• Food Science and Biotechnology
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• v.15 no.4
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• pp.499-505
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• 2006

Clostridium botulinum spores are widely distributed in nature. Type A and proteolytic type B bacteria produce heat-resistant spores that are primarily involved in most of the food-borne botulism outbreaks associated with low-acid canned foods. Food-borne botulism results from the consumption of food in which C. botulinum has grown and produced neurotoxin. Growth and toxin production of type A and proteolytic type B in canned foods can be prevented by the use of thermal sterilization alone or in combination with salt and nitrite. The hazardousness of C. botulinum in low-acid canned foods can also be reduced by preventing post-process contamination and introducing hazard analysis and critical control point (HACCP) practices during production. Effectiveness of non-thermal technologies such as high pressure processing with elevated process temperatures on inactivation of spores of C. botulinum will be discussed.

• Food Science of Animal Resources
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• v.32 no.6
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• pp.713-717
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• 2012

The objective of this study was to evaluate the effect of sodium habituation on thermal resistance of Staphylococcus aureus in various ready-to-heat (RTH) sauces. The strain mixture of S. aureus strains KACC10768, KACC10778, KACC11596, KACC13236 and NCCP10862 was habituated up to 9% of NaCl. The inocula of NaCl-habituated and non-habituated S. aureus were inoculated in 5 g portions of pork cutlet, meat and Carbonara sauces at 7 Log CFU/g, and the samples were vortexed vigorously. The inoculated samples were then exposed to 60 and $70^{\circ}C$ in a water-bath, and survivals of total bacteria and S. aureus were enumerated on tryptic soy agar and mannitol salt agar, respectively, every 30 min for 120 min. At 60oC, the cell counts of total bacteria and the significant difference in survivals between sodium-habituated and non-habituated S. aureus were observed only in the Carbonara sauce; the tailing effect, which is the period of no reduction of bacterial cell counts, was observed in pork cutlet, meat and Carbonara sauces subjected to $60^{\circ}C$. At $70^{\circ}C$, total bacterial populations and sodium-habituated and non-habituated S. aureus cell counts in meat and Carbonara sauce also significantly decreased (p<0.05) after 30 min of heat treatment, followed by the obvious tailing effect. Sodium-habituated S. aureus cell counts in meat and Carbonara sauces were higher (p<0.05) than those of non-habituated S. aureus at $70^{\circ}C$. The results indicate that sodium habituation of S. aureus cells may increase the thermal resistance of the pathogen in RTH sauces; moreover, heating RTH sauces for a short time before serving may not sufficiently decrease the cell counts of S. aureus, particularly for sodium-habituated strain.

• Journal of Microbiology and Biotechnology
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• v.20 no.7
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• pp.1077-1085
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• 2010

With an emphasis on its thermal behavior with different pHs and salts, the kinetic and thermodynamic parameters of the purified polygalacturonase (PG) from E. carotovora subsp. carotovora (Ecc) BR1 were studied, as the characterization of an enzyme is significant in the context of burgeoning biotechnological applications. The thermodynamic parameters for polygalacturonic acid hydrolysis by the purified PG were ${\Delta}H^*$=7.98 kJ/mol, ${\Delta}G^*$=68.86 kJ/mol, ${\Delta}S^*$=-194.48 J/mol/K, ${\Delta}G_{E-S}$=-1.04 kJ/mol, and ${\Delta}G_{E-T}$=-8.96 kJ/mol. In addition, its turnover number ($k_{cat}$) was 21/sec. The purified PG was stable within a temperature range of $20-50^{\circ}C$ and was deactivated at $60^{\circ}C$ and $70^{\circ}C$. The thermodynamic parameters (${\Delta}H^*$, ${\Delta}G^*$, ${\Delta}S^*$) for the irreversible inactivation of the PG at different temperatures ($30-60^{\circ}C$) were determined, where the effectiveness of various salts and different pHs (4-8) for the thermal stability of the PG were also characterized. The efficacy of various salts for the thermal stability of the PG was in the following order: $MgCl_2$ > $BaCl_2$ > KCl > $CaCl_2$ >NaCl. Therefore, the present work presents the biochemical, substrate hydrolysis thermodynamics and the thermal stabilization parameters of the PG from Ecc.

