• Korean Journal of Microbiology
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• v.52 no.2
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• pp.236-241
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• 2016

The Schizosaccharomyces pombe $sdu1^+$ gene, belonging to the PPPDE superfamily of deubiquitinating enzyme (DUB) genes, was previously shown to encode a protein with ubiquitin C-terminal hydrolase (UCH) activity and to participate in the response against oxidative and nitrosative stresses. This work focused on the reactive oxygen species (ROS)-dependent regulation of the S. pombe $sdu1^+$ gene. UCH activities, encoded by the $sdu1^+$ gene, were attenuated in the S. pombe cells exposed to $H_2O_2$, superoxide radical-generating menadione (MD), and nitric oxide (NO)-generating sodium nitroprusside (SNP). Reduced glutathione (GSH) and its precursor N-acetylcysteine (NAC) were able to significantly enhance the UCH activities in the absence or presence of $H_2O_2$. However, the influences of both GSH and NAC on the ROS levels in the absence or presence of $H_2O_2$ were opposite to their effects on the UCH activities under the same conditions. The UCH activities in the Sdu1-overexpressing S. pombe cells were also diminished under exposure to $H_2O_2$, MD and SNP, but still remained to be higher than those in the vector control cells. In brief, it is proposed that the S. pombe $sdu1^+$ gene is regulated by ROS in a negative manner, the meaning of which largely remains elusive.

• Applied Chemistry for Engineering
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• v.26 no.5
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• pp.624-629
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• 2015

A biosensor including the homogenized tissue of mugwort embedded in carbon paste, which senses hydrogen peroxide, was constructed and its electrochemical properties were validated using voltammetry. The good linearity of Hanes-Woolf plot implied that the reduction reaction of substrate was catalyzed by mugwort peroxidase at the electrode surface. Also the small value of symmetry factor, 0.28, indicated that electrochemical kinetics of the sensor is very sensitive to the change of electrode potential. Many experimental results collected above proved that the dissociation of hydrogen peroxide is dependent on the catalytic power of mugwort peroxidase qualitatively and quantitatively at the surface of the mugwort electrode. It is our firm belief that the marketed HRP can be replaced with mugwort tissue.

• KSBB Journal
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• v.25 no.6
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• pp.520-526
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• 2010

In this work we have investigated the production of catalase from Bacillus sp. strains, which were screened and identified from soil. These strains were cultivated in shaking flasks with tryptic soy broth (TSB) at $30^{\circ}C$ and 200 rpm. Effects of the temperature and pH on the stability of the native catalase and whole cell viability were studied in the temperature range of $25-60^{\circ}C$ and the pH range of 7-13. Korean natural zeolite was added to culture medium and mixed with microorganisms for 24 hours. The native catalase maintained its activity over $50^{\circ}C$. The enzyme acitiviy of the catalase from Bacillus flexus BKBChE-3 was highest among the Bacillus sp. strains studied. Bacillus flexus BKBChE-3 and immobilized Bacillus cells have survived under extreme conditions of over $50^{\circ}C$ and pH 12. 60 mL of 10.5 mM $H_2O_2$ solution were entirely removed within 1 hour with catalase produced from Bacillus sp. on the flask. When Bacillus cells were immobilized on Korean natural zeolite, colony forming unit of Bacillus flexus BKBChE-3 was increased and high efficiency of hydrogen peroxide removal was observed.

• Applied Chemistry for Engineering
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• v.28 no.3
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• pp.369-374
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• 2017

The curtailment of production cost is important for the mass production of biosensors. Since horseradish peroxidase, which is a key material of enzyme electrodes for hydrogen peroxide analysis is rather expensive, this has been a limiting factor for fabricating carbon paste based enzyme electrodes. In this paper, the acacia leaf tissue as a zymogen easily obtainable in our living environment was used as an alternative to horseradish peroxidase for developing a hydrogen peroxide sensor and the electrochemical properties were evaluated. Ten or more electrochemical parameters alongside the other experimental results acquired by the potentiostatic method demonstrated that our enzyme electrodes can be used for the quantitative analysis of hydrogen peroxide. This also indicates that acacia leaves can take the place of the marketed peroxidase.

