Home About us Contact
|
Home About us Contact | ||
|
|
||
Thermal Inactivation (thermal + inactivation)
Terms modified by Thermal Inactivation Selected AbstractsThermal Inactivation of Salmonella on Cantaloupes Using Hot WaterJOURNAL OF FOOD SCIENCE, Issue 2 2006Ethan B. Solomon ABSTRACT The inactivation of Salmonella on cantaloupes using hot water was investigated. Whole melons, inoculated with a cocktail of Salmonella isolates, were subjected to thermal treatments of various lengths in water at 65 °C, 75 °C, and 85 °C. Treatment with water at 85 °C for 60 and 90 s resulted in reductions of up to 4.7 log colony forming units (CFU) per square centimeter of rind. However, the rind of melons treated at 85 °C for 90 s were noticeably softer than the rind of melons treated for 60 s. Thermal penetration profiles were measured and computer simulations were conducted to verify the effect of hot water treatment conditions on the internal temperatures of cantaloupe melons. Experimental and simulation data indicated that the internal temperature of melons treated with hot water did not increase rapidly compared with the rind temperature. Regardless of the process temperature used, the temperature of the edible flesh, 10 mm from the surface of the rind, remained at least 40 °C cooler than the surface temperature of cantaloupe melons. These results demonstrate the utility of hot water for the inactivation of Salmonella on cantaloupes and provide a framework to producers of fresh-cut melon for the potential use of hot water as an intervention treatment. [source] Comparative Study of Thermal Inactivation of Escherichia coli O157:H7, Salmonella, and Listeria monocytogenes in Ground PorkJOURNAL OF FOOD SCIENCE, Issue 4 2004R. Y. Murphy ABSTRACT: Thermal inactivation of Escherichia coli O157:H7, Salmonella, and Listeria monocytogenes in ground pork was compared. The D (decimal reduction time at a certain heating temperature) values of E. coli O157:H7, Salmonella, and L. monocytogenes at 55 to 70°C were 33.44 to 0.048 min, 45.87 to 0.083 min, and 47.17 to 0.085 min, respectively. The z (temperature rise for 1 log10 reduction of D) value of E. coli O157:H7, Salmonella, and L. monocytogenes in ground pork was 4.94°C, 5.89°C, and 5.92°C, respectively. Significant difference was found on the D and z values between E. coli O157:H7 and Salmonella or between E. coli O157:H7 and L. monocytogenes. The D and z values of Salmonella in ground pork were not significantly different from L. monocytogenes. [source] Thermal Inactivation of Salmonella Senftenberg and Listeria innocua in Beef/Turkey Blended Patties Cooked via Fryer and/or Air Convection OvenJOURNAL OF FOOD SCIENCE, Issue 5 2002R.Y. Murphy ABSTRACT: Beef/turkey blended patties, containing 107 to 108 cfu/g of Salmonella Senftenberg or Listeria innocua, were battered and breaded. The effect of frying (177 °C) and air convection cooking (288 °C) on thermal inactivation of S. Senftenberg and L. innocua was evaluated. A model was obtained to correlate product internal temperature with frying and oven cooking time. Cooking method significantly affected thermal history and subsequently the thermal inactivation of S. Senftenberg and L. innocua. The effect of frying time interacted with oven cooking time. Increasing frying time reduced the oven cooking time. Mathematical models were developed to correlate the survival rate of S. Senftenberg or L. innocua with frying and oven cooking time. [source] AN ESTEROLYTIC ACTIVITY FROM A WILD EDIBLE MUSHROOM, LYCOPERDON PERLATUMJOURNAL OF FOOD BIOCHEMISTRY, Issue 4 2009AHMET COLAK ABSTRACT Lycoperdon perlatum Pers. (Lycoperdaceae, Agaricales, Agaricomycetidae, Agaricomycetes, Basidiomycota, Fungi) was evaluated for its esterolytic potential. Native electrophoresis of the crude extracts showed four bands having Rf values of 0.34, 0.39, 0.52 and 0.59. The esterase showed the highest activity toward a short-chain substrate, p -nitrophenyl acetate. Optimum reaction conditions for L. perlatum crude extract were attained at pH 8.0 and 40C. Esterolytic activity of enzyme extract was stimulated in the presence of Mn2+, Fe2+, Ca2+ and Zn2+ in the reaction mixture. The enzyme activity was stimulated by incubation at pH 6.0 but retained 77% of its original activity at its optimum pH after 24 h. Thermal inactivation was displayed after incubation for 20 min at various temperatures above 30C. At 1 mM final concentration, 2-mercaptoethanol, dithiothreitol, ethylenediamine tetraacetic acid and p -methylphenyl sulfonylfluoride inhibited the esterolytic reaction. These results support that the crude L. perlatum extract possesses an esterolytic activity having properties similar to other esterases. PRACTICAL APPLICATIONS Esterases catalyzing the cleavage and formation of ester bonds are known ,/,-hydrolases (EC 3.1.1.X). Esterases are used for the synthesis of flavor esters for the food industry, modification of triglycerides for fat and oil industry and resolution