• Title/Summary/Keyword: Maltooligosaccharides

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Enzymatic Hydrolysis of Korean Ginseng Starch and Characteristics of Produced Maltooligosaccharides

  • Kim, Na-Mi;Lee, Jong-Soo;Lee, Byung-H.
    • Journal of Ginseng Research
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    • v.24 no.1
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    • pp.41-45
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    • 2000
  • Maltooligosaccharides were produced from ginseng starch by hydrolysis of $\alpha$-amylase. And it was investigated that physicochemical properties and intestinal bacteria growing effort of maltooligosaccharides. The optimum level of the ginseng maltooligosaccharides was produced when 10% ginseng starch was hydrolyzed with 50 unit of Amano A $\alpha$-amylase per gram starch at 85。C for 24h. Viscosity and water holding capacity of the ginseng maltooligosaccharides were 37.7 cps at 20。C and 110.1% at 75% relative humidity, respectively. The ginseng maltooligosaccharides enhanced the growth of Bifidobaterium infantis.

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Production and Property of Maltooligosaccharide by Bacillus cereus LAM 1072 with Response Surface Methodology (반응표면분석에 의한 Bacillus cereus IAM 1072의 말토올리고당 생산 및 특성)

  • 이명열;강태수
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.27 no.4
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    • pp.639-647
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    • 1998
  • This study was carried out to produce the maltooligosaccharides directly from the culture medium containing high concentration of soluble starch as carbohydrate source by Bacillus cereus IAM 1072. Optimum conditions for the production of maltopentaose and maltooligosaccharides were predicted as 10.62 and 10.92 in C/N ration, 115.74 and 116.51 rpm in agitation speed, 30.19 and 30.9$0^{\circ}C$, respectively. And at these conditions, products of maltopentaose and maltooligosaccharides were 23.23 and 50.33g/L, respectively. From the results of continuous culture for maltopentaose, the productivity increased up to 6.9 times, showing 6.6g/L/hr compared with 0.96g/L/hr batch culture. Maltopentaose showed lower sweetness at 3% concentration representing 1/5 of that sugar. Also, swelling power of maltooligosaccharides was reached to the same point with sugar after fermentation.

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Chromatographic Separation of Maltopentaose from Maltooligosaccharides

  • Lee, Jae-Wook;Kwon, Tae-Ouk;Moon, Il-Shik
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.8 no.1
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    • pp.47-53
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    • 2003
  • An experimental study on the chromatographic separation of maltopentaose from a mixture, including glucose, maltose, maltotriose, and maltopentaose, was carried out in a nonionic polymeric sorbent column while varying the operating conditions, such as the solution pH, buffer contents, and isopropyl alcohol (1PA) concentration. Unlike the pH and buffer contents, the IPA concentration had a Significant impact on the single component chromatograms for maltopentaose. The retention times of the maltooligosaccharides with the nonionic polymeric sorbent Sp207 were in the following order: glucose < maltose < maltotriose < maltopentaose. From the experimental binary, ternary, and quaternary chromatograms, gradient chromatographic separation with a changing IPA concentration as a function of time was required to obtain high-purity maltopentaose and reduce the elution time.

Purification and Characterization of Branching Specificity of a Novel Extracellular Amylolytic Enzyme from Marine Hyperthermophilic Rhodothermus marinus

  • Yoon, Seong-Ae;Ryu, Soo-In;Lee, Soo-Bok;Moon, Tae-Wha
    • Journal of Microbiology and Biotechnology
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    • v.18 no.3
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    • pp.457-464
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    • 2008
  • An extracellular enzyme (RMEBE) possessing ${\alpha}-(1{\rightarrow}4)-(1{\rightarrow}6)$-transferring activity was purified to homogeneity from Rhodothermus marin us by combination of ammonium sulfate precipitation, Q-Sepharose ion-exchange, and Superdex-200 gel filtration chromatographies, and preparative native polyacrylamide gel electrophoresis. The purified enzyme had an optimum pH of 6.0 and was highly thermostable with a maximal activity at $80^{\circ}C$. Its half-life was determined to be 73.7 and 16.7 min at 80 and $85^{\circ}C$, respectively. The enzyme was also halophilic and highly halotolerant up to about 2M NaCl, with a maximal activity at 0.5M. The substrate specificity of RMEBE suggested that it possesses partial characteristics of both glucan branching enzyme and neopullulanase. RMEBE clearly produced branched glucans from amylose, with partial ${\alpha}-(1{\rightarrow}4)$-hydrolysis of amylose and starch. At the same time, it hydrolyzed pullulan partly to panose, and exhibited ${\alpha}-(1{\rightarrow}4)-(1{\rightarrow}6)$-transferase activity for small maltooligosaccharides, producing disproportionated ${\alpha}-(1{\rightarrow}6)$-branched maltooligosaccharides. The enzyme preferred maltopentaose and maltohexaose to smaller maltooligosaccharides for production of longer branched products. Thus, the results suggest that RMEBE might be applied for production of branched oligosaccharides from small maltodextrins at high temperature or even at high salinity.