• Journal of Food Hygiene and Safety
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• v.23 no.2
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• pp.157-162
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• 2008

Enterobacter sakazakii was initially referred to as yellow-pigmented Enterobacter cloacae and reclassified in 1980. E. sakazakii infection cause life-threatening meningitis, septicemia, and necrotizing enterocolitis in infants. Powdered infant formula (PIF) and baby foods may be the important vehicle of E. sakazakii infection. It has been reported that E. sakazakii was isolated from PIF and sunsik ingredients produced in Korea. Some infants have been fed sunsik as a weaning diet. Therefore, it is necessary that this organism should be inactivated on preparing PIF and sunsik at homes and in hospitals. The cocktail of three Korean E. sakazakii strains (human, sunsik and soil isolates) were used to investigate the inactivation of this organism with hot water at 50, 60, 65, 70 and $80^{\circ}C$ and microwave heating for 60, 75, 90, 105 and 120 sec. Reconstituted PIF and sunsikwere inoculated with cocktailed vegetative cells of E. sakazakii at 6 log CFU/mL. Thermal inactivation of vegetative cells of E. sakazakii were achieved by reconstituted PIF and sunsik with hot water at $60^{\circ}C$ or greater and with microwave heating at 2,450 MHz for 75 sec or longer. Considering that biofilm formation of E. sakazakii was adapted to survive the dry environment that is PIF and sunsik and thermal resistance increased, it is suggested that inactivation of E. sakazakii was used by hot water at $70^{\circ}C$ or greater and microwave heating for 90 sec or longer. Reconstituted PIF and sunsik were inoculated with cocktailed vegetative cells of E. sakazakii at 2 to 3 log CFU/mL to investigate the growth curve of this organism and stored at 5, 10, 15, 20, 25, 30 and $35^{\circ}C$. Viable counts slightly changed at 5, $10^{\circ}C$ during 48 h but grew at $15^{\circ}C$ or greater. Considering that E. sakazakii is able to grow in infant formula milk at refrigerator temperature, reconstituted PIF and sunsik that are not immediately consumed should be discarded or stored at refrigeration temperatures within 24 h.

• Korean Journal of Food Science and Technology
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• v.47 no.5
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• pp.593-598
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• 2015

This study determined the thermal resistance of Bacillus cereus, Escherichia coli O157:H7, and Listeria monocytogenes in multi-grain soymilk and proposes processing conditions that meet the national standard for retort food products in Korea. D and z values were calculated from thermal inactivation kinetic curves after heating at 55, 60, and $65^{\circ}C$. The D value for B. cereus at $55^{\circ}C$ was the highest (22.8 min), followed by that for E. coli O157:H7 (18.8 min) and L. monocytogenes (17.6 min). At $60-65^{\circ}C$, the order was L. monocytogenes ($D_{60-65^{\circ}C}=3.4-0.9min$), E. coli O157:H7 (3.0-0.3 min), and B. cereus (1.2-0.3 min). The z values for these species were 5.2, 5.5, and $7.7^{\circ}C$, respectively. The Korean national standard for retort food products was achieved by thermal processing at $124{\pm}2^{\circ}C$ for 0.3-2.2 min. This study provides useful data for ensuring both the microbiological safety and product quality of multi-grain soymilk products.

• Korean Journal of Food Science and Technology
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• v.12 no.3
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• pp.209-215
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• 1980

Proteases from papaya latex were partially purified by ammonium sulfate precipitation and separated into two fractions (Fraction I and II ) by carboxymethyl cellelose column chromatography. Each fraction, mixture of the two fractions, and crude extract of the papaya latex at pH 7.0 were inactivated at the range of $60{\sim}90^{\circ}C$ and thermal properties of the enzymes were investigated. In the thermal inactivation of fraction I, the enthalpy of activation was 89.5 kJ/mol; the entropy of activation, -44.0 J/mol K; the free energy of activation, 104.6 kJ/mol; z-value, $25^{\circ}C$. For fraction II, the enthalpy of activation was 96.5 kJ,/mol; the entropy of activation, -22.0 J/mol K; the free energy of activation, 104.0 kJ/mol; z-value, $23^{\circ}C$. For the mixture of fraction I and II, the enthalpy of activation was 90.9 kJ/mol; the entropy of activation, -38.8 J/mol·K; the free energy of activation, 104.2 kJ/mol; z-value, $24.6^{\circ}C$. For crude extract, the enthalpy of activation was 113.8 kJ/mol; the entropy of activation, 22.0 J/mol·K; the free energy of activation, 106.2 kJ/mol; z-value, $23.2^{\circ}C$. It was indicated that the fraction I was more heat-stable than the fraction II and this suggested that the thermal stability of the proteases in papaya latex is probably due to the fraction I.