• Journal of Hydrogen and New Energy
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• v.27 no.4
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• pp.378-385
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• 2016

In this study, we synthesized a biocatalyst consisting of glucose oxidase (GOx), polyethyleneimine (PEI) and carbon nanotube (CNT) with addition of glutaraldehyde (GA)(GA/[GOx/PEI/CNT])for fabrication of glucose sensor. Main bonding of the GA/[GOx/PEI/CNT] catalyst was formed by crosslinking of functional end groups between GOx/PEI and GA. Catalytic activity of GA/[GOx/PEI/CNT] was quantified by UV-Vis and electrochemical measurements. As a result of that, high immobilization ratio of 199% than other catalyst (with only physical adsorption) and large sensitivity value of $13.4{\mu}A/cm^2/mM$ was gained. With estimation of the biosensor stability, it was found that the GA/[GOx/PEI/CNT] kept about 88% of its initial activity even after three weeks. It shows GA minimized the loss of GOx and improved sensing ability and stability compared with that using other biocatalysts.

• Journal of Korean Society of Environmental Engineers
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• v.27 no.12
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• pp.1263-1269
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• 2005

Horseradish peroxidase, had the phenol degradation rate of 95% in aqueous phase, was covalently immobilized on the surface of reticulated vitreous carbon(RVC) and the degradation of phenol was performed with in situ generated $H_2O_2$-immobilized HRP complex in an electrochemical reactor. The incorporation of carboxylic group on the RVC surface was confirmed by FT/IR spectrometry and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride(EDC) was used for peptide bonds between the carboxylic groups on the RVC surface and amine groups from HRP. The optimal conditions of in situ $H_2O_2$ generation such as concentration($10{\sim}200$ mM) and pH($5.0{\sim}8.0$) of electrolyte, supply of $O_2(10{\sim}50$ mL/min) and applied voltage($-0.2{\sim}-0.8$ volt, vs. Ag/AgCl) from potentiostat/galvanostat were determined by concentration of hydrogen peroxide and current efficiency. It was observed that the RVC immobilized HRP was stable maintaining 89% of the initial activity during 4 weeks. The phenol degradation rate of 86% was attained under the optimal condition of in situ $H_2O_2$ generation.

• Proceedings of the Korean Society of Dyers and Finishers Conference
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• 2012.03a
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• pp.94-94
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• 2012

섬유산업은 원가 경쟁력 향상과 산업 고도화에 필요한 미래형 저에너지 염색가공 핵심 기술을 통한 고부가가치 섬유제품의 창출과 섬유산업의 선진화달성에 꾸준히 노력을 해 왔다. 염색가공업의 에너지 소비는 섬유산업에서 염색가공업이 연료 사용량의 77%, 전기사용량의 54%를 차지하여 섬유산업의 에너지절감을 위해서는 염색가공 공정에서의 에너지 절감이 가장 중요하다. 국내 염색가공 분야의 4백여 업체를 대상으로 실시한 애로 기술에 관한 설문 조사결과에 따르면 염색공업의 에너지 절약형 구조로의 전환을 위해서 가장 시급히 요구되는 우선기술 1순위는 에너지절약형 염색가공 공정기술로 에너지 절감의 필요성을 반영하고 있다. 효소(Enzyme)가 섬유산업에 도입되기 시작한 것은 면섬유의 호발에 아밀라제가 사용되기 시작하면서 부터이며, 최근 유럽선진국들의 강화된 환경규제와 눈부신 바이오테크놀러지(Biotechnology)의 발전에 기인하여 섬유산업에서 관심과 적용이 확대되고 있다. 섬유산업에서 효소적용의 장점은 효소 그 자체가 자연산물이기 때문에 생분해 되고 중성에 가까운 pH에서 반응하므로 처리액이 환경문제를 일으키지 않으며, 기질특이성을 가져 매우 선택적으로 반응하여 부반응으로 인한 섬유의 손상을 최소화 하는 효과를 들 수 있으며, 무엇보다 소량 저온반응으로 인한 에너지절감이 가장 큰 장점이라 할 수 있다. 실제 섬유산업에서는 전분호제를 제거하는 아밀라아제, 데님워싱 및 면섬유의 후가공에 사용하는 셀룰라아제, 표백 후 잔류하는 과산화수소를 제거하는 카탈라제 등을 적용하는 사례가 많아지고 있으며, 이 밖의 다양한 공정에 효소 이용연구가 활발히 진행되고 있다. 본 연구에서는 그 동안 섬유 업체에서 직물의 표면 잔털을 제거하여 매끄러운 외관과 선명한 색상을 재현하기위해 후가공으로 셀룰라아제를 이용했던 공정을 개선하여, 효소를 이용한 정련-Bio polishing-염색의 3공정을 1욕처리를 통해 기존 단독으로 진행되어진 기존제품과의 중량, 외관, 색상재현성, 정련성 등을 비교하여 에너지 절약형 공정기술의 효과를 극대화 해보았다.

