• KSBB Journal
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• 제17권2호
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• pp.158-161
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• 2002

본 연구에서는 화학무기, 농약 등에 사용되는 신경독성물질인 유기인화합물의 측정을 위하여 유기인화합물의 효소반응 저해작용을 이용한 광바이오센서장치의 시제품을 제작하였다. 효소반응을 위하여 효소로는 신경세포의 필수효소인 acetylcholinesterase, acetylthiocholine iodide을 사용하였으며 효소반응의 저해제인 유기인화합물로는 paraoxon을 사용하였다. 센서의 폭정원리는 유기인화합물에 의해 저해된 효소반응정도를 효소반응의 생성물인 아세트산의 정량적 측정으로 분석하였으며, pH에 의하여 최대 흡광파장의 변화가 일어나는 litmus를 사용하여 흡광도 측정으로 아세트산의 정량분석을 수행하였다. 광바이오센서 시제품의 제작은 광원으로 고취도 LED와 광세기 측정을 위한 photodiode로 구성하였으며, 제작된 센서를 이용한 실험결과로부터 0 ppm에서 2 ppm의 paraoxon 농도에서 구성된 센서시스템의 선형적 신호 변화를 관찰하였다. 이상의 실헐결과로부터 광바이오센서 시제품은 2분의 반응시간으로 신속하고 정확한 유기인화합물의 정량분석이 가능함을 확인하였다.

• Applied Biological Chemistry
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• 제11권
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• pp.43-47
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• 1969

본(本) 연구(硏究)에서 얻어진 결과(結果)를 요약(要約)하면 다음과 같다. 1. Glucose Isomerizing Enzyme을 분비(分泌)하는 Actinomyces과(科) 균주(菌株)를 토양(土壤)으로부터 분리(分離)하였으며 2. 본(本) 균주(菌株)가 생성(生成)하는 Glucose Isomerizing Enzyme를 Glucose에 작용(作用)시킨 결과(結果) 생성(生成)된 당(糖)은 Fructose 일종(一種)만을 생성(生成)하였으며 그외(外)의 당(糖)의 부생물(副生物)은 검출(檢出)되지 아니 하였다.

• BMB Reports
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• 제30권2호
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• pp.113-118
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• 1997

Aspartase from Hafnia alvei was inactivated by N-ethylmaleimide (NEM) and 5,5' -Dithiobis-(2-znitrobenzoic acid) (DTNB) following pseudo-first order kinetics. Their apparent reaction orders were 0.83 and 0.50 for NEM and DTNB modifications, respectively, indicating that inactivation was due to a sulfhydryl group in the active site of aspartase and participation of the sulfhydryl group in an essential step in the catalytic reaction. When aspartase was modified by DTNB, the enzyme activity was restored by dithiothreitol treatment, indicating that cysteine residuetsl islarel possibly at or near the active site. The pH-dependence of the inactivation rate by NEM suggested that an amino acid residue having pK value of 8.3 was involved in the inactivation. When aspartase was incubated with NEM and L-aspartate together, L-aspartate markedly protected the enzyme from inactivation by NEM, but the other reagents used did not.

• Journal of Microbiology and Biotechnology
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• 제11권6호
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• pp.928-933
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• 2001

Approximately 0.1 mg/ml of polyvinyl alcohol (PVA) was degraded by the growing cell, Brevibacillus laterospours, for 30 h, and 0.2 mg/ml of PVA was degraded by the cell-free extract that was isolated from Brevibacillus laterosporus. Approximately $0.29{\mu}g$/ml of acetic acid was produced from PVA by using the cell-free extract as a catalyst for 40 min. $V_{max}\;and\;K_m$ value of purified PAV-degradation enzyme was 3.75g/l and 2.75 g/l/min in reaction with EDTA and 3.99 g/l and 2.98 g/l/min in reaction without EDTA, respectively. Molecular weight of the purified enzyme determined by SDS-PAGE was 63,000 Da. Alcohol dehydrogenase and aldehyde dehydrogenase activities were qualitatively detected on a native acrylamide gel by an active staining method, indicating the existence of the metabolic pathway to use PVA as a substrate.

• Journal of Microbiology and Biotechnology
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• 제10권1호
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• pp.99-102
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• 2000

To establish optimal conditions for esterification by Candida cylindracea, lipase reactions were performed simultaneously, separately, or individually in the varying initial rates of $0.014-0.060\mu$mole free fatty acids consumed min-1g-1. The reactants which were conditioned at aw of 0.12 gave the highest initial rate of esterifying $0.060\mu$mole free fatty acids consumed min-1g-1. These results suggest that the esterifying activity of lipase in an organic system depends on the transfer of available water within the reaction system.

