• Journal of Microbiology and Biotechnology
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• v.18 no.5
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• pp.997-1003
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• 2008

Viral safety is a prerequisite for manufacturing clinical antihemophilic factor VIII concentrates from human plasma. With particular regard to the hepatitis A virus (HAV), a terminal dry-heat treatment ($100^{\circ}C$ for 30 min) process, following lyophilization, was developed to improve the virus safety of a solvent/detergent-treated antihemophilic factor VIII concentrate. The loss of factor VIII activity during dry-heat treatment was of about 5%. No substantial changes were observed in the physical and biochemical characteristics of the dry-heat-treated factor VIII compared with those of the factor VIII before dry-heat treatment. The dry-heat-treated factor VIII was stable for up to 24 months at $4^{\circ}C$. The dry-heat treatment after lyophilization was an effective process for inactivating viruses. The HAV, murine encephalomyocarditis virus (EMCV), and human immunodeficiency virus (HIV) were completely inactivated to below detectable levels within 10 min of the dry-heat treatment. Bovine herpes virus (BHV) and bovine viral diarrhea virus (BVDV) were potentially sensitive to the treatment. However porcine parvovirus (PPV) was slightly resistant to the treatment. The log reduction factors achieved during lyophilization and dry-heat treatment were ${\geq}5.55$ for HAV, ${\geq}5.87$ for EMCV, ${\geq}5.15$ for HIV, 6.13 for BHV, 4.46 for BVDV, and 1.90 for PPV. These results indicate that dry-heat treatment improves the virus safety of factor VIII concentrates, without destroying the activity. Moreover, the treatment represents an effective measure for the inactivation of non-lipid-enveloped viruses, in particular HAV, which is resistant to solvent/detergent treatment.

• Journal of Microbiology and Biotechnology
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• v.17 no.3
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• pp.524-529
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• 2007

Pressure inactivation behavior of Bacillus amyloliquefaciens spores was investigated in deionized water. The spores of B. amyloliquefaciens were subjected to $105^{\circ}C$ and 700 MPa. The magnitude of the decrease in viability after pressure treatment was similar to that after pressure treatment followed by heat shock. The increase of dipicolinic acid (DPA) release was correlated with the spore inactivation, and the hydrophobicity did not significantly change during the pressure-assisted thermal processing (PATP). Lag phase duration increased with increasing pressure process time. The mechanisms of spore germination and inactivation during the PATP were related to a complex physiological process.

• Journal of the Korean Society of Food Science and Nutrition
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• v.40 no.10
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• pp.1469-1473
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• 2011

The efficacy of antimicrobial agents and heat treatments on spore inactivation was investigated. Grapefruit seed extract (GFE) and ethylenediaminetetraacetic acid (EDTA) were used and as antimicrobial agents, and heat treatments were conducted at $70^{\circ}C$, $80^{\circ}C$, and $90^{\circ}C$ for 30 minutes. Heat treatments at $90^{\circ}C$ were the most effective on spore inactivation as a single treatment and caused a 2.3 log reduction. When combined with a single treatment to discover synergistic effects, 1% GFE with $80^{\circ}C$ heat treatments and 0.5 mM EDTA with $80^{\circ}C$ heat treatments resulted in 2.1 log and 3.2 log reductions, respectively, though they did not show reductions at each single treatment (GFE 1% (v/v), EDTA 0.5 mM, $80^{\circ}C$). So it was concluded that by combining GFE, EDTA in low concentration treatment, and heat treatment, B. cereus spores can be effectively inactivated.

• Journal of Microbiology and Biotechnology
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• v.21 no.2
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• pp.212-217
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• 2011

${\alpha}$ and ${\beta}$-subunits (ApCpnA and ApCpnB) are group II chaperonins from the hyperthermophilic archaeum Aeropyrum pernix K1, specialized in preventing the aggregation and inactivation of substrate proteins under conditions of transient heat stress. In the present study, the cooperativity of ${\alpha}$- and ${\beta}$-subunits from the A. pernix K1 was investigated. The ApCpnA and ApCpnB chaperonin genes were overexpressed in E. coli Rosetta and Codonplus (DE3), respectively. Each of the recombinant ${\alpha}$- and ${\beta}$-subunits was purified to 92% and 94% by using anionexchange chromatography. The cooperative activity between purified ${\alpha}$- and ${\beta}$-subunits was examined using citrate synthase (CS), alcohol dehydrogenase (ADH), and malate dehydrogenase (MDH) as substrate proteins. The addition of both ${\alpha}$- and ${\beta}$-subunits could effectively protect CS and ADH from thermal aggregation and inactivation at $43^{\circ}C$ and $50^{\circ}C$, respectively, and MDH from thermal inactivation at $80^{\circ}C$C and $85^{\circ}C$. Moreover, in the presence of ATP, the protective effects of ${\alpha}$- and ${\beta}$-subunits on CS from thermal aggregation and inactivation, and ADH from thermal aggregation, were more enhanced, whereas cooperation between chaperonins and ATP in protection activity on ADH and MDH (at $85^{\circ}C$) from thermal inactivation was not observed. Specifically, the presence of both ${\alpha}$- and ${\beta}$- subunits could effectively protect MDH from thermal inactivation at $80^{\circ}C$ in an ATP-dependent manner.

