• Korean Journal of Soil Science and Fertilizer
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• v.43 no.1
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• pp.90-95
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• 2010

The application of livestock manure to cropland is a practice that has been used for centuries. Agricultural crops can utilize nutrients from manure, and the producer can utilize land for disposal, although in a "sustainable system" the concept is manure utilization and not waste disposal. However, meeting regulatory criteria regarding microbial quality remains an expensive and time consuming process. The purpose of this study was to quantify the level of environmental impact of soil moisture and temperature on fecal coliform (Escherichia coli or E. coli) survival in upland soils for sound application of livestock manure. Samples were collected up to 30 days depending on the given conditions. The inactivation rate of E. coli increased linearly with increased temperature while the inactivation rate gradually decreased with decreased soil moisture level. The overall findings of this study showed that the temperature was the limited factor on E. coli survival in soils over soil moisture content. This study will provide useful and practical guidelines to applicators of soil in deciding appropriate handling and time frames for land application for sustainable agriculture.

• BMB Reports
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• v.32 no.5
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• pp.515-520
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• 1999

Incubation of two types of glutamate dehydrogenase isoproteins from bovine brain with the arginine-specific dicarbonyl reagent phenylglyoxal resulted in a biphasic loss of enzyme activity. Reaction of the glutamate dehydrogenase isoproteins with phenylglyoxal caused a rapid loss of 53~62% of the enzyme activities and modification of two residues of arginine per enzyme subunit. Prolonged incubation of the glutamate dehydrogenase isoproteins with phenylglyoxal resulted in the modification of an additional four residues of arginine per enzyme subunit without further loss of the residual activities. Partial protection against inactivation was provided by the coenzyme NADH or substrate 2-oxoglutarate. The most marked decrease in the rate of inactivation was observed by the combined addition of NADH and 2-oxoglutarate, suggesting that the first two modified arginine residues are in the vicinity of the catalytic site. However, inactivation of the glutamate dehydrogenase isoproteins by phenylglyoxal appears to be partial with approximately 40% activity remained after an extended reaction time with excess reagent, suggesting that the modified arginine residues may not be directly involved in catalysis. The lack of complete protection by substrates also suggest the possibility that the modified arginine residues are not directly involved at the active site, and the partial loss of activity by the modification of arginine residues may be due to a conformational change. There were no significant differences between the two glutamate dehydrogenase isoproteins in sensitivities to inactivation by phenylglyoxal, indicating that the microenvironmental structures of the glutamate dehydrogenase isoproteins are very similar to each other.

• Korean Journal of Microbiology
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• v.18 no.3
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• pp.123-132
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• 1980

Bacterial virus f2 and its RNA were examined to elucidate the mode of ozone utilizing sucrose density gradient analysis and electtron microscopic techniques. the inactivation kinetics of the virus f2 by ozonation showed that the viruses were inactivated during the first 5 sec of the reaction and were further inactivated at a slower rate during the next 10 min at 0.09 and 0.8mg/l ozone concentrations. The virus coat was broken by ozonation into many pieces of protein subunits and the adsorption of the viruses to the host pili was inversely related to the extent of the breakage of the virus. The viral RNA was released from the virus particles during ozone, but ozone inactivation of the RNA enclosed in the protein coat could not ruled out the possibility that the RNA was secondarily sheared by a reaction with the broken coat protein.

• Korean Journal of Veterinary Research
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• v.11 no.2
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• pp.137-140
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• 1971

Survival and thermal inactivation after heat treatment at $143^{\circ}F$ were observed among 27 strains of coliform bacteria isolated from dairy cattle. The results obtained were as follows. 1. The obvious differences in heat-sensitivity were observed among the strains tested. 2. No strain was found resistant to the heat treatment of $143^{\circ}F$ for 30 minutes. 3. A marked effect of density of coliform bacteria on the survival after the heat treatment was observed. As the density of coliform bacteria was increased, the rate of survival was increased markedly regardless of the length of heat treatment.

• BMB Reports
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• v.36 no.4
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• pp.359-366
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• 2003

The effects of zinc on arginine kinase and its collapsed-state intermediate were studied. Both arginine kinase and the collapsed-state intermediate were inactivated in the presence of zinc, following a biphasic kinetic course. The corresponding apparent rate constants of inactivation at different zinc concentrations and conformational changes in the presence of 0.5 mM zinc were obtained. The conformational changes of arginine kinase and the collapsed-state intermediate were followed by fluorescence spectra and circular dichroism spectra. Comparison of the results for arginine kinase and the collapsed-state intermediate showed that the collapsed-state intermediate was more susceptible to zinc, which indicated that the collapsed-state intermediate was more flexible and unstable than arginine kinase. The special structure of arginine kinase might explain these diverse phenomena.