Recombinant Expression and Characterization of Thermoanaerobacter tengcongensis Thermostable $\alpha$-Glucosidase with Regioselectivity for High-Yield Isomaltooligosaccharides Synthesis

  • Zhou, Cheng;Xue, Yanfen;Zhang, Yueling;Zeng, Yan;Ma, Yanhe
    • Journal of Microbiology and Biotechnology
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    • v.19 no.12
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    • pp.1547-1556
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    • 2009
  • A novel thermostable $\alpha$-glucosidase (TtGluA) from Thermoanaerobacter tengcongensis MB4 was successfully expressed in E. coli and characterized. The TtgluA gene contained 2,253 bp, which encodes 750 amino acids. The native TtGluA was a trimer with monomer molecular mass of 89 kDa shown by SDS-PAGE. The purified recombinant enzyme showed hydrolytic activity on maltooligosaccharides, p-nitrophenyl-$\alpha$-D-glucopyranide, and dextrin with an exotype cleavage manner. TtGluA showed preference for short-chain maltooligosaccharides and the highest specific activity for maltose of 3.26 units/mg. Maximal activity was observed at $60^{\circ}C$ and pH 5.5. The half-life was 2 h at $60^{\circ}C$. The enzyme showed good tolerance to urea and SDS but was inhibited by Tris. When maltose with the concentration over 50 mM was used as substrate, TtGluA was also capable of catalyzing transglycosylation to produce $\alpha$-1,4-linked maltotriose and $\alpha$-1,6-linked isomaltooligosaccharides. More importantly, TtGluA showed exclusive regiospecificity with high yield to produce $\alpha$-1,6-linked isomaltooligosaccharides when the reaction time extended to more than 10 h.

Preparation Mechanism of Glycoprotein by Periodate-oxidized Soluble Starch and Maltooligosaccharides (과요오드산 산화당에 의한 인공단백질의 조제 메카니즘)

  • Ann, Yong-Geun
    • Korean Journal of Food Science and Technology
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    • v.31 no.2
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    • pp.482-487
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    • 1999
  • Periodate-oxidized soluble starch and maltohexaose reacted with ${\alpha}-NH_2$ group of free amino acids and ${\varepsilon}-NH_2$ group of peptidyl lysine. The result shows that periodate-oxidized soluble starch and maltooligosaccharides reacted with protein and formed Schiff base between CHO group of oxidized sugar and ${\varepsilon}-NH_2$ group of surface lysine of protein molecule. Carbon and hydrogen composition of sweet potato ${\beta}-amylase$ modified with oxidized soluble starch increased and it's nitrogen composition decreased. Carbohydrate contents of sweet potato ${\beta}-amylase$ modified with oxidized soluble starch were 13.2% (pentamer), 13.4% (monomer), and with oxidized maltohexaose were 9.7% (pentamer), 9.3% (monomer) by $phenol-H_2SO_4$ method. Alpha-amino group of N-terminal, and ${\varepsilon}-NH_2$ group of lysine, of sweet potato ${\beta}-amylase$ were reacted with oxidized soluble starch by dinitrophenylation were 70% (pentamer), 73% (monomer) and 33% (pentamer), 26% (monomer), respectively, in comparison with native enzyme.