• Journal of the Korean Electrochemical Society
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• v.11 no.3
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• pp.165-169
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• 2008

The effect of reduction of carbon dioxide by CODH(Carbon Monoxide Dehydrogenase) was compared on glassy carbon and gold working electrodes. In case of gold electrode, the choice of the optimum applied potential is very important since $H_2$ evolution can be mixed with $CO_2$ reduction. On the other hand, efficient $CO_2$ reduction was observed up to -650 mV vs. NHE on glassy carbon in neutral solution due to the larger overpotential for $H_2$ evolution on glassy carbon surface than that on gold surface. The optimum potential for $CO_2$ reduction was found to be $-570{\sim}600\;mV$ vs. NHE. The current efficiency of $CO_2$ to CO decreased dramatically at more negative potential according to the activity of enzyme decrease and the hydrogen evolution.

• Applied Biological Chemistry
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• v.41 no.1
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• pp.47-52
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• 1998

3-Hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the conversion of HMG-CoA to mevalonic acid, the first intermediate of isoprenoid biosynthetic pathway in plants. The enzyme was solubilized with 0.4% Brij (polyoxyethylene ether) W-1 from a microsomal fraction of etiolated rice seedlings (Oryza sativa L.) in which its maximal activity was observed on the fourth day after germination. HMGR was purified to near homogeneity by employing $(NH_4)_2SO_4$ fractionation plus chromatographic procedures including DEAE-Sephadex A-50 and HMG-CoA-hexane-agarose affinity column. The size of the purified enzyme was estimated to be 55 kDa when judged by SDS-PAGE analysis with silver staining method. The apparent $K_m$ and $V_{max}$ values for HMG-CoA were determined to be $180\;{\mu}M$ and 107 pmol/min/mg, and those for NADPH were $810\;{\mu}M$ and 32.1 pmol/min/mg, respectively.

• Journal of the Korean Electrochemical Society
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• v.11 no.3
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• pp.170-175
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• 2008

Screen printed carbon electrodes (SPEs) modified with co-immobilized osmium-based redox polymers can be used to apply multi-detecting biosensors. In this study, we report our initial studies of multi-detecting biosensor concepts using two osmium-based redox polymers for horseradish peroxidase-mediated reduction of ${H_2}{O_2}$ coupled to glucose oxidase-mediated oxidation of glucose. We target to synthesize two osmium redox polymers of potentials use, a chloride-containing redox polymer ($E^{O'}$ + 0.520 vs. Ag/AgCl) and a methoxy-containing redox polymer $E^{O'}$ + 0.150 vs. Ag/AgCl). The former show good catalytic electrical signals with horseradish peroxidase and the latter's redox polymer is to be an effective redox mediator of glucose oxidation by glucose oxidase.