of racemic mixtures used for the synthesis of fine chemicals for the pharmaceutical industry. Therefore, the search for new enzyme sources is important for the development of new enzymes and applications. [source] Heat-moisture Treatments of Cowpea Flour and Their Effects on Phytase InactivationJOURNAL OF FOOD SCIENCE, Issue 2 2005Nicole S. Affrifah ABSTRACT: Samples of finely ground cowpea flour with moisture content adjusted to 10%, 25%, 35% (dry basis) were heated in sealed retort pouches at 70 to 95°C for periods of 2 to 32 min. Phytase showed a high thermal resistance with residual activity ranging between 50% and 95%. Thermal inactivation of cowpea phytase was adequately described by a fractional conversion model based on a 1st-order rate equation. Overall, increasing temperature and initial moisture content resulted in increased enzyme inactivation. Estimated activation energies between 70 and 95°C were 33.3, 37.9, and 43.4 kJ/mol at 10%, 25%, and 35% moisture, respectively. The kinetic models generated were successfully used to predict phytase activity in cowpea flour. [source] Comparative Study of Thermal Inactivation of Escherichia coli O157:H7, Salmonella, and Listeria monocytogenes in Ground PorkJOURNAL OF FOOD SCIENCE, Issue 4 2004R. Y. Murphy ABSTRACT: Thermal inactivation of Escherichia coli O157:H7, Salmonella, and Listeria monocytogenes in ground pork was compared. The D (decimal reduction time at a certain heating temperature) values of E. coli O157:H7, Salmonella, and L. monocytogenes at 55 to 70°C were 33.44 to 0.048 min, 45.87 to 0.083 min, and 47.17 to 0.085 min, respectively. The z (temperature rise for 1 log10 reduction of D) value of E. coli O157:H7, Salmonella, and L. monocytogenes in ground pork was 4.94°C, 5.89°C, and 5.92°C, respectively. Significant difference was found on the D and z values between E. coli O157:H7 and Salmonella or between E. coli O157:H7 and L. monocytogenes. The D and z values of Salmonella in ground pork were not significantly different from L. monocytogenes. [source] Thermal Inactivation Kinetics of Salmonella and Listeria in Ground Chicken Breast Meat and Liquid MediumJOURNAL OF FOOD SCIENCE, Issue 4 2000R.Y. Murphy ABSTRACT: Thermal inactivation of Listeria innocua and 6 Salmonella serotypes in ground chicken breast meat was compared to that in peptone (0.1%) - agar (0.1%) solution. Inoculated samples were packed in a thin-wall metal tube and submerged in a water bath at temperatures ranging from 55.0 to 70.0 °C. For Salmonella and Listeria, the D values in ground chicken breast meat at 55 to 70 °C were higher (p < 0.0001) than those in peptone-agar solution; however, the z values were not significantly different. Complete first-order inactivation models, with Arrhenius temperature dependency, were developed for each inoculum and medium. [source] Increasing the thermal stability of euphauseraseFEBS JOURNAL, Issue 1 2001A cold-active, multifunctional serine protease from Antarctic krill A molecular model of Antarctic krill euphauserase based on the known crystal structure of its fiddler crab analog, collagenase I, indicates that the core structure of these enzymes is almost identical. Euphauserase is a cold-active and thermally sensitive enzyme with a high affinity for Lys, Arg and large hydrophobic amino acids. Residue Phe137 in euphauserase, localized in loop D (autolysis loop), is highly exposed on the surface of the molecule. Therefore, it appeared to be an easy target for autolysis. The broadly specific euphauserase has a low affinity for negatively charged residues. In order to increase the stability of the enzyme, two mutants were created in which residue Phe137 was replaced by a Glu and an Asp residue. Both mutations resulted in increased stability of the recombinant euphauserase towards thermal inactivation. [source] Expression and regulation of alkaline phosphatases in human breast cancer MCF-7 cellsFEBS JOURNAL, Issue 5 2000Lai-Chen Tsai The effect of retinoic acid and dexamethasone on alkaline phosphatase (AP) expression was investigated in human breast cancer MCF-7 cells. Cellular AP activity was induced significantly by retinoic acid or dexamethasone in a time-dependent and dose-dependent fashion. A marked synergistic induction of AP activity was observed when the cells were incubated with both agents simultaneously. Two AP isozymes, tissue-nonspecific (TNAP) and intestinal (IAP), were shown to be expressed in MCF-7 cells as confirmed by the differential rate of thermal inactivation of these isozymes and RT-PCR. Based on the two-isozyme thermal-inactivation model, the specific activities for TNAP and IAP in each sample were analyzed. TNAP activity was induced only by retinoic acid and IAP activity was induced only by dexamethasone. Whereas dexamethasone conferred no significant effect on TNAP activity, retinoic acid was shown to inhibit IAP activity by , 50%. Interestingly, TNAP was found to be the only isozyme activity superinduced