• Journal of Microbiology
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• v.34 no.2
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• pp.158-165
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• 1996

The signal transduction pathways through the RAS gene product and adenyl cyclease play a critical role in regulation of the cell cycle in yeast, Saccharomyces cerevisiae. We examined the genetic relationship between the spt3 gene and ras/cAMP pathway. A mutation in the SPT3 gene suppressed cell cycle arrest at the G1 phase caused by either an inactivation of the RAS or CYR1 gene which encodes a yeast homologue of human ras proto-oncogene or adenyl cyclase, respectively. The phenotypes such as sporulation and heat shock resistancy, that resulted from a partial inactivation of the RAS or CYR1 genes, were also suppressed by the spt3 mutation. Expression of the SSA1 gene encoding one of th heat shock proteins (Hsp70) can be induced by heat shock or nitrogen starvation. Expression of this gene is derepressed in cry1-2 and spt3 mutants. The bcy 1 mutation repressed by the bcy1 mutation, but not in spt3 mutants. These results suggest that the SPT gene is involved in expression of genes that are affected by the RAS/cAMP pathway.

• Korean Journal of Food Science and Technology
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• v.28 no.4
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• pp.790-795
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• 1996

Citrus juice was treated with supercritical carbon dioxide $(SC-CO_{2})$ as an alternative to heat for pectinesterase (PE) inactivation to minimize undesirable changes in flavor, color and ascorbic acid loss caused by the current heat treatment, and the effect of temperature $(40,\;50,\;60^{\circ}C)$, pressure (138, 276 bar) and process time $(5{\sim}130\;min) $ on PE activity was determined. PE in temperature control samples was inactivated by 54% at $40^{\circ}C$ after 130 min, 84% at 50% after 60 min and 83% at $60^{\circ}C$ after 30 min treatment compared to the original juice. PE inactivation in $(SC-CO_{2})$ treated samples at 138 bar was 83% at $40^{\circ}C$ after 130 min, 88% at $50^{\circ}C$ after 20 min and 87% at $60^{\circ}C$ after 10 min. %PE inactivation due to pressure was higher at low temperature and lower at high temperature. Higher temperature, Pressure and longer process time resulted in higher %PE inactivation. Nonlinearity in the curves of PE inactivation at different temperatures and pressures indicated that at least two forms of PE existed in citrus juice with different stabilities.

• Journal of the Korean Society of Food Science and Nutrition
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• v.46 no.10
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• pp.1265-1269
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• 2017

This study was performed to evaluate the effects of combined treatment of clove bud essential oil (CBEO) and mild heat (MH) on inactivation of Escherichia coli O157:H7 inoculated onto red oak leaves. Combined treatment of 0.2% CBEO with MH at $50^{\circ}C$ exhibited the highest inhibitory effect against E. coli O157:H7 among treatments, resulting in 1.45 log reduction compared with water washing treatment. In addition, inhibitory effect of the combined treatment was maintained during storage of red oak leaves at $4^{\circ}C$ for 9 days, showing 1.67~2.25 log reductions compared with non-treated samples. Thus, these results indicate that combined treatment with CBEO/MH can be used to ensure the microbiological safety of fresh leaf vegetables such as red oak leaves during storage.

• The Plant Pathology Journal
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• v.17 no.6
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• pp.389.2-389
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• 2001

• Korean Chemical Engineering Research
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• v.44 no.1
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• pp.92-96
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• 2006

Enzymes in organic media afford many advantages such as chiral synthesis and resolution, modification of fats and oils and production of biodegradable polymers. However, the nature of solvents influences the activity and stability of enzymes, and the presence of organic solvents always constitute a risk of enzyme inactivation. Heat-shock protein Hsp90, one of the molecular chaperone, was applied for understanding of enzyme inactivation and for increasing of enzyme stability in water-miscible organic solvent. Hsp90 showed stabilization effect on HRP in the 30％ of DMSO, in the 30％ and 50％ of dioxane. Hsp90 also showed reactivation effect on the inactivated HRP by water-miscible organic solvent such as dioxane and DMSO. In addition, structural analysis using fluorescence spectrophotometry and circular dichroism showed that exposure of HRP in water-miscible organic solvent caused appreciable conformational changes and enzyme inactivation, and the unfolded HRP by water-miscible organic solvent was refolded by Hsp90.

• The Korean Journal of Zoology
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• v.17 no.3
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• pp.107-116
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• 1974

The metabolism of CdR-2-$^14 C$ and UdR-2-$^14 C$ in mouse small intestine has been studied in connection with the effect of heat treatment on the enzymes concerned in vitro. CdR-2-$^14 C$ is deaminated reaidly by CdR-aminohydrolase at nucleoside level and then degraded into U by the action of nucleosidase which is quite resistant to cleave N-pentose bond of cytosine nucleosides, CdR and CR. High inactivation temperature of $80^\\circC$ was observed for CdR-aminohydrolase, while nucleosidase has an inactivation temperature of $60^\\circC$. CdR-aminohydrolases in various tissues of mouse were inactivated at $80^\\circC$, but not one in tissues of rabbit. It might be assumed that there are correlations between order specificity and inactivation temperature of the enzyme. A physiological significance of the appearance of CdR-aminohydrolase in differentiated tissues of mammals possibly be regarded as a main function in catabolic pathways.