• Korean Journal of Veterinary Service
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• v.42 no.4
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• pp.265-274
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• 2019

Delayed arrival of blood samples from the field and a large number of samples delivered often causes delay in sample analysis leading to inaccurate measurements. Therefore, this study aimed to assess whether prolonged storage in refrigerator could influence the stability of cattle blood samples and to establish an optimal time limit for complete blood count (CBC) parameters and blood gas and electrolyte (BGE) parameters analyses. Samples collected from healthy cows were tested immediately for CBC and BGE using automated hematology, blood gas and electrolyte analyzers. Samples were kept in refrigerator at 4℃ and analyzed after 6 h, 12 h, 24 h, 48 h, 72 h, 120 h, and 192 h of storage. Mean differences between observations were assessed at 5% significance level using ANOVA and Duncan's multiple range test. Total CBC parameters and the platelet profile remained stable for 192 h, except for MCHC. Among leukocyte-related counts, NEU and EOS remained stable for 192 hours. WBC and LYM, and MONO values produced inconsistent measurements which recovered its initial measurement after 12 h and 24 h of storage, respectively, then remained stable until 120 h. Among the blood gas indices, PCO₂, PO₂, tCO₂, and BE showed declining and significant changes over time, but pH, tHb, and SO₂ remained stable for 192 h. Electrolyte status in the blood showed that ions are unstable and tend to change in as early as 6 h of storage. This study established that cattle blood specimens for CBC analysis can be stored for 120 h at 4℃, but specimens for BGE analyses must be tested within 6 to 24 h.

• Proceedings of the IEEK Conference
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• 2001.10a
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• pp.448-452
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• 2001

An Experimental study was carried out to develop a simple method of processing copper waste sludge which is produced by PBC manufacturing. The procedure is based on leaching of wet sludge in 2N H$_2$SO$_4$, and the solid / liquid ratio is controlled approximately at 1/10. The recovery of copper is 85.4%, and pH of the leachate is 3.20. Adding ammonia solution into leachate forms ammine, and hydroxide compounds derived from other impurities in leachate at pH 10. The hydroxide compound can be treated by ferrite process, and the product is a stable oxide compound. Then the ammine solution is heated to evaporate ammonia, and the copper hydroxide is formed. Heating at 8$0^{\circ}C$by aeration, copper hydroxide is transformed into copper oxide with a purity of 98.4%. This process can recover most copper from sludge and the residue can be stabilized by the formation of a stable oxide compound which is not hazardous to environment.

• Journal of Microbiology and Biotechnology
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• v.22 no.8
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• pp.1092-1100
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• 2012

Ten Bacillus strains with antimicrobial activities were isolated from Cheonggukjang produced at different parts in Korea. They all inhibited Listeria monocytogenes ATCC 19111 and nine inhibited Bacillus cereus ATCC 14579. Four isolates (W42, H27, SKE 12, and K21) showing strong inhibiting activities were identified as B. subtilis. B. subtilis W42 was the most inhibiting strain. The antimicrobial activity of culture supernatant from B. subtilis W42 was destroyed completely by proteinase K treatment, indicating that a bacteriocin was the responsible agent. The bacteriocin, Bac W42, was most stable at pH 7 and stable between pH 3-6 and 8-9. Bac W42 was stable up to $80^{\circ}C$. BHI (brain heart infusion) and TSB (tryptic soy broth) were the best media for the activity (320 AU/ml) followed by LB (160 AU/ml). Bac W42 was partially purified by column chromatographies. The specific activity was increased from 1,151.2 AU/ml to 9,043.5 AU/ml and the final yield was 26.3%. Bac W42 was 5.4 kDa in size as determined by SDS-PAGE. Bac W42 showed bactericidal activity against L. monocytogenes ATCC 19111.