• Journal of the Korean Society of Food Science and Nutrition
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• v.19 no.4
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• pp.301-304
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• 1990

Factors affecting thermal inactivation and reactivation of korean radish peroxidase were inves-tigated,. The enzyme was stable below pH4.0 and above pH 8.0 The thermostablity of the enzyme was increased by addition of glucose sodium chloride and albuminl The inactivated enzyme by heat treatment was reactivated at room temperaturem The optimal pH for reactivation of the enzyme was pH of 9.0 The reactivation rate of the enyme was not afected by addition of glucose sodium chloride and albumin, The reactivation was completely inhibited by addition of sulfhydryl reagent such as dithiothreitol.

• BMB Reports
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• v.31 no.2
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• pp.139-143
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• 1998

The catabolic ${\alpha}-acetolactate$ synthase purified from Serratia marcescens ATCC 25419 was rapidly inactivated by the tryptophane-specific reagent, N -bromosuccinimide, and the arginine-specific reagent, phenylglyoxal. The enzyme was inactivated slowly by the cysteine-specific reagent N-ethylmaleimide. The second-order rate constants for the inactivation by N-bromosuccinimide, phenylglyoxal. and N -ethylmaleimide were $114,749M^{-1}min^{-1}$, $304.3M^{-1}min^{-1}$, and $5.1M^{-1}min^{-1}$, respectively. The reaction order with respect to N-bromosuccinimide, phenylglyoxal, and N-ethylmaleimide were 1.5,0.71, and 0.86, respectively. The inactivation of the catabolic aacetolactate synthase by these modifying reagents was protected by pyruvate. These results suggest that essential tryptophane, arginine, and cysteine residues are located at or near the active site of the catabolic ${\alpha}-acetolactate$ synthase.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.05a
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• pp.198-201
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• 2004

To investigate hydrostatic pressure (HP) effect on myofibrillar protein (Mf) extracted from bovine Semitendinosus muscle, Ca- and Mg-ATPase activities to evaluate denaturation of myosin and actin, and soluble protein contents were observed. In Mf treated with 100 MPa for 5 min was not observed denaturation of myosin and actin. In Mf treated with 200 MPa for 5 min, denaturation of myosin and actin were observed but inactivation rate was low (0.0136 $min^{-1}$). Inactivation rate of myosin and actin was dramatically increased above 300 MPa treatment. However denaturation of myosin and actin was not that critical with duration time. By increasing pressure size, the amount of myosin and actin in soluble protein eluted in 20 mM potassium phosphate buffer (pH 7.0) containing 0.6 M NaCl were decreased. SDS-PAGE of soluble protein released from Mf suspension in 0.1 M NaCl buffer (pH 7.0) showed that low molecular weight proteins (15${\sim}$36 KDa) were released by HP treatment above 200 MPa. From the results, denaturation of myosin and actin, and release of light molecule proteins of Mf were observed by HP treatment over 200 MPa.

• Korean Journal of Food Science and Technology
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• v.29 no.6
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• pp.1175-1183
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• 1997

Lethal effects of high voltage pulsed electric fields (PEF) on suspensions of Lactobacillus plantarum cells in phosphate buffer solution were examined by using continuous recycle treatment system. Critical electric field strength and treatment time needed for inactivation of L. plantarum were 13.6 kV/cm and $16.1\;{\mu}s$ at room temperature, respectively. As decrease in frequency (decreasing pulse number), the degree of inactivation of L. plantarum was increased. A 2.5 log reduction in microbial population could be achieved with an electric field strength of 80 kV/cm, 300 Hz frequency and $2000\;{\mu}s$ treatment time. Survivability was decreased with increase in total treatment time (cycle number) and frequency at the same cycle number. As sterilization model of continuous recycle PEF treatment, $logS=-N_m\;log\;m+B$ and $N_m=k_1\;P_n+k_2$ were established. This model was very well fitted to tile empirical data. The rate of inactivation increased with increase in the processing temperature. The maximum reduction in survivability (5.6 log reduction) was obtained with 80 kV/cm electric field strength at $50^{\circ}C$ for $1000\;{\mu}s$ treatment.

• BMB Reports
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• v.33 no.4
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• pp.317-320
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• 2000

The succinic semialdehyde dehydrogenase from bovine brain was inactivated by treatment with phenylglyoxal, a reagent that specifically modifies arginine residues. The inhibition at various phenylglyoxal concentrations shows pseudo-first-order kinetics with an apparent secondorder rate constant of 30 $M^{-1}min^{-1}$ for inactivation. Partial protection against inactivation was provided by the coenzyme $NAD^+$, but not by the substrate succinic semialdehyde. Spectrophotometric studies indicated that complete inactivation of the enzyme resulted from the binding of 2 mol phenylglyoxal per mol of enzyme. These results suggest that essential arginine residues, located at or near the coenzyme-binding site, are connected with the catalytic activity of brain succinic semialdehyde dehydrogenase.