filtration was detected as a single peak on HPLC analysis. The oligosaccharides formed by enzyme reaction was identified as levanheptaose (DP7) by HPLC and by ESI-MASS.

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Purification and Characterization of Exo-xylanase from Escherichia coli Cells Harboring the Recombinant Plasmid pMGl (재조합 균주 Escherichia coli가 생산하는 Bacillus stearothermophilus Exo-xylanase의 정제 및 특성)

  • 문애란;최용진
    • Microbiology and Biotechnology Letters
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    • v.20 no.5
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    • pp.574-582
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    • 1992
  • Exo-xylanase encoded by the xylA gene of Bacillus stearothermoPhillus was produced from Escherichia coli ]M109 carrying a recombinant plasmid pMGL Synthesis of the enzyme was observed to be cell-associated, and about 94% of the enzyme synthesized was located in the cytoplasmic region. The maximum production was attained when the E. coli strain was grown at $37^{\circ}C$ for 8 hours on the medium containing 0.5% fructose, 1.0% tryptone, 1.0% sodium chloride, and 0.5% yeast extract. The exo-xylanase was purified to homogeneity using a combination of salting out with ammonium sulfate, DEAE-Sepharose CL-6B ion exchange chromatography, Sephadex G-IOO gel filtration, and Sephadex G-150 gel filtration. The' purified enzyme was most active at pH 6.0 and $45^{\circ}C$. $Ca^{2+}$ and $Co^{2+}$ activated the exo-xylanase activity by about 20% while $Ag^{2+}$, $Fe^{2+}$, $Mg^{2+}$ and $Zn^{2+}$ inhibited the enzyme activity by up to 60%. The $K_m$, value on p-nitrophenyl-$\beta$-D-xylanopyranoside was 2.75 mM. The enzyme had a pI value of 4.7. The estimated molecular weight of the native protein was 200,000 daL SDS-polyacrylamide gel electrophoresis analysis suggested that the native enzyme was a trimer composed of three identical 66,000 da!. polypeptides. The purified enzyme efficiently converted all the xylo-oligosaccharides tested to xylose. It was also confirmed that the enzyme split xylans in an exo-manner even though the degree of hydrolysis was fairly low. The xylanolytic enzyme was, therefore, classified to be one of the few bacterial exo-xylanases lacking transferase activity.

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