• Journal of Animal Science and Technology
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• v.44 no.6
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• pp.719-726
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• 2002

Nutritional adequacy of growing Thoroughbred horses raised in an alternate feeding system - grazing during late spring through late fall and stable feeding for the rest of seasons - was assessed by determining vitamin E and trace mineral levels in the serum and blood chemistry related to nutrition and health. During the stable feeding in winter and early spring, 50 growing female horses were fed concentrates (1.4% of their body weight), grass hay (0.62%) and alfalfa hay (0.37%). For the grazing period, the same horses were fed supplementary concentrates (1.1%) during late spring through early summer, and concentrates (1.1%) and alfalfa hay (0.5%) during late summer through late fall. Blood samples were collected before grazing in early spring, and during grazing in early summer through late fall. Serum vitamin E, BUN, GTP, total bilirubin and direct bilirubin levels were increased (P<0.01) by grazing compared to those measured before the initiation of grazing. Horses had lower (P<0.01) serum Fe contents in early summer than in late fall or in time of stable feeding. Stable feeding increased (P<0.01) serum Cu content compared to grazing in both early summer and late fall. In late fall, serum Zn level increased (P<0.01) compared to that found in the other seasons. Blood glucose and creatinine levels decreased (P<0.01) after grazing. Results indicate that supplementations of some minerals and vitamin E are not always necessary in diets for growing horses and should be done after careful evaluation of diets with regard to concentrations and biological availability of minerals.

• Applied Biological Chemistry
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• v.27 no.4
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• pp.271-277
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• 1984

Molecular weight of Exo-maltotetraohydrolase produced by Pseudomonas stutzeri IAM 12097 was estimated to be approrimately 63,000 and 60,000 with SDS-polyacrylamide gel electrophoresis and Sephadex-G-100 gel filtration, respectively. The isoelectric point was appeared to be pH 4.8. Optimum pH, the stable pH range and optimum temperature of this enzyme were pH 6.6, $pH6.0{\sim}10.5\;and\;45{\sim}50^{\circ}C$. The enzyme was stable below $40^{\circ}C$ and was rapidly inactivated above $55^{\circ}C$. This enzyme was inactivated completely by $Ag^+,\; Hg^{++},\;I_2$ and ${\beta}-cycoldextrin$, and slightly by EDTA, ${\rho}-CMB$ and IAA. Michaelis constant(Km) of this enzyme toward soluble starch, amylose and amylopectin were 7.70mg/ml, 6.17mg/ml, 5.56mg/ml, respectively.

• Microbiology and Biotechnology Letters
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• v.20 no.5
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• pp.534-542
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• 1992

Trypsin inhibtor produced by Streptomyces sp. S-217 was purified by solvent extraction and various column chromatographies. and physico-chemical properties of the inhibitor were investigated. Inhibitor complex was formed for incubation of 10 min. Streptomyces 5-217 showed the highest production of trypsin inhibitor when it was cultivated at $37^{\circ}C$ for 66 hr in the medium containing 2% mannitol & 0.9% peptone, pH 7.0. Trypsin inhibitor was purified by column chromatography and high performance liquid chromatography. Trypsin inhibitor indicated the maxium wavelength at 215 nm and solubilities in water, methanol and dimethyl sulfoxide were 95, 70 and 75%, respectively. The concentration of 50% inhibition ($IC^{50}$) was 15 $\mu$g/ml. The inhibitor was stable on heating at $100^{\circ}C$ for 60 min in pH 5~9 and was more stable in alkaline region than acidic region.

• Food Science and Preservation
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• v.12 no.5
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• pp.489-495
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• 2005

Polyphenol oxidase (PPO) from Burdock (Arctium lappa L.) was purified and characterized. Purification of polyphenol oxidase was achieved by ammonium sulfate precipitation, Phenyl-sepharose CL-4B hydrophobic chromatography and Sephadex G-100 gel filtration chromatography. The molecular mass of the purified PPO was estimated to be 30 kDa by SDS polyacrylamide gel electrophoresis. In a substrate specificity, maximum activity was achieved with chlorogenic acid, followed by catechol and catechin. Whereas, there was low activity with hydroquinic acid, resorcinol or tyrosine. The optimum pH and temperature for enzyme activity were 7.0 and 35$\circC$ with catechol, respectively. The enzyme was most stable at pH 7.0 while unstable at acidic and alkaline pH. The enzyme was stable when heated to 40$\circC$. But heating at 50$\circC$ for more than 30 min caused 50% loss of activity. Ascorbic acid, L-cystein and $Cu^{2+}$ inhibited the activity of pholyphenol oxidase.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.3
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• pp.279-285
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• 1992

