• 생명과학회지
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• 제12권3호
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• pp.281-287
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• 2002

소 간으로부터 퀴논 환원효소를 정제하였으며 정제된 효소는 벤조퀴논과 나프토퀴논 뿐만 아니라 페난트렌 퀴논의 환원도 촉매하였다. 소 간으로부터 정제된 퀴논 환원 효소는 아릴니트로소 화합물의 생변환을 촉매하였으며 반응 생성물은 TLC, GC, GC-MS, NMR을 사용하여 확인되었다. 이 반응은 포유동물 퀴논 환원효소의 강력한 저해제인 Cibacron blue 3GA나 dicumarol에 의하여 크게 저해되었다.

• Journal of Microbiology and Biotechnology
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• 제32권5호
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• pp.663-671
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• 2022

The saccharification of cellulose and hemicellulose is essential for utilizing lignocellulosic biomass as a biofuel. While cellulose is composed of glucose only, hemicelluloses are composed of diverse sugars such as xylose, arabinose, glucose, and galactose. Sulfolobus acidocaldarius is a good potential candidate for biofuel production using hemicellulose as this archaeon simultaneously utilizes various sugars. However, S. acidocaldarius has to be manipulated because the enzyme that breaks down hemicellulose is not present in this species. Here, we engineered S. acidocaldarius to utilize xylan as a carbon source by introducing xylanase and β-xylosidase. Heterologous expression of β-xylosidase enhanced the organism's degradability and utilization of xylooligosaccharides (XOS), but the mutant still failed to grow when xylan was provided as a carbon source. S. acidocaldarius exhibited the ability to degrade xylan into XOS when xylanase was introduced, but no further degradation proceeded after this sole reaction. Following cell growth and enzyme reaction, S. acidocaldarius successfully utilized xylan in the synergy between xylanase and β-xylosidase.

• 한국물환경학회지
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• 제26권4호
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• pp.574-579
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• 2010

In this study the enzyme inhibition method using dehydrogenase which has been popularly used to estimate ecotoxicity was optimized. When three bacterial strains, Escherichia coli HB101, Enterobacter asburiae KCAD-4, and Aeromonas media KCAD-13, were compared, KCAD-4 was considered as the adequate strain to estimate toxicity because of its sensitivity and reproducibility. The optimal bacterial density was estimated as $5.4{\times}10^9CFU/mL$, at which the maximum sensitivity was observed. The phosphate buffer was suitable for the reaction solution. When the reaction times required for inhibition of enzyme activity by contact of toxicants and for reaction of damaged bacteria and substrate were tested, the optimal value was estimated as 20 min and 2 hrs, respectively. It is expected that the optimized conditions can be used to develop the standardized kits to estimate ecotoxicity of heavy metals in effluent from the industrial wastewater treatment facilities.

• 미생물학회지
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• 제27권1호
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• pp.35-42
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• 1989

The mode of transglycosylation reaction observed during the action of low-molecular-weigh $\beta$-D-glucosidase ($\beta$-D-glucoside glucohydrolase, EC3.2.1.21) purified from Trichoderma koningii ATCC 26113 was investigated using $^{1}H$-NMR spectroscopy. The enzyme was purified by the series of procedures including ammonium sulfate precipitation, and fractionations by column chromatographies on Bio-Gel P-150, DEAE-Sephadex A-50, and SP-Sephadex C-50. The final purification was performed by the band eluation after preparative polyacrylamide gel electrophoresis. The enzyme showed its molecular size of 78,000 through the analysis of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its isoelectric point of 5.80 through the analysis of analytical isoelectric focusing. The H-1 proton resonances were analyzed. After the reaction of the enzyme with cellobiose, the reaction products were separated by high performance liquid chromatography using refractive index detector. H-1 resonances of the products were consisted with those of gentiobiose [$\beta$-D-glucopyranosyl--(1,6)-D-glucopyranose], and cellotriose [$\beta$-D glucopyranosyl-(1,4)-$\beta$-D-glucopyranosyl]-(1,4)-D-glucopyranose] with minor resonances of sophorose [$\beta$-D-glucopyranosyl-(1,2)-D-glucopyranose], respectively.

