• 제목/요약/키워드: glucose isomerase

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Arthrobacter sp. L-3로부터 Glucose Isomerase의 생산 (Production of Glucose Isomerase from Arthrobacter sp. L-3)

  • 이은숙;남궁석
    • 한국식품영양학회지
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    • 제10권1호
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    • pp.117-121
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    • 1997
  • Arthrobacter sp. L-3로부터 glucose isomerase의 생산성을 검토하였다. 배지의 탄소원으로는 glucose와 xylose를 혼합해서 공급한 것이 효소 생산성이 가장 높았다. 질소원으로는 yeast extract가 가장 높은 효소 생산성을 나타내었다. Glucose isomerase의 생산성은 배양시간이 40시간일 때 가장 높게 나타났다.

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호알칼리성 Streptomyces sp. B-2의 Glucose Isomerase 생성조건 (Formation of Glucose Isomerase from Alkalophilic Streptomyces sp. B-2)

  • 이은숙
    • 동아시아식생활학회지
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    • 제7권1호
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    • pp.35-39
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    • 1997
  • Studies on the glucose isomerase produced by alkalophilic Streptomyces sp. B-2. Glucose Isomerase (E. C. 5.3.1.5) which reversibly catalyzes reaction between D-glucose and D-fructose was demonstrated in cell free extracts of alkalophilic Streptomyces sp. B-2 isolated form soil. The maximum enzyme activity was found at glucose concentration 4(g/$\ell$) , xylose concentration 6(g/$\ell$), magnesium ion 1.0(g/$\ell$), yeast extract concentration 2.0(g/$\ell$), peptone concentration 3(g/$\ell$).

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Arthrobacoer sp. L-3가 생성하는 Glucose Isomerase의 최적 생성조건 (Efficient Production of Glucose Isomerase from Atrhrobacter sp. L-3)

  • 이은숙
    • 동아시아식생활학회지
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    • 제7권1호
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    • pp.29-33
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    • 1997
  • The efficient production of glucose isomerase (G. I0.) produced form Arthrobacter sp. L-3 was studied. The optimum culture time of the enzyme was 40hr. The maximum enzyme activity was found at glucose concentration 1%. G. I. activity did not affect inoculum size. The glucose isomerase activity was strongly influenced by the addition of glucose.

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호알칼리성 Streptomyces sp.B-2에 의한 Glucose Isomerase의 정제 (Purification of Glucose Isomerase from ALkalophilic Streptomyces sp. B-2)

  • 이은숙;이준우
    • 동아시아식생활학회지
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    • 제10권5호
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    • pp.439-444
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    • 2000
  • 호알칼리성 방선균 Streptomyes sp. B-2를 Glucose Isomerse 생성을 위해 토양에서 분리했다. Glucose Isomerase(G.I)는 high fructose glucose syrup과 fructose의 생산을 위해서 식품 공업에서 아주 중요시되고 있는 효소이다. 호알칼리성 방선균 Streptomyces sp. B-2가 생성하는 glucose isomerase(G.I.)를 정제하였다. G.I.는 (NH$_4$)$_2$So$_4$분획, DEAE-cellulose, Sephadex G-200 chromatography하여 순수 분리 하였다. 순수분리된 G.I.는 electrophoresis에 의해 확인을 했다. SDS-acrylamide gel electrophoresis에 의해 정제된 효소는 single band를 보여주었다.

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방선균의 xylB 변이주에 의한 포도당 이성화효소의 생산

  • 주길재;이인구
    • 한국미생물·생명공학회지
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    • 제25권1호
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    • pp.75-81
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    • 1997
  • Streptomyces chibaensis J-59 did not grow in the culture medium containing only xylose or xylan as a carbon source, because it was defective in xylulokinase production; xylB mutant. S. chibaensis J-59 was able to produce xylanase and $\beta $-xylosidase as well as glucose isomerase. The glucose isomerase in S. chilbaensis J-59 was induced in the medium containing xylan or xylose which could be utilized as an inducer but not sa carbon and energy sources. So we tried to produce glucose isomerase whthout consumption of xylose or xylan as an inducer by using xylB mutant S. chilbaensis J-59. The optimum condition for the production of the glucose isomerase was attained in a culture medium composed of 1% xylan, 0.15% glucose, 1.5% corn steep liquor, 0.1% MaSO$_{4}$ $\CDOT $7H$_{2}$O, and 0.012% CoCL$_{2}$ $\CDOT $ 6H$_{2}$O(pH 7.0). The production of the enzyme reached to a maximum level when the bacteria were cultured for 42 h at 30$\circ $C. The enzyme production in a jar fermentor was increased twice as much as that in a flask culture.

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Arthrobacter sp. L-3이 생성하는 Glucose Isomerase의 정제 (Purification of Glucose Isomerase from Arthrobacter sp. L-3)

  • 방병호;남궁석
    • 한국식품영양학회지
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    • 제4권2호
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    • pp.155-160
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    • 1991
  • Authrobacter sp. L-3이 생성하는 glucose isomerase를 DEAE-cellulose column chromatography법으로 2단계 NaCl농도 구배로 용출함으로서 순수분리하였다. 이것이 SDS-acrylamide gel electrophoresis상에서 단일띠를 보임으로서 매우 잘 분리되었음을 알 수 있었다. Glucose isomerase의 Km값과 Vmax값이 각각 0.175M, 0.29로 얻어졌다. 한편, SDS-acrylamide gel electrophoresis와 Sephadex-G10050에 의한 gel filtration으로부터 분자량이 각각 42,000과 180,000으로 얻어져, 이 효소는 분자량이 42,500인 4개의 subunit로 구성되었음을 알 수 있었다.

