• The Korean Journal of Food And Nutrition
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• v.34 no.1
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• pp.26-35
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• 2021

Myrosinases (thioglucosidases) catalyze the hydrolysis of a class of compounds called glucosinolates, of which the aglycones show various biological functions. It is often necessary to minimize the loss of myrosinase activity during thermal processing of cruciferous vegetables. Myrosinase was isolated from a popular spice, white mustard (Sinapis alba), and its thermal inactivation kinetics was investigated. The enzyme was extracted from white mustard seeds and purified by a sequential processes of ammonium sulfate fractionation, Concanavalin A-Sepharose column chromatography, and gel permeation chromatography. At least three isozymes were revealed by Concanavalin A-Sepharose column chromatography. The purity of the major myrosinase was examined by native polyacrylamide gel electrophoresis and on-gel activity staining with methyl red. The molecular weight of the major enzyme was estimated to be 171 kDa. When the consecutive step model was used for the thermal inactivation of the major myrosinase, its inactivation energy was 44.388 kJ/mol for the early stage of destruction and 32.019 kJ/mol for the late stage of destruction. When the distinct two enzymes model was used, the inactivation energy was 77.772 kJ/mol for the labile enzyme and 95.145 kJ/mol for the stable enzyme. The thermal inactivation energies lie within energy range causing nutrient destruction on heating.

• BMB Reports
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• v.36 no.2
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• pp.167-172
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• 2003

The kinetics of thermal inactivation of copper-containing amine oxidase from lentil seedlings were studied in a 100 mM potassium phosphate buffer, pH 7, using putrescine as the substrate. The temperature range was between $47-60^{\circ}C$. The thermal inactivation curves were not linear at 52 and $57^{\circ}C$; three linear phases were shown. The first phase gave some information about the number of dimeric forms of the enzyme that were induced by the higher temperatures using the "conformational lock" pertaining theory to oligomeric enzyme. The "conformational lock" caused two additional dimeric forms of the enzyme when the temperature increased to $57^{\circ}C$. The second and third phases were interpreted according to a dissociative thermal inactivation model. These phases showed that lentil amine oxidase was reversibly-dissociated before the irreversible thermal inactivation. Although lentil amine oxidase is not a thermostable enzyme, its dimeric structure can form "conformational lock," conferring a structural tolerance to the enzyme against heat stress.

• Food Science of Animal Resources
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• v.29 no.3
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• pp.310-316
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• 2009

In this study, the influence of pressure assisted mild thermal inactivation (PAMTI) on E. coli ATCC 10536 was examined at 200 MPa and temperature range of $20-50^{\circ}C$. Inactivation rate significantly increased (p<0.05) as temperature and time increased at 200 MPa. The maximum inactivation (7.91 log reduction) was obtained at $50^{\circ}C$ for 30 min under 200 MPa, which meant the complete inactivation of E. coli ATCC 10536. Inactivation kinetics were evaluated with the first order inactivation rate (k), activation energy ($E_a$), thermal death time (TDT), and z value. Kinetic parameters were significantly (p<0.05) influenced by variation temperature of PAMTI. In this study, the synergistic effect of pressure and temperature were found in the inactivation of E. coli ATCC 10536 through PAMTI.

• Journal of Microbiology and Biotechnology
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• v.17 no.4
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• pp.616-623
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• 2007

The effects of initial concentration and pulsed pressurization on the inactivation of Clostridium sporogenes spores suspended in deionized water were determined during thermal processing $(TP;\;105^{\circ}C,\;0.1MPa)$ and pressure-assisted thermal processing $(PATP;\;105^{\circ}C\;and\;700MPa)$ treatments for 40 min and 5min holding times, respectively. Different inoculum levels $(10^4,\;10^6\;and\;10^8CFU/ml)$ of C. sporogenes spores suspended in deionized water were treated at $105^{\circ}C$ under 700MPa with single, double, and triple pulses. Thermally treated samples served as control. No statistical significances (p>0.05) were observed among all different inoculum levels during the thermal treatment, whereas the inactivation rates $(k_1\;and\;k_2)$ were decreased with increasing the initial concentrations of C. sporogenes spores during the PATP treatments. Double- and triple-pulsed pressurization reduced more effectively the number of C. sporogenes spores than single-pulse pressurization. The study shows that the spore clumps formed during the PATP may lead to an increase in pressure-thermal resistance, and multiple-pulsed pressurization can be more effective in inactivating bacterial spores. The results provide an interesting insight on the spore inactivation mechanisms with regard to inoculum level and pulsed pressurization.

