• Korean Journal of Food Science and Technology
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• v.17 no.2
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• pp.75-80
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• 1985

To utilize lipase obtained from Candida cylindracea for lipid hydrolysis, methods to immobilize lipase by adsorption and reaction characteristics of the immobilized lipase by adsorption were investigated. Among the tested adsorbents, silica gel was selected as a suitable adsorbent. The optimum condition for adsorption of lipase was when 47.5 units of lipase were adsorbed to 1.6g of silica gel at pH7.0 and $5^{\circ}C$ for 100 min. Optimum pH and temperature for activity of the immobilized lipase were at $37^{\circ}C$ and pH7.0, which were same as the soluble lipase. Optimum enzyme concentration of the immobilized lipase were 30g for milk fat and 80g for olive oil, whereas those of the soluble lipase were 800 units for milk fat and 1200 units for olive oil. The optimum substrate concentrations of the immobilized and soluble lipases were 20% lipid, regardless of lipid types. Rapid hydrolysis of milk fat was observed with the soluble lipase for the initial 4 hours and with the immobilized lipase for the initial 8 hours. The immobilized lipase produced same amount of capric acid as the soluble lipase, but more myristic acid and less butyric acid than the soluble lipase.

• Applied Biological Chemistry
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• v.49 no.4
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• pp.315-321
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• 2006

Inhibitors of acetylcholinesterase(AchE), such as organophosphates and carbamates, interfere the action of AchE in nerve and may lead to a severe impairment of nerve functions or even death. Therefore, insect AchE is the biological target of predominant insecticides used in agriculture. Biosensors are sensitive and can be used as dispoisable sensors for environmental control. In recent years, the use of AchEs in biosensor technology has gained enormous attention, in particular with respect to insecticide detection. The principle of biosensors using AchE as a biological recognition element is based on the inhibition the catalytic activity by the agents to be detected. We here present a strip-type biosensor based on AchE inhibition. In this study, acetylcholinesterase and PVA-SbQ(polyvinyl alcohol functionalized with methyl pyridinium methyl sulfate) were co-immobilized on immobilone-P membranes. Immobilization of the enzymes showed a stability in 6 months without activity loss in $4^{\circ}C$ storage. Enzymes immobilized on surfaces of membrane responded to organophosphates and carbamate more sensitivitive than enzyme in solution. Organophosphates and carbamates concentrations could be detected by entrapped and surface immobilized enzymes, in 5 min. For chlorpyrifos, carbofuran, cabaryl, and methidathion, the detection limits of AChE-strip were similar to that of HPLC/GC method.

• Journal of Life Science
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• v.27 no.11
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• pp.1381-1392
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• 2017

This review described solvent-tolerant lipases and their potential industrial, biotechnological and environmental impacts. Although organic solvent-tolerant lipase was first reported in organic solvent-tolerant bacterium, many organic solvent-tolerant lipases are in not only solvent-tolerant bacteria but also solvent-intolerant bacterial and fungal strains, such as the well-known Bacillus, Pseudomonas, Streptomyces and Aspergillus strains. As these lipases are not easily inactivated in organic solvents, there is no need to immobilize them in order to prevent an enzyme inactivation by solvents. Therefore, the solvent-tolerant lipases have the potential to be used in many biotechnological and biotransformation processes. With the solvent-tolerant lipases, a large number insoluble substrates become soluble, various chemical reactions that are initially impossible in water systems become practical, synthesis reactions (instead of hydrolysis) are possible, side reactions caused by water are suppressed, and the possibility of chemoselective, regioselective and enantioselective transformations in solvent and non-aqueous systems is increased. Furthermore, the recovery and reuse of enzymes is possible without immobilization, and the stabilities of the lipases improve in solvent and non-aqueous systems. Therefore, lipases with organic-solvent tolerances have attracted much attention in regards to applying them as biocatalysts to biotransformation processes using solvent and non-aqueous systems.

