• 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)

• 한국미생물생명공학회:학술대회논문집
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• 한국미생물생명공학회 1976년도 제8회 학술발표회
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• pp.190.3-190
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• 1976

본 균주가 생성하는 glucose isomerase에 관한 제성질에 대해서는 전보에 이미 발표한 바 있다. 금반에는 isomerase 생성에 있어서 제요인의 검토의 일환으로 비증식상에서 inducer로서 0.5％ Xylose를 첨가해 주었을 때의 효소생성능에 관하여 검토하였다.(중략)

• 한국미생물·생명공학회지
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• 제25권1호
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• pp.15-22
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• 1997

A bacterial strain J-59 was isolated from a humus soil, which produced simultaneously a thermostable glucose isomerase as well as xylanase. The morphological, cultural and physiological characteristics of the isoisomerase strain J-59 were detemined by the use of the media and methods described in International Streptomyces Project. The chemotaxonomic characteristics of the isolated strain J-59 were determined by the analysis of G+C molar % of DNA, diaminipimelic acid, composition of fatty acid and menaquinone. As the results of various examinations, the strain J-59 was identified to be Streptomyces chibaensis. This strain produced glucose isomerase intracellularly and xylanase extracellularly when grown in a medium containing xylan, but it was not able to utilize the xylose or xylan as a carbon source. The glucose isomerase of S. chibaensis J59 was highly thermostable, which retained more than 75% activity in the presence of Co$^{2+}$ at 80$\circ $C for 72 h.

• International Journal of Industrial Entomology and Biomaterials
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• 제17권2호
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• pp.189-195
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• 2008

The sequence of hydroxypyruvate isomerase gene was obtained in NCBI. In this study, the hydroxypyruvate isomerase gene of Bombyx.mori was identified and annotated with bioinformatics tools. The result was confirmed by RT-PCR, prokaryotic expression, mass spectrographic analysis and sub-cellular localization. The hydroxypyruvate isomerase cDNA comtains a 783bp ORF, and has 4 exons. The deduced protein has 260 amino acid residues with the predicted molecular weight of 29169.30 Da, isoelectric point of 6.10, and contains conserved PRK09997 and Hfi domains. The hydroxypyruvate isomerases of Nasonia vitripennis and Bombyx mori have a high homology. Through RTPCR analysis, we found that this transcript was present in testis, ovary, blood-lymph, fat body, midgut, silk gland and tuba Malpighii. This protein was located in cytoplasm through immunohistochemistry. We submitted the cloned gene under the accession number EU344910. The enzyme has been classified under accession number EC 5.3.1.22.

• 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 $42.8\%$.

• 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 $Mg^{2+}$.

• 한국미생물·생명공학회지
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• 제4권4호
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• pp.145-151
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• 1976

토양에서 분리한 glucose isomerase 생산균주 Streptomyces sp. K-14 (KFCC 35051)를 시험균주로 선정하여 몇가지 glucose isomerase 생산의 최적조건을 규명하여 다음의 결과를 얻었다. 1. 본 균주는 탄소원으로 xylose 대신 xylan에서도 glucose isomerase가 유도되며, xylan의 최적농도는 1~2%였다. 2. 유기태 질소원으로 corn steep liquor를 사용할때에 glucose isomerase 생산이 가장 양호하였고 무기태 질소는 거의 영향이 없었다. corn steep liquor의 최적농도는 1～2%였다. 3. 본균주의 효소생산에 무기이온으로 $Mg^{＋＋}$과 Co$^{＋＋}$만이 영향이 있었고 기타의 무기이온은 영향이 없었으며, 그 최적농도는 $MgSO_4$$7H_2O$로서 4.0mM이고 $CoSO_4$ㆍ$7H_2O$로서 1~2mM이였다. 4. 본 균주의 효소생산 최적pH는 7.0~7.5였다. 5. 밀기울 및 옥수수혜축을 사용한 효소생산 최적배지조성은 밀기울및 옥수수혜축 3%, 분말 corn steep liquor 2%, $MgSO_4$$7H_2O$ 0.1% 및 $CoSO_4$$7H_2O$ 0.012%이며, 최적 배양조건은 배지의 pH 7.0, 통기량 1.5~2$\ell$/min, 회전수 200rpm,배양온도 $30^{\circ}C$에서 약 40시간 배양하여 최대 효소활성을 나타내었다. 이상의 결과를 검토한바 Streptomyces sp. K-14(KFCC 35051) 균주는 glucose isomerase 생산을실용화하는데 적합한 균주라고 생각된다.