• 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 and Biotechnology
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• v.16 no.11
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• pp.1684-1689
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• 2006

Airborne microorganisms, which are currently termed bioaerosols, have received attention owing to the harmful effects they have on human health. As the concern over airborne microorganisms grows, there also grows an urgent need to study and develop efficient methods for controlling them. In this study, thermal energy using a thermal tube was tested as a control method, mainly against airborne E. coli. For a comparison, B. subtilis var. niger spores were utilized in the experimentation. It was found that the widely known inactivation conditions for microorganisms were not adequate against airborne microorganisms. The experimental results demonstrated the need for extensive studies that should investigate adequate and economic conditions to control against airborne bacteria. In this study, thermal energy exposed by the thermal tube demonstrated an inactivation performance for controlling E. coli bioaerosols.

• Archives of Pharmacal Research
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• v.5 no.2
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• pp.45-52
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• 1982

Staibilization effect of Panax ginseng C. A. Meyer on .betha.-D-Galactosidase inactivation was proved by kinetic studies of thermal inactivation of the enzyme. The water extract Panax ginseng C. A. Meyer showed stabilization activity at minimal concentration of 10ppm. The methanolic extract was purified to obtain ginseng saponins, and two groups of the ginsenosides, i. e. protopanaxadiol and protopanaxatriol were isolated. They also showed a protective effect against the thermal and chemical inactivation of the enzyme; p-chloromercuribenzoic acid and hydroxylamine known as protein modifier greatly inactivated the enzyme but inactivation was significantly balocked by the ginseng component MG$^{2+}$, known as a cofactor, stabilized the enzyme and the poor stabilization effect by it was potentiated by ginseng components.s.

• Journal of Microbiology and Biotechnology
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• v.25 no.1
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• pp.33-43
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• 2015

GAM-1 and GAM-2, two themostable glucoamylases from Aspergillus niger B-30, possess different molecular masses, glycosylation, and thermal stability. In the present study, the effects of additives on the thermal inactivation of GAM-1 and GAM-2 were investigated. The half-lives of GAM-1 and GAM-2 at 70℃ were 45 and 216 min, respectively. Data obtained from fluorescence spectroscopy, circular dichroism spectroscopy, UV absorption spectroscopy, and dynamic light scattering demonstrated that during the thermal inactivation progress, combined with the loss of the helical structure and a majority of the tertiary structure, tryptophan residues were partially exposed and further led to glucoamylases aggregating. The thermal stability of GAM-1 and GAM-2 was largely improved in the presence of sorbitol and trehalose. Results from spectroscopy and Native-PAGE confirmed that sorbitol and trehalose maintained the native state of glucoamylases and prevented their thermal aggregation. The loss of hydrophobic bonding and helical structure was responsible for the decrease of glucoamylase activity. Additionally, sorbitol and trehalose significantly increased the substrate affinity and catalytic efficiency of the two glucoamylases. Our results display an insight into the thermal inactivation of glucoamylases and provide an important base for industrial applications of the thermally stable glucoamylases.

• Microbiology and Biotechnology Letters
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• v.17 no.4
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• pp.365-369
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• 1989

Thermal inactivation of Tyichoderma viride cellobiohydrolase was investigated by immunoassay and residual enzyme assay such as carboxymethyl cellulase (CMCase) and filter paper degradation activity (FPase). Arrhenius plots of cellobiohydrolase were appeared as straight line. The Z-values of cellobiohydrolase calculated by CMCase, FPase and immunoassay were 5.2$^{\circ}C$, 6.4$^{\circ}C$ and 5.8$^{\circ}C$, respectively. The thermodynamic parameters obtained from FPase were better agreement with those of immunoassay than CMCase assay.

• Food Science of Animal Resources
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• v.18 no.3
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• pp.269-275
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• 1998

The purpose of this study was to determine the thermal inactivation of Salmonella enteritidis, Salmonella typhimurium and E. coli O111 in liquid cultures treated with microwave energy. Furthermore, this study was to introduce new methodologies for studying nonthermal microwave effects on microorganisms, using controlled microwave energy and specially designed apparatuses. For the automatic temperature control during microwave heating, the real time data acquisition and computation system is designed with BASIC routine. The automatic temperature control system used in the experiments perform relatively stable control at the experiment temperature of 45, 50, 55 60$^{\circ}C$ and 65$^{\circ}C$ for 30 minutes. The effects of microwave heating on liquid cultures was compared with that of conventional heating, still reduces effectively the number of pathogenic bacteria in liquid cultures. While no particular differences between microwave heating and conventional heating was observed in the activation of E. coli at 45$^{\circ}C$ test, the activation of Sal. enteritidis and Sal. typhimurium was slightly reduced during the microwave treatments.