Cytidine deaminase (EC 3.5.4.5) from Aspergillus fumigatus IFO 5840, which was the first cytidine deaminase to be found in a mold, was fractionated with ammonium sulfate (35-60%). When the enzyme solution in 0.25M of Tris-HCI buffer (pH 7.2) was preincubated at $37^{\circ}C$ for 25min, the enzyme activity was reached to maximum state. The optimum pH and temperature for the enzyme activity were found to be 6.8 to 7.2 and near $37^{\circ}C$, respectively. The enzyme was stable in a pH 7.2 to 9.0, and was generally stable at 4$0^{\circ}C$, but after treating at 6$0^{\circ}C$ for 20min at the optimal pH, 17% of the enzyme activity was inactivated, and disappeared completely by treating at 1$0^{\circ}C$ for 25min. Activation energy (Ea) of fungal cytidine deaminase was calculated as 14.190 Kcal /mol by the Arrhenius plot, and temperate coeffient ($Q_{10}$ ) of the enzyme was calculated as 2.163.

• Journal of Environmental Health Sciences
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• v.31 no.6
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• pp.498-503
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• 2005

Stability of soybean isoflavone isomers according to extraction conditions such as temperature, pH, and extracting solvents was investigated. Heating induced three chemical reactions to occur for malony1 derivatives of isoflavones, namely decarboxylation of malony1 groups into acety1 derivatives, deesterification of malony1 residues, and hydrolysis of $\beta$-glycosidic bonds. Among the twelve isoflavone isomers, change in concentrations of acety1glycosides were most pronounced: Acety1 derivatives were present only in trace amounts in unheated hypocotyls, but the content increased dramatically during heating. As for the glycosides, concentrations of daidzin and glycitin increased due to heat treatment, though that of genistin remained almost unchanged. Heat decomposition rates and the patterns differed among the three malony1 derivatives. After 120 min at $80^{circ}C$, the relative concentrations of daidzin, glycitin and genistin were increased from $9.2\%$, $12.4\%$ and $3.3\%$ to $19.3\%$, $21.9\%$ and $6.2\%$, respectively. When crude isoflavones were solubilized in glycine buffer (pH 10.0) and incubated at $80^{circ}C$, deesterification occurred faster than at pH 7.0. When the pH of isoflavone solution was increased, the malony1glycosides were hydrolyzed to their respective glycosides at increased rate. Both acetyl and aglycone forms were unchanged and only de-esterification reactions occurred. At the acidic pH, malonylglycosides were much stable both at 60 and $80^{circ}C$. However at pH 10, $80^{circ}C$ and 1 hr, $75-80\%$ of malonylglycosides were transformed to their deesterified glycosides. When isoflavones were extracted with $60\%$ aqueous ethanol at $60^{circ}C$, isoflavone isomers were stable and the deesterification reactions did not occur in these conditions. However, at $80^{circ}C$ deesterification of malonyiglycosides occurred significantly with $15-20\%$ of malonylglycosides being hydrolyzed into their respective glycosides. This experiment showed that malonylglycosides undergo decomposition when heated or exposed to alkaline conditions. Also, aqueous ethanol was preferred to aqueous methanol as solubilizing media for obtaining extract with minimum degradation of malonylglycosides.

• Korean Journal of Microbiology
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• v.30 no.2
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• pp.71-77
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• 1992

A 50 KD metalloprotease of Serratia marcesrens ATCC 21074 was purified by ammoniumsulfate precipitation. DEAE-cellulose ion exchange chromatography, and sephadex ti-100gel filtration. Optimal pH and temperature of enzyme were pH 8.0 and 37"C, respectively.This enzyme was stable in the ranges of 10-37$^{\circ}$C and pH 5.0--11.0. Thermal denaturationwas investigated by differential scanning calorimetry. Onset temperature of denaturationand endothermic peak temperature were 376$^{\circ}$C and 43.2"C. re:,pectively. The denaturationenthalpy was -8.4mJimg. The purified metalloprotease was ri.sistant to autodigestion for24 hr at 30$^{\circ}$C. Metalloprotease in culture supernatant was also resistant to autodigestionin this conditions. Heat-denatured enzyme. however. was rapidly digested by the nativeenzyme. The metalloprotease was stable to proteolytic digestion by mammalian proteasessuch as trypsin. a-chymotrypsin, and elastase. But the enzyme was easily digested bybacterial protease. thermolysin.bacterial protease. thermolysin.