when the cells were costimulated with retinoic acid and dexamethasone. Northern blot and RT-PCR analysis were then used to demonstrate that the steady-state TNAP mRNA level was also superinduced, which indicates that the superinduction is regulated at the transcriptional or post-transcriptional levels. In the presence of the glucocorticoid receptor antagonist RU486, the dexamethasone-mediated induction of IAP activity was blocked completely as expected. However, the ability of RU486 to antagonize the action of glucocorticoid was greatly compromised in dexamethasone-mediated superinduction of TNAP activity. Furthermore, in the presence of retinoic acid, RU486 behaved as an agonist, and conferred superinduction of TNAP gene expression in the same way as dexamethasone. Taken together, these observations suggest that the induction of IAP activity by dexamethasone and the superinduction of TNAP by dexamethasone were mediated through distinct regulatory pathways. In addition, retinoic acid plays an essential role in the superinduction of TNAP gene expression by enabling dexamethasone to exert its agonist activity, which otherwise has no effect. [source] Production, purification and thermal characterisation of invertase from a newly isolated Fusarium sp. under solid-state fermentationINTERNATIONAL JOURNAL OF FOOD SCIENCE & TECHNOLOGY, Issue 7 2008Iram Shaheen Summary Production of invertase employing a newly isolated Fusarium sp. under solid-state fermentation was optimised. Different process parameters were optimised. The maximum enzyme activity under optimum conditions was 47.23 ± 2.12 U gds,1 with nitrogen additives. The enzyme was purified by ammonium sulphate precipitation, diethylaminoethyl cellulose ion-exchange chromatography and Sephadex gel filtration. This protocol gave 20.25-fold purification and 5.53% recovery. The optimum pH and temperature for activity were 5.0 and 50 °C. The Km and Vmax values for the enzyme were 8.33 mm and 21.48 ,mol min,1, respectively. A detailed kinetic study of thermal inactivation has been carried out. Enthalpy of activation (,H*) decreased when entropy (,S*) of activation increased at higher temperatures. Moreover, free energy of denaturation (,G*) increased at higher temperature making the enzyme thermally stable. A possible explanation for the thermal inactivation of invertase at higher temperatures is also discussed. [source] Esterification of n -butyric acid with n -butyl alcohol and transesterification of (R,,S)-phenylethanol by lipase immobilized on cellulose acetate,TiO2 gel fibreJOURNAL OF CHEMICAL TECHNOLOGY & BIOTECHNOLOGY, Issue 1 2002Yuko Ikeda Abstract Lipase (EC 3.1.1.3) was immobilized on cellulose acetate,TiO2 gel fibre by the sol,gel method. The immobilized lipases were used for esterification of n -butyric acid with n -butyl alcohol and enantioselective acylation of (R, S)-phenylethanol using vinyl acetate as an acyl donor. Compared with native lipase, the activity of the immobilized lipase was stable and relatively unaffected by the water content of the solvent and the substrate concentration. The data indicate that the lipases are immobilized on the fibre surface and that enzyme activity is influenced by bound water. However, the thermal reactivity and enantioselectivity of the immobilized lipase were less than those of native lipase. This may not reflect thermal inactivation of the enzyme but rather significant thermal contraction of the gel fibre by cellulose crystallization, resulting in liberation of bound water and a decrease in the amount of enzyme which is available for the reaction. Copyright © 2001 Society of Chemical Industry [source] THE EFFECT OF REFRIGERATED STORAGE ON SENSORY PROFILE AND PHYSICAL-CHEMICAL CHARACTERISTICS OF MINIMALLY PASTEURIZED ORANGE JUICEJOURNAL OF FOOD PROCESSING AND PRESERVATION, Issue 2009TATIANA BEATRIS TRIBESS ABSTRACT Minimal pasteurization of orange juice (OJ) consists of using minimum holding time and temperature to ensure partial inactivation of pectin methylesterase (PME). This process produces juice with preserved sensory attributes and has a better acceptance by consumers when compared with commercially pasteurized OJ. Sensory profile and physical-chemical characteristics of minimally processed OJ was determined, during refrigerated storage, for two OJ blends with different pH values and the same level of PME thermal inactivation. A selected and trained sensorial panel (n = 16) performed sensory analysis, based on a quantitative descriptive analysis, twice a week for 30 days, evaluating the attributes of appearance (suspended particles and color intensity), odor (natural orange and fermented orange) and flavor (orange characteristic, fermented orange, acid and bitter taste). Storage presented great effect on OJ sensory profile; however, it was not noticeable on physical-chemical characteristics. PRACTICAL APPLICATIONS Minimal pasteurization of orange juice (OJ) consists of using minimum holding time and temