• Korean Journal of Soil Science and Fertilizer
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• v.21 no.4
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• pp.380-385
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• 1988

The urease adsorption on zeolite and the various properties of adsorbed urease were investigated to find out the influence of zeolite on activity and properies of urease. Free urease in solution was adsorbed on zeolite untill the max. adsorption, and the amount of max. adsorption was 11.3mg urease/100mg zeolite at pH 7.0. It is apparent that free urease was adsorbed on the outer surface of zeolite by cation exchange reaction, and more than 70% of urease adsorption was adsorbed within 30 min. The activity of adsorbed urease was decreased by 89.6%, whereas Km value was increased to 34.4mM, which is higher than that of free urease. The optimum pH of adsorbed urease was widened 6.5 to 7.0, compared to that of free urease 7.0. The resistance of urease to protease became weaker by adsorption, however substrate specificity and thermal stability were not affected.

• Journal of Applied Biological Chemistry
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• v.60 no.2
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• pp.173-178
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• 2017

This study was conducted to investigate the effect of pyroligneous acids on urea hydrolysis for the purpose of inhibiting ammonia volatilization during urea fertilizer application. Different types of synthetic urease inhibitors have been searched and developed, but their use is limited due to varying inhibition effects on soil urease, and environmental problems. In this study, the effect of pyroligneous acids, a natural substance, on urea hydrolysis in soil was evaluated by analyzing inhibition of urease activity. Pyroligneous acids inhibited plant urease and microbial urease activity, as well as soil urease with various urease complex. In addition, pyroligneous acids exhibited non-competitive urease inhibition effect through urease kinetics and inhibited urea hydrolysis in the soil. This study showed that pyroligneous acids treatment with urea fertilizer decreases the loss of urea fertilizer, improves the efficiency of nitrogen application on plant and reduces the amount of nitrogen fertilizers applied in soil.

• Journal of Microbiology and Biotechnology
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• v.14 no.2
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• pp.330-336
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• 2004

Fifty-two pathogenic Vibrio parahaemolyticus strains were isolated from the environments of Busan and Yeosu, Korea. Forty-three of these strains showed protease activities, whereas 4 strains showed $\alpha / \beta$ hemolysin activities and 6 strains had urease activities. Their pathogenic factors were not overlapping except one strain, which had both protease and hemolysin activities. The 6 urease-positive strains (V. parahaemolyticus YKB4, YKB14, S25, YFB20, YFO21, and YFO22) showed the same biochemical characteristics as a reference strain [V. parahaemolyticus KCTC 2471 (urease-negative)], except for urease production. The 6 urease-positive strains showed different urease activities in their culture supernatant during the growth. The urease activity of S25 increased sharply at the late exponential phase, and was the highest at the initial stationary phase and was kept until the late stationary phase. The other 5 isolates, except C25, showed urease activities at the mid-stationary phase and increased steadily until the late stationary phase, when the urease activity was maximal. To compare the degree of virulence of V. parahaemolyticus with different pathogenic factors, hemolysin, protease, or urease-positive strains were injected into groups of 10 each of ICR mice (7- to l0-week-old males). The lethal rates of urease-positive V. parahaemolyticus, YKB14, YKB4, and S25, were significantly high, being 50, 70, and 80%, respectively. Protease-positive V. parahaemolyticus strains FM39 and FM50 showed 40% and 60% of lethal rate, respectively. Hemolysin-positive V. parahaemolyticus strains S34 and S72 had no mortality, similar to nonpathogenic V. parahaemolyticus FM12.

• Journal of Life Science
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• v.13 no.1
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• pp.67-72
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• 2003

Helicobacter pylori is the etiologic agent of human gastritis and peptic ulceration and produces urease as the major protein component on its surface. H. pylori urease is known to serve as a major virulence factor and a potent immunogen. Recombinant H. pylori urease expressed in E. coli was purified by simple purification procedures utilizing (CNBr-activated Sepharose-anti-urease IgG immunoaffinity chromatography or epoxy- activated Sepharose-urea affinity chromatography. Urease was apparently bound so tightly to the anti-urease IgG resin that it could not be eluted at various elution conditions except at certain extreme pH 1, including 100 mM carbonate (pH 10.5) buffer solution, which was shown to elute slightly inactivated but relatively pure enzyme. Urease eluted from the epoxy-activated Sepharose-urea affinity column showed higher activity, but the smaller UreA subunit of the enzyme appeared as a Fainter band of diminished intensity when subjected to SDS-polyamide gel electrophoresis.

• Korean Journal of Soil Science and Fertilizer
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• v.21 no.1
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• pp.73-78
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• 1988

A laboratory experiments were carried out to study the urea transformation and kinetics of soil urease in paddy soils with different properties. Urea transformation in paddy soils followed first-order kinetics, the rate of urea hydrolysis and the first-order constant was higher in the soil with high total urease activity (TUA) and accumulated urease activity (AUA) than those with low TUA and AUA. The values of Km and Vmax indicated that the Km values of accumulated urease in the soils were different in each soils and lower than that of microbial urease. However, the Km values of microbial urease were nearly same each other.