• Journal of the Korean Electrochemical Society
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• v.17 no.3
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• pp.164-171
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• 2014

A highly sensitive and selective non-enzymatic glucose sensor has gained great attention because of simple signal transformation, low-cost, easily handling, and confirming the blood glucose as the representative technology. Until now, glucose sensor has been developed by the immobilization of glucose oxidase (GOx) on the surface of electrodes. However although GOx is quite stable compared with other enzymes, the enzyme-based biosensors are still impacted by various environment factors such as temperature, pH value, humidity, and toxic chemicals. Non-enzymatic sensor for direct detecting glucose is an attractive alternative device to overcome the above drawbacks of enzymatic sensor. Many efforts have been tried for the development of non-enzymatic sensors using various transition metals (Pt, Au, Cu, Ni, etc.), metal alloys (Pt-Pb, Pt-Au, Ni-Pd, etc.), metal oxides, carbon nanotubes and graphene. In this paper, we show that Ni-based nano-particles (NiNPs) exhibit remarkably catalyzing capability for glucose originating from the redox couple of $Ni(OH)_2/NiOOH$ on the surface of ITO electrode in alkaline medium. But, these non-enzymatic sensors are nonselective toward oxidizable species such as ascorbic acid the physiological fluid. So, the anionic polymer was coated on NiNPs electrode preventing the interferences. The oxidation of glucose was highly catalyzed by NiNPs. The catalytically anodic currents were linearly increased in proportion to the glucose concentration over the 0~6.15 mM range at 650 mV versus Ag/AgCl.

• Korean Journal of Soil Science and Fertilizer
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• v.49 no.5
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• pp.614-620
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• 2016

Mine soils are usually unfavorable for plant growth due to their acidic condition and low contents of organic matter and nutrients. To investigate the effect of organic material and lime on nitrogen processes in an acidic metal mine soil, we conducted an incubation experiment with treating livestock manure compost, dolomite, and oyster shell and measured soil pH, dehydrogenase activity, and concentration of soil inorganic N ($NH_4{^+}$ and $NO_3{^-}$). Compost increased not only soil inorganic N concentration, but also soil pH from 4.4 to 4.8 and dehydrogenase activity from 2.4 to $3.9{\mu}g\;TPF\;g^{-1}day^{-1}$. Applying lime with compost significantly (P<0.05) increased soil pH (5.9-6.4) and dehydrogenase activity ($4.3-7.0{\mu}g\;TPF\;g^{-1}day^{-1}$) compared with applying only compost. Here, the variation in dehydrogenase activity was significantly (P<0.05) correlated with that in soil pH. Soil inorganic N decreased with time by 14 days after treatment (DAT) due to N immobilization, but increased with time after 14 DAT. At 28 DAT, soil inorganic N was significantly (P<0.05) higher in the lime treatments than the only compost treatment. Especially the enhanced dehydrogenase activity in the lime treatments would increase soil inorganic N due to the favored mineralization of organic matter. Although compost and lime increased soil microbial biomass and enzyme activity, ammonia oxidation still proceeded slowly. We concluded that compost and lime in acidic mine soils could increase soil microbial activity and inorganic N concentration, but considerable ammonium could remain for a relatively long time.

• Korean Chemical Engineering Research
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• v.61 no.3
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• pp.407-411
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• 2023

The urease is covalently immobilized on the surface of the magnetic particles to catalyze the conversion of urea to bicarbonate anion. The conversion was confirmed qualitatively using high-pressure liquid chromatography and UV/Vis spectrometry, and analyzed quantitatively with cyclic voltammetry. The amount of conversion with respect to time was measured and analyzed by the reaction rate equation to calculate a reaction rate constant of 0.0474 min-1. In the 1 to 3 cycles, a conversion percentage of over 90% was found, and it was possible to reuse the urease 8 times up to the percentage of 50%. It was also observed that the stability evaluated for storage for 30 days was maintained. As a result of this study, it can be seen that the urease covalently immobilized on the scaffold can be used for urea removal for the purpose of producing ultrapure water.

• Journal of the Korean Society of Food Science and Nutrition
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• v.14 no.2
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• pp.164-170
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• 1985

Yellowish modified wool, dithiocarbamate(DTC) wool, was synthesized by partial hydrolysis in 0.2 N-NaOH reacting with carbon disulfide to use as ${\alpha}-amylase$ immobilization matrix. ${\alpha}-amylase$ was immobilized reacting with sulfide group of DTC-wool by covalent binding within 1 hour. 0.5 gram of this preparation, $DTC-wool-{\alpha}-amylase$, contained 150 ug of enzyme protein and its specific activity was about 90% of the native one. General properties of $DTC-wool-{\alpha}-amylase$ were a little different from optimum temperature, optimum pH, heat stability, kinetic constants and activation energy. An apparent Michaelis constant and maximum velocity of $DTC-wool-{\alpha}-amylase$ were 5.56 mg/ml and 0.37 mg/ml. $min^{-1}$ respectively, while activation energy was 16.6 kcal/mole.