• 한국식품영양과학회지
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• 제9권1호
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• pp.59-73
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• 1980

A detailed procedure was described for the isolation of cratine kinase (ATP-Creatine phosphotransferase, E. C. 2. 7. 3. 2.) from the muscle of the snake Bungarus fasciatus. The original isolation procedure of Kuby et al. for the rabbit muscle enzyme has been modified and extended to include a chromatographic step. The properties of the enzyme have been investigated and kinetic constants for the reverse reactions determined as the followings: 1) A molecular weight of the enzyme was determined by gel filteration on Sephadex G-100 and by electrophoresis on SDS-polyacrylamide was 86,000. 2) Two reactive sulphydryl groups were detected with dithiobis nitrobenzoic acid (DTNB). 3) The nucleotide substrate specificity in the reverse reaction was determined as ADP*2'-dADP＞GDP＞XDP＞UDP with magnesium as the activating metal ion. 4) The order of the metal specificity in the reverse reaction Mg>Mn>$Ca{\sim}Co$ was determined with ADP as substrate. 5) A detailed kinetic analysis was carried out in the reverse direction with $MaADP^-$ as the nucleotide substrate. Initial velocity and product inhibition studies($MaADP^{2-}$ competitive with respect to MgADP- and noncompetitive with respect to $N-phosphorycreatine^{2-}$ ; Creatine competitive with respect to $N-phosphorycreatine^{2-}$ and noncompetitive with respect to Ma $ADP^-)$ indicated that the reaction obeyed a sequential mechanism of the rapid equilibrium random type.

• 한국농업기계학회:학술대회논문집
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• 한국농업기계학회 2005년도 하계 학술대회 논문집
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• pp.331-336
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• 2005

• Biotechnology and Bioprocess Engineering:BBE
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• 제11권4호
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• pp.299-305
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• 2006

Aromatic L-amino acid transaminase is an enzyme that is able to transfer the amino group from L-glutamate to unnatural aromatic ${\alpha}-keto$ acids to generate ${\alpha}-ketoglutarate$ and unnatural aromatic L-amino acids, respectively. Enrichment culture was used to isolate thermophilic Bacillus sp. T30 expressing this enzyme for use in the synthesis of unnatural L-amino acids. The asymmetric syntheses of L-homophenylalanine and L-phenylglycine resulted in conversion yields of >95% and >93% from 150 mM 2-oxo-4-phenylbutyrate and phenylglyoxylate, respectively, using L-glutamate as an amino donor at $60^{\circ}C$. Synthesized L-homophenylalanine and L-phenylglycine were optically pure (>99% enantiomeric excess) and continuously pre-cipitated in the reaction solution due to their low solubility at the given reaction pH. While the solubility of the ${\alpha}-keto$ acid substrates is dependent on temperature, the solubility of the unnatural L-amino acid products is dependent on the reaction pH. As the solubility difference between substrate and product at the given reaction pH is therefore larger at higher temperature, the thermophilic transaminase was successfully used to shift the reaction equilibrium toward rapid product formation.

• Journal of Microbiology and Biotechnology
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• 제28권2호
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• pp.298-304
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• 2018

The single-vessel multienzyme UDP-${\alpha}$-$\text\tiny{D}$-glucose recycling system was coupled with a forward glucosylation reaction to produce novel glucose moiety-conjugated derivatives of different tetracycline antibiotic analogs. Among five tetracycline analogs used for the reaction, four molecules (chlorotetracycline, doxytetracycline, meclotetracycline, and minotetracycline) were accepted by a glycosyltransferase enzyme, YjiC, from Bacillus licheniformis to produce glucoside derivatives. However, the enzyme was unable to conjugate sugar units to rolitetracycline. All glucosides of tetracycline derivatives were characterized by ultraviolet absorbance maxima, ultra-pressure liquid chromatography coupled with photodiode array, and high-resolution quadruple time-of-flight electrospray mass spectrometry analyses. These synthesized glucosides are novel tetracycline derivatives.

• 한국미생물생명공학회:학술대회논문집
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• 한국미생물생명공학회 1979년도 추계학술대회 심포지움
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• pp.245.2-246
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• 1979

Heat treated whole cell of Aspergillus niger containing glucose oxidase-catalase system was entrapped in gelatin matrix crosslinked by glutaral-dehyde. The reaction characteristics of immobilized enzyme was studied in a fludized reactor. Heat treatment enhanced the stability and improved the properties of micellium for the immobilized process. The immobilized enzyme system showed the maximum activity at $35^{\circ}C$ and at pH 5.5. The optimum substrate concentration was 0.04M glucose. The activity of immobilized glucose oxidase was in proportion to the concentration of dissolved oxygen in reaction mixture as other reaction conditions were fixed. It was also demonstrated that the limiting factor for the activity of the immobilized glucose oxidase was the oxygen diffusion resistance which increases proportionally to the glucose concentration.

• 공업화학
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• 제5권2호
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• pp.209-214
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• 1994

Mono alkyl glycerides have bean obtained in good yield by enzyme catalyst from soybean oil. The reaction was carried out in an oil rich microemulsion formula. Best results were obtained with sodium bis(2-ethyl hexyl) sulfo succinate(AOT), isooctane as hydrocarbon component and buffer of pH 7. The enzyme used was a 1,3-specific lipase which leaves the 2-position intact. However, the 2-monoglyceride formed slowly undergoes long chain acyl migration to 1-mono-glyceride. Optimal reaction time at $35^{\circ}C$ reaction temperature was found to be three hour.