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Enhancement of enzymatic activity of ${\beta}-cyclodextrin$ glucanotransferase from Bacillus firmus var. alkalophilus by site-directed mutagenesis

  • Lee, Gwang-U;Sin, Hyeon-Dong;Lee, Yong-Hyeon
    • 한국생물공학회:학술대회논문집
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    • 2001.11a
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    • pp.656-659
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    • 2001
  • Cyclodextrin glucanotransferase (CGTase) (EC 2.4.1.19) use starch to produce cyclic maltooligosaccharides (cyclodextrins, CDs) which are of interest in various applications. To obtain a novel CGTase having high CD-forming activity, ${\beta}-cyclodextrin$ glucanotransferase $({\beta}-CGTase)$ from Bacillus firmus var. alkalophilus was modified through site-directed mutagenesis and constructed five mutants, H59T, H59Q, Y96M, 9O-PPI-93, and ${\Delta}(148-154)D$, respectively. Y96M and ${\Delta}(148-154)D$ showed much higher level of conversion yields of starch into CDs from 28.6% to about 39% compared to wild-type ${\beta}-CGTase$, respectively, but 90-PPI-93 maintained similar convesion yields of starch to CDs. And their ${\beta}-CD$ ratios to total CDs were not changed and maintained, and convesion yields to linear maltooligosaccharides of all mutants were not changed significantly. These results indicates that five mutations of ${\beta}-CGTase$ from Bacillus firmus var. alkalophilus appears to be important roles for increase of overall CD production rather than change of its product specificity, especially.

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Purification and Characterization of Alkali-resistant Amylases from Pseudomonas sp. (Pseudomonas sp.로부터 알칼리내성 amylase의 정제 및 특성 확인)

  • Lee, Jeong-Eun;Jhon, Deok-Young
    • Korean Journal of Food Science and Technology
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    • v.40 no.1
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    • pp.70-75
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    • 2008
  • Two extracellular amylase isozymes were purified and characterized from alkalophilic Pseudomonas sp. KFCC 10818 for the production of maltooligosaccharides. The molecular weights of the homogeneous proteins were 50 kDa and 75 kDa, respectively. The 50 and 75 kDa amylases showed optimum temperatures at 35 and $40^{\circ}C$, respectively. The optimum pH of the enzymes ranged from pH 6-8, and the enzymes were resistant to an alkaline condition of pH 12. Via the enzyme's actions, the final products from maltooligosaccharides or soluble starch were maltose and maltotriose. Calcium was a potent activator of the 50 kDa amylase. Finally, the N-terminal amino acid sequences of the 50 and 75 kDa amylases were QTVPKTTFV and DTVPGNAFQ, respectively.

Changes in Characteristics of Brown Rice (Goami) Alcohol Fermentation By-Product by Cellulase (Cellulase처리에 따른 현미(고아미) 알코올발효 부산물의 특성 변화)

  • Woo, Seung-Mi;Jang, Se-Young;Park, Nan-Yong;Kim, Tae-Young;Yeo, Soo-Hwan;Kim, Sang-Burm;Jeong, Yong-Jin
    • Food Science and Preservation
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    • v.15 no.1
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    • pp.99-104
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    • 2008
  • To utilize non-heat treated alcoholic by-products of brown rice (Goami) as food sources, the quality characteristics changes according to the treatment conditions of cellulase were evaluated. Results showed that the increase of hydrolysis temperature correspondingly increased the soluble solids and total sugar amounts in the by-products of Goami, and total dietary fiber amount was found to be around 0.67% Reducing sugar concentration was the highest at the hydrolysis temperature of $70^{\circ}C$. Maltooligosaccharides amounts were detected to be the highest at the hydrolysis temperature of $80^{\circ}C$ and were also, maltopentose and maltopentose were found. In the soluble solid, total dietary fiber, reducing sugar and total sugar according to the cellulase concentration, the content of hydrolysates with enzyme were higher than control, and the content of hydrolysates with enzyme was similar (6.30 and 0.69% 3,600 and 5,500 mg% respectively). The content of maltooligosaccharides was increased with the increase of enzyme concentration, and the content was similar at more than 0.6%(w/w) of enzyme concentration. The soluble solids and total dietary fiber by hydrolysis time were found to be 6.25% and 0.70%, respectively at more than 60 min. of hydrolysis. The content of reducing sugar, total sugar and maltooligosaccharides were increased with the increase of hydrolysis time, and the content was similar at more than 120min. of hydrolysis (3,800, 5,680 and 1,950 mg% respectively). Based upon these results, the byproducts of Goami are expected to be valuable as various food sources showing the highest dietary fiber and maltooligosaccharides contents by the hydrolysis at $80^{\circ}C$ for 120 min. with the addition of 0.6%(w/w) of cellulase.