• Korean Journal of Food Science and Technology
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• v.34 no.6
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• pp.1067-1072
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• 2002

Peroxidase was used as a standard enzyme to determine optimum blanching conditions of Flammulina velutipes and Lyophyllum ulmarium. Crude peroxidase extracted from raw mushrooms had maximum activity at $10{\sim}15^{\circ}C$ and pH 5.5 (50 mM, potassium phosphate buffer) using substrates of $H_2O_2$ and p-Phenylendiamine. Thermal inactivation of the crude peroxidase followed the first-order kinetics. The activation energy and z value of the crude peroxidase for F. velutipes were 59.58 kcal/mol and $9.0^{\circ}C$, whereas were 43.05 kcal/mol and $12.4^{\circ}C$ for L. ulmarium, respectively. On the basis of thermal kinetics parameters obtained, the optimum blanching conditions for F. velutipes and L. ulmarium were 1 min at $70^{\circ}C$ and 5 min at $80^{\circ}C$, respectively. Activation energies and z values of peroxidases extracted from heat-treated mushrooms were 7.97 and 6.55 kcal/mol, and $59.8^{\circ}C\;and\;74.1^{\circ}C$ for F. velutipes and L. ulmarium, respectively.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2004.04b
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• pp.30-33
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• 2004

Shallow p+-n junctions were formed by low-energy ion implantation and dual-step annealing processes The dopant implantation was performed into the crystalline substrates using $BF_2$ ions. The annealing was performed with a rapid thermal processor and a furnace. FA+RTA annealing sequence exhibited better junction characteristics than RTA+FA thermal cycle from the viewpoint of junction depth. A new simulator is designed to model boron diffusion in silicon, which is especially useful for analyzing the annealing process subsequent to ion implantation. The model which is used in this simulator takes into account nonequilibrium diffusion, reactions of point defects, and defect-dopant pairs considering their charge states, and the dopant inactivation by introducing a boron clustering reaction. Using a resonable parameter values, the simulator covers not only the equilibrium diffusion conditions but also the nonequilibrium post-implantation diffusion. Using initial conditions and boundary conditions, coupled diffusion equation is solved successfully. The simulator reproduced experimental data successfully.

• Food Science of Animal Resources
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• v.39 no.6
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• pp.863-876
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• 2019

The thermal-death times of Listeria monocytogenes were determined in inoculated restructured goat steak at 60℃, 65℃, and 70℃ of sous-vide temperatures. D-values of L. monocytogenes in inoculated restructured goat steak ranged from 7.27 min at 60℃ to 0.46 min at 70℃. Times need to yield at least a 6 log reduction of L. monocytogenes at their temperatures for this product were 47, 12, and 3 min, respectively. After sous-vide, all microbial counts in non-inoculated samples were not detectable, except the aerobic and anaerobic mesophilie and lactic acid bacteria counts were lower than 2 Log CFU/g. For sous-vided and grilled sous-vided samples, sous-vide loss and surface shrinkage were the lowest in samples sous-vided at 60℃ for 47 min (p<0.05). These samples demonstrated the lowest CIE L^*, shear force, hardness, gumminess and chewiness and the highest CIE a^* and hue angle (p<0.05). Therefore, sous-vide at 60℃ for 47 min provided convenient ready-to-cook restructured goat steak for microbiology safety and optimization of physicochemical quality.

• KSBB Journal
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• v.13 no.5
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• pp.502-510
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• 1998

Stabilization of antibody, which is specific to Salmonella typhimurium antigens, present in dry states on membranes was accomplished, and its shelf-life, i.e., duration for maintaining minimum 90% of the initial activity, under optimal conditions was determined. To prepare two major components of an immuno-strip, the antibody was not only immobilized on nitrocellulose membrane surfaces but also placed within the pores of glass fiber membrane after conjugating it with old colloids as signal generator. Among potential stabilizers of the immuno-components, a disaccharide, trehalose, showed a significant protection effect of immunoglobulin structure from thermal energy. Optimal concentrations of trehalose for the respective component were significantly different (8-fold higher for the antibody-gold conjugate than for the immobilized antibody), which probably resulted from distinct densities and configurations of antibody present on the membranes. An additional requirement for the gold conjugate was freeze-drying of this substance such that the conjugate can be readily resolubilized upon contact with aqueous medium. By using the components prepared under optimal conditions, immuno-strips were constructed and exposed to thermal energy. Signals with less than 10% decrease in the intensity were maintained for approximately 21 days at 60$^{\circ}C$. Compared to previous reports, this result represented a 2-year shelf-life at room temperature. it was, however, two times longer if determined from thermal acceleration tests based on the theory of inactivation rate of protein. Such discrepancy between the two estimates could be mainly attributed to errors in accurately controlling temperatures and also to changes in the physical properties of membranes due to a high thermal energy.