• Biomolecules & Therapeutics
• /
• v.1 no.2
• /
• pp.220-225
• /
• 1993

Effect of BR-900317 on the angiotensin I-induced pressor response in pithed rats and the effects of its single oral administration on plasma angiotensin converting enzyme (ACE) activities in normotensive rats and on the cardiovascular system in hypertensive model rats (SHR, RHR), were compared with those of captopril. BR-900317 attenuated the angiotensin I-induced pressor effects in pithed rats. In a single oral dose administration study, BR-900317 inhibited the plasma ACE activities in a dose-dependent fashion. Duration of the action of BR-900317 was similar to that of captopril. BR-900317 produced antihypertensive effect in spontaneously hypertensive rats and dose-dependent antihypertensive effect in 2-kidney Goldblatt hypertensive rats without affecting heart rate. These results suggest that the main mechanism of the antihypertensive effect of BR-900317 is the suppression of angiotensin II production due to the inhibition of the ACE.

• Korean Journal of Microbiology
• /
• v.27 no.4
• /
• pp.430-435
• /
• 1989

Dextranase and glucose-osidase was investigated as an anti-plaque agent and a component of dentifrice. In vitro synthesis of the water-insoluble glucan was decreased with increasing amount of dextranase and glucose-oxidase. Dextranase was effective on the decrease of viable S. mutans, and the formation of plaque decreased. But it is not effective on the degradatio of plaque. As a research for addition of enzyme to the dentifrice components, we formulated the Model Dentifrice for stabilization of enzyme. At the Model Dentifrice, we confirmed the stability of enzyme by evalution of activity for a long time.

• BMB Reports
• /
• v.36 no.2
• /
• pp.167-172
• /
• 2003

The kinetics of thermal inactivation of copper-containing amine oxidase from lentil seedlings were studied in a 100 mM potassium phosphate buffer, pH 7, using putrescine as the substrate. The temperature range was between $47-60^{\circ}C$. The thermal inactivation curves were not linear at 52 and $57^{\circ}C$; three linear phases were shown. The first phase gave some information about the number of dimeric forms of the enzyme that were induced by the higher temperatures using the "conformational lock" pertaining theory to oligomeric enzyme. The "conformational lock" caused two additional dimeric forms of the enzyme when the temperature increased to $57^{\circ}C$. The second and third phases were interpreted according to a dissociative thermal inactivation model. These phases showed that lentil amine oxidase was reversibly-dissociated before the irreversible thermal inactivation. Although lentil amine oxidase is not a thermostable enzyme, its dimeric structure can form "conformational lock," conferring a structural tolerance to the enzyme against heat stress.

• Biotechnology and Bioprocess Engineering:BBE
• /
• v.7 no.5
• /
• pp.268-274
• /
• 2002

Enzymatic hydrolysis of waste office paper was evaluated using three commercial cellulases, Acremonium cellulase, Meicelase, and Cellulosin T2. Varying the enzyme loading from 1 to 10% (w/w) conversion of waste office paper to reducing sugar was investigated. The conversion increased with the increase in the enzyme loading: in the case of enzyme loading of 10% (w/w), Acremonium cellulase yielded 79%conversion of waste office paper, which was 17% higher compared to Meicelase, 13% higher than that of Cellulosin T2. Empirical model for the conversion (%) of waste office paper to re-ducing sugar (x) was derived from experimental results as follow, x = $kE^{m}t^{(aE+b)}$ where k, m, a, and b de-note empirical constants. E indicates initial enzyme concentration.

• Advances in Traditional Medicine
• /
• v.3 no.1
• /
• pp.46-50
• /
• 2003

We studied the inhibitory effect of Green Life Enzyme (GLE) on compound 48/80-induced anaphylactic response in a murine model. GLE inhibited compound 48/80-induced systemic anaphylactic shock at the dose of 10 g/kg by 87.5%. When GLE was given as pre-treatment at concentrations ranging from 0.01 to 1.0 g/kg, it inhibited passive cutaneous anaphylaxis activated by anti-dinitrophenyl (DNP) IgE. In addition, GLE (0.1 mg/ml) inhibited anti-DNP IgE-induced tumor necrosis $factor-{\alpha}$ production from mast cells by 69% compared to saline value. These results indicate that GLE may possess anti-anaphylactic and anti-inflammatory activity.

• The Journal of the Korea institute of electronic communication sciences
• /
• v.13 no.3
• /
• pp.579-586
• /
• 2018

With the beginning of the new era of bigdata, information extraction or prediction are an important research area. Here, we present the acquisition of semi-automatically curated large-scale biological database and the prediction of enzyme reaction annotation for analyzing the pharmacological activities of drugs. Because the xenobiotic metabolism of pharmaceutical drugs by cellular enzymes is an important aspect of pharmacology and medicine. In this study, we apply and analyze similarity models to predict bimolecular reactions between human enzymes and their corresponding substrates. Thirteen models select to reflect the characteristics of each cluster in the similarity model. These models compare based on sensitivity and AUC. Among the evaluation models, the Simpson coefficient model showed the best performance in predicting the reactivity between the enzymes. The whole similarity model implement as a web service. The proposed model can respond dynamically to the addition of reaction information, which will contribute to the shortening of new drug development time and cost reduction.

• Journal of Life Science
• /
• v.21 no.1
• /
• pp.127-133
• /
• 2011

${\beta}$-Galactosidase was immobilized on chitosan bead by covalent bonding using glutaraldehyde. The characteristics of the immobilized enzyme were investigated. Maximum immobilization yield of 75% was obtained on chitosan bead. Optimum pH and temperature for the immobilized enzyme was 7.0 and $50^{\circ}C$, respectively. The immobilized enzyme showed a broader range of pH and temperature compared to a free one. A mathematical model for the operation of the immobilized enzyme in a packed-bed reactor was established and solved numerically. Under different inlet lactose concentrations and feed flow rate conditions, lactose conversion was measured in a packed-bed reactor. The experimental results of continuous operation in a packed-bed reactor were compared to theoretic results using Michaelis-Menten kinetics with competitive product inhibition and external mass transfer resistance. The model predicted the experimental data with errors less than 5%. Process optimization of continuous operation in a packed-bed reactor was also conducted. In a recirculation packed-bed operation, conversion of lactose was 97% in 3 hours. In a continuous packed-bed operation, the effect of flow rate and initial lactose concentration was investigated. Increasing flow rates and initial lactose concentration decreased the conversion of substrate.

• KSBB Journal
• /
• v.10 no.5
• /
• pp.540-546
• /
• 1995

Dry corn gluten meal of 70% protein content was enzymatically hydrolyzed by alkaline protease in a pH-state reactor. Such process variables as temperature, pH, and enzyme-to-substrate ratio were varied, and at each condition degree of hydrolysis was monitored and calculated. The ultimate degree of hydrolysis, which ranged between 25 and 28% based on gluten protein mass, was not significantly affected by the process variables. However, $50^{\circ}C$ and pH 9-10 appeared optimum. Kinetic analysis indicated enzyme deactivation was negligible during the hydrolysis, and the experimental data were near perfectly fitted to the model kinetic equation which was modified after neglecting enzyme deactivation term. The enzyme reaction was 1$100\times$ scaled up and basically the same hydrolysis performance was resulted. Amino acid analysis showed the hydrolyzate was relatively rich in glutamine/glutamic acid, leucine, and alanine at 19.6, 16.1, and 12.3 mole %, respectively.

• Journal of Applied Biological Chemistry
• /
• v.43 no.3
• /
• pp.147-151
• /
• 2000

A gene, nprM, from Bacillus megaterium ATCC 14945 was obtained by PCR using primers synthesized based on two nprM sequences from two different strains, and cloned into Escherichia coli. The gene nprM encoded an extracellular neutral protease, and the molecular mass of the expressed enzyme was estimated to be approximately 36kDa on a denaturating gel. The enzyme was activated by $Ca^{2+}$, and the optimum concentration of $Ca^{2+}$ was 5 mM. The enzyme was inhibited by EDTA but not by PMSF. The optimal pH and temperature of the cloned enzyme were $50^{\circ}C and pH 7.5-8.0, respectively, and were similar to those of the enzyme from the gene gonor cell. The cloned NprM caused internal cleavage of the native endoglucanase of B. subtilis BSE616 as a model foregin protein, and resulted in a small truncated but still active endoglucanase.

• Journal of Microbiology and Biotechnology
• /
• v.20 no.4
• /
• pp.737-748
• /
• 2010

Glutaminase production in Zygosaccharomyces rouxii by solid-state fermentation (SSF) is detailed. Substrates screening showed best results with oatmeal (OM) and wheatbran (WB). Furthermore, a 1:1 combination of OM:WB gave 0.614 units/gds with artificial sea water as a moistening agent. Evaluation of additional carbon, nitrogen, amino acids, and minerals supplementation was done. A central composite design was employed to investigate the effects of four variables (viz., moisture content, glucose, corn steep liquor, and glutamine) on production. A 4-fold increase in enzyme production was obtained. Studies were undertaken to analyze the time-course model, the microbial growth, and nutrient utilization during SSF. A logistic equation ($R^2$=0.8973), describing the growth model of Z. rouxii, was obtained with maximum values of ${\mu}_m$ and $X_m$ at $0.326h^{-1}$ and 7.35% of dry matter weight loss, respectively. A goodfit model to describe utilization of total carbohydrate ($R^2$=0.9906) and nitrogen concentration ($R^2$=0.9869) with time was obtained. The model was used successfully to predict enzyme production ($R^2$=0.7950).