• BMB Reports
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• 제30권4호
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• pp.258-261
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• 1997

A simple quantitative assay method for ribonuclease activity has been developed. This method is based on the decrease of fluorescence intensity emitted by the ethidium bromide bound to RNA due to the degradation of RNA by ribonuclease. The substrate RNA was reacted with ribonuclease A and the fluorescence intensity was measured after the addition of ethidium bromide. The intensity difference was calculated using a blank reaction mixture containing no RNase. Whole cellular RNA substrate produced a significant error and was not suitable for this assay method possibly because of local microheterogeniety caused by high molecular weight rRNA. but satisfying results were obtained with tRNA substrate. The intensity difference increased linearly by raising enzyme concentration up to $2{\times}10^{-4}$ Kunitz Units of ribonuclease A. More refined and reliable results were obtained by use of initial reaction velocities which were calculated from the plots of intensity difference vs time. A linear relationship between initial velocities and enzyme concentrations was observed up to 0.01 Kunitz Units of enzyme.

• Applied Biological Chemistry
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• 제14권3호
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• pp.207-212
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• 1971

An enzyme preparation from a newly isolated Candida that showed a high lipase activity was subjected to examination of its reaction rate under various conditions. The original and a diluted enzyme solutions showed the zero order curve starting at the point of 50 minutes in time. When PVA was used as an emulsifyer more activity was observed than the case of gum arabic. The optimal temperature and pH were $37{\sim}40^{\circ}C$ and 7.0, respectively. Oleic acid as a fatty acid conferred on the enzyme an inhibitory action while calcium ion a positive one. Sodium cholate yielded an increase in reaction rate at the first stage.

• 한국식품영양과학회지
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• 제28권1호
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• pp.74-80
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• 1999

Growth and bacteriocin production by Lactobacillus sp. GM7311 in tofu residue treated with two commercial amylases were investigated. The optimal condition of amylase Ⅰ(liquefied enzyme for sauce) and Ⅱ(multienzyme 2,000) for the enzyme reaction was showed at pH 6.0 and 4.0, respectively. The optimal temperature was 40oC both. At the enzyme dosage 4% and 3% and reaction time 1hr, about 2% of reduced sugar needed bacteriocin production was obtained. The enzymatic treatment of tofu residue enhanced bacteriocin production by lactic acid bacteria, particularly in the tofu residues added 2.0% yeast extract. But, we couldn't see the increment of bacteriocin activity in the tofu residues added other nitrogen sources such as proteose peptone No. 3 and lab lemco powder. Also, in the comparision of amylase I and Ⅱ, bacteriocin activity in the tofu residue treated with amylase Ⅰ was better than that of amylase Ⅱ.

• 한국식품영양과학회지
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• 제28권1호
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• pp.172-177
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• 1999

Branched maltodextrin which contains branched sugars as well as linear sugars was produced by Tranzyme L 500. Branched sugar content increased as reaction time between substrate(D.E. 19) and 0.05% of Tranzyme L 500 at pH 5.5, 55oC increased. Branched sugar content was 14.9% at 24 hr of reaction and reached 27% after 60 hr. Total branched sugar content increased regardless of substrate D.E. as enzyme concentration increased. However, when concentrations of enzyme were 0.1, 0.2%, production of branched sugars of which content were 46.6%, 52.6% respectively at those enzyme concentrations, was higher at D.E. 19 than any other conditions.

• KSBB Journal
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• 제6권2호
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• pp.147-156
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• 1991

Diazotized chitin (CHITN) was synthesized reacting with NaN3 and HCl to alkaline hydrolyzed chitin for the support of immobilized enzyme. Immobilized $\beta$-glucosidase on diazotized chitin(CHITN-Gase) was produced reacting with glutaraldehyds as bifunctional reagent. CHITN-Gase activities were determined reacting with p-nitrophenol-$\beta$-D-glucopyranoside in plug flow reactor as a reference. Optimum temperature, optimum pH, reaction constant and deactivation rate were determined with variation of flow rate and H/D. The particle size of immobilized enzyme in the best was, 35 mesh (CHITN35-Gase). The optimum conditions of immobilized enzyme were $70^{\circ}C$ in temperature and 5.0 in pH. Diameter and flow rate of plug flow reactor in the best was 8.5mm in diameter and 0.8ml/min in flow rate. Reaction constant was mainly influenced by electrostatic force. The best glucose hydrolizing activities of CHITN3 5-Gase was 3.34$\times$10-5 M/1. while that of native-$\beta$-glucosidase was 2.44$\times$10-5 M/1.