• Journal of Life Science
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• v.10 no.1
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• pp.94-100
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• 2000

Urease is an important microbial enzyme and its production is a marker to predict potential pathogenicity. An unusual halophilic bacterium producing urease was isolated from sea product and identified as Vibrio parahaemolyticus KH410. Its biochemical properties were indole negative, gelatin positive, sodium citrate positive and Kanagawa positive whereas other characteristics were identical as the standard strain except it showed a positive reaction on Christensen's urea agar. V. parahaemolyticus urease production was directly related to urea concentration. The production of urease was noticeable by the addition of 0.2% urea, 0.5% glucose, 2% NaCl in LB broth, and the initial pH of 5.5. The maximum production reached after 6 hr of incubation at 37$^{\circ}C$. However, NiCl2, metal ions, phosphorus did not affect production of urease.

• Advances in Traditional Medicine
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• v.5 no.1
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• pp.43-47
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• 2005

Jack bean urease was immobilized on gelatin beads with the help of glutaraldehyde. The optimum immobilization (67.6%) was obtained at 30mg/ml gelatin concentration, 0.5 mg/bead enzyme protein concentration, 1 % glutaraldehyde and at $4^{\circ}C$ incubation temperature. The $t_{1/2}$ of immobilized urease was approximately 90 days at $4^{\circ}C$ compared with $t_{1/2}$ of 20 days for the soluble urease, under identical condition. The apparent optimum pH shifted from 7.3 to 8.0 when the urease was immobilized. The optimum stability temperature of immobilized urease was found to be $60^{\circ}C$ while that of soluble urease was $45^{\circ}C$. Time-dependent thermal inactivation studies showed monophasic kinetics for soluble urease and immobilized urease at $70^{\circ}C$, respectively. The immobilized urease beads stored at $4^{\circ}C$ showed practically no leaching over a period of 30 days. Here we are presenting an easy and economical way of immobilizing urease on the gelatin beads making it suitable for various applications.

• Asian Journal of Turfgrass Science
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• v.6 no.1
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• pp.23-28
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• 1992

Urea, the major N source of world agriculture involves a serious urea-N loss through NH$_3$volatilization. Approaches to decrease N loss include using urease inhibitors in view of the environmental protection and the increase of urea-N efficiency. The purpose of laboratory researches was toassess the potential value of urease inhibitors to increase urea-N efficiency in soil and Kentucky blue-grass(Poa Pratensis L.) turf. The activity of urease inhibitors Phenyiphosphorodiamjdate(ppD) and N-(n-butyl) thiophosphoric triamjde(NBPT) measured to break-down ammonia volatilization. The soil and turf used in this project were from the fairway in one of the Korean gof course. The researches were carried out for two weeks to measure the urease activities on urea hydrolysis under four temperatures (10~ 40$^{\circ}C$) and for one week on turfgrass using forced-draft system. Results indicated that Urea-N involves considerable loss through gaseous NH$_3$ by urease activities in plant-soil systems. Urease inhibitors PPD and NBPT have potential value for increasing N use efficiency by reduing NH$_3$ volatilization. NBPT deserves futher evaluation as fertilizer amendment than PPD use of urea in turf industries.

• Journal of Pharmaceutical Investigation
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• v.15 no.3
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• pp.93-99
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• 1985

For the effective immobilization of urease on chitosan matrix with glutaraldehyde, optimal activation methods were studied, and its enzymatic properties was investigated. In the stability of enzyme. the retained activity of the native urease was 55% after it was soaked af pH 7 for 10 hrs., while the retained activity of immobilized one was about 62% after soaked at pH 6.5-8.5 for the same time. After heat treatment at $60^{\circ}C$ for 10 hrs., the native urease lost the most of its activity, while immobilized urease retained 54% of its activity by the same treatment. The retained activity of immobilized urease did not decrease nearly when it was stored at room temperature for 25 days. From Linweaver-Burk plots, the $V_{max}$ value of native urease was $66{\mu}M/l$ and that of immobilized urease was $41{\mu}M/l$, while Km value 40mM/l for both enzymes was unaltered.

• Korean Journal of Pharmacognosy
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• v.36 no.1 s.140
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• pp.56-59
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• 2005

Urease plays an important role in the urea metabolism and the effect of urease activity on human and environment is enormous. For instance, urease acts as a virulence factor of the urinary and gastrointestinal tracts infections in human and animal, being involved in kidney stone formation, catheter encrusatation, pyelonephritis, ammonia encephalopathy, hepatic coma, and urinary tract infections. Widespread urease activity in soil induces a plant damage due to ammonia toxicity and pH increase. Therefore, urease activity regulation through urease inhibitors would lead to an enhanced efficiency of urea nitrogen uptake in plants and to the improved therapeutic strategies for ureolytic bacterial infections. To search for new inhibitory compounds on urease activity from herbs, MeOH extracts of herbs were screened. Among of them, the MeOH extracts of Areca catechu exhibited an excellent inhibitory effect on urease activity. Two compounds were isolated from the ethyl acetate fraction by the activity guided fractionation. Their chemical structures were identified as (+)-catechin(compound I) and allantoin(compound II) by spectroscopic evidence, respectively. Compound I showed a stronger inhibitory effect on urease activity than compound II.