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Isolation of Glucose Isomerase Hyperproducing Strain, Streptomyces sp. SM 805 and Its Enzymatic Properties

  • Kim, Hong-Rip
    • Journal of Microbiology and Biotechnology
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    • 제2권2호
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    • pp.78-84
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    • 1992
  • Streptomyces sp. No.8, which produced glucose isomerase was isolated from soil samples. The isolated strain, No.8, was identified as belonging to the Genus Streptomyces. A mutant strain, SM 805, showed the greatest ability to produce glucose isomerase. It was developed from the strain, No.8, by mutagenesis induced by NTG and UV treatment. The mutant strain, SM 805, produced about 7 times more glucose isomerase than the parental strain, No.8. This enzyme catalyzed the isomerization of D-xylose, D-glucose and D-ribose. It was inactive in the absence of metal ions, but was activated by the addition of $Mg^{2+}$ or $Co^{2+}$. The optimum temperature and pH for enzyme activity were $80^\circ{C}$ and pH 8.5, respectively. The enzyme was stable in a pH range of 6.0 to 10.0, and it was highly thermostable. There was no activity loss below $80^\circ{C}$, and even above $90^\circ{C}$ about 45% of its activity was retained. The reaction equilibrium was reached when about 53% fructose was present in the reaction mixture. Whole cells containing glucose isomerase from Streptomyces sp. SM 805 were immobilized by glutaraldehyde treatment. The resultant immobilized enzyme pellets showed a relatively long stability during the isomerizing reaction. The half-life of the immobilized enzyme during the operating was 45 days in the presence of 10mM $Mg^{2+}$.

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Streptomyces sp. K-53 균주로부터 생산된 xylanase와 glucose isomerase의 관계에 관한연구

  • 김정순;정태화;한문희
    • 한국미생물생명공학회:학술대회논문집
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    • 한국미생물생명공학회 1975년도 추계학술발표회
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    • pp.181.1-181
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    • 1975
  • 토양에서 분리한 glucose isomerase를 생성하는 Streptomyces속 균주중에서 xylanase 활성이 가장 높은 균주 Streptomyces sp. K-53을 xylan을 함유한 영양배지에서 배양하여 xylan에 의한 xylanase의 유도 과정과 xylan의 분해산물이 xylose를 이용하여 glucose isomerase를 생성하는 과정의 일연의 관계를 알아보기 위해서 몇가지 실험한 결과는 다음과 같다.(중략)

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Application of a Compatible Xylose Isomerase in Simultaneous Bioconversion of Glucose and Xylose to Ethanol

  • Chandrakant Priya;Bisaria Virendra S.
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제5권1호
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    • pp.32-39
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    • 2000
  • Simultaneous isomerisation and fermentation (SIF) of xylose and simultaneous isomerisation and cofermentation (SICF) of glucose-xylose mixture was carried out by the yeast Saccharomyces cerevisiae in the presence of a compatible xylose isomerase. The enzyme converted xylose to xylulose and S. cerevisiae fermented xylulose, along with glucose, to ethanol at pH 5.0 and $30^{\circ}C$. This compatible xylose isomerase from Candida boidinii, having an optimum pH and temperature range of 4.5-5.0 and $30-35^{\circ}C$ respectively, was partially purified and immobilized on an inexpensive, inert and easily available support, hen egg shell. An immobilized xylose isomerase loading of 4.5 IU/(g initial xylose) was optimum for SIF of xylose as well as SICF of glucose-xylose mixture to ethanol by S. cerevisiae. The SICF of 30 g/L glucose and 70 g xylose/L gave an ethanol concentration of 22.3 g/L with yield of 0.36 g/(g sugar consumed) and xylose conversion efficiency of $42.8\%$.

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Actinoplanes missouriensis KCTC 1780의 응집 균체에 의한 과당생산 (Production of High Fructose Syrup by Flocculated Actinoplanes missouriensis KCTC 1780)

  • 조정일
    • 한국식품영양학회지
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    • 제6권4호
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    • pp.268-275
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    • 1993
  • The whole cells of Actinoplanes missouriensis KCTC 1780 which produce glucose isomerase was immobillized by flocculation method for the effective production of high fructose syrup using packed-bed bioreactor system. Among the flocculation methods used In this study, the glucose Isomerase activity of flocculated cells using 5% polyethylenimmine and 0.2% glutaraldehyde was the highest as 46.3 unit, and the flocculant was 10.3g(wet weight) per 100m1 of broth, and the residual activity was 92.5%. In the batch operation of glucose isomerization using the flocculated cells, the optimum pH, temperature and isomerization ratio were 7.0, 75$^{\circ}C$ and 31%, respectively. The optimum concentration of Mg2+ which was activator on the glucose isomerization of flocculated cells was 0.1M, and glucose isomerase activity was increased by about 40% compared to none of Mg2+. In the packed-bed bioreactor system with 1.2 hour of residence time at 7$0^{\circ}C$, the reaction stability maintained until 96 hour without toss of activity, and the equilibrium was kept up to 120 hours of the operation.

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