• 생명과학회지
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• 제14권4호
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• pp.636-643
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• 2004

김치에서 분리된 Lactococcus sp. JK-8 균주에 의해 생산되는 D-xylose isomerase를 17배 정제하여 물리 화학적인 특성을 조사하였다 D-Xylose isomerase의 N 말단 아미노산 서열을 결정한 결과 Ala-Tyr-Phe-Asn-Asp-Ile-Ala-Pro-Ile-Lys로 확인되었고 이것은 Lactococcus 속의 D-xylose isomerase와는 유사하지 않았다. 정제된 효소의 분자량은 gel filtration의 경우 180 kDa, subunit의 분자량은 SDS-PAGE에서 45 kDa으로 측정되었고 이 효소는 4개의 subunit으로 구성된 homotetramer였다. 최적 반응 pH는 pH 7부근이었고 pH 6∼8 사이에서 안정하였다. 최적 반응온도는 7$0^{\circ}C$였고 1 mM $Mn^{2+}$의 존재 하에서는 7$0^{\circ}C$ 이상에서도 안정하였다. 이 효소도 다른 D-xylose isomerase처럼 활성과 열 안정성을 위해서 $Mg^{2+}$, $Co^{2+}$또는 $Mn^{2+}$와 같은 2가의 양이온을 필요로 하였으며, 이중 $Mn^{2+}$가 효소 활성에 가장 효과적이었다. 기질 특이성에 관한 연구에서는 D-xylose를 사용했을 때 높은 활성을 가짐을 알 수 있었다. 이 효소의 pI 값은 4.8이었고, D-xylose에 대한 Km 값은 5.9 mM이었다.

• 한국미생물·생명공학회지
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• 제4권4호
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• pp.138-144
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• 1976

Xylose를 효소 유도물질로한 배지에서 glucose isomerase를 생산하는 균주를 분리하기 위하여 전국각지의 토양시료 150점에서 약 280주의 Streptomyces속 균주를 분리하여 그 중에서 효소 활성능이 높은 5주를 분리하였다. 이들 균주의 성질을 조사한 결과, 서로 다른 균종임을 확인하고 분류가 완성될 때까지 Streptomyces(st) spp. K-14, K-53, K-71, K-77 및 K-733 이라 부르기로 하였다. 특히 K-77과 K-733균주는 포자 표면이 침상형임으로 다른 균종과 완전히 구별되었다. 이들 균주 중에서 K-14균주는 효소 활성능이 가장 양호하였다.

• Journal of Microbiology and Biotechnology
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• 제14권2호
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• pp.312-316
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• 2004

Five strains, producing bacterial thermostable L-arabinose isomerase, were isolated from Korean soil samples obtained from compost under high temperature circumstances. Among these strains, the CBG-Al showed the highest L-arabinose isomerase activity at $60^\circ{C}$ and was selected as a D-tagatose producing strain from D-galactose. This strain was identified as Geobacillus thermodenitrificans based on the 16S rRNA analysis, and biological and biochemical characteristics. The isolated strain was aerobic, rod-shaped, Gram-positive, nonmotile, and an endospore-forming bacterium. No growth was detected in culture temperature below $40^\circ{C}$. The maximum growth temperature and maximum temperature of enzyme activity were $75^\circ{C}$ and $65^\circ{C}$, respectively. In metal ion effects, $Ca^{2+}$ was the most effective enzyme activator with the reaction rate by 150%. In a 5-1 jar fermentor with 3-1 MY medium, L-arabinose isomerase activity was growth-associated and pH decreased rapidly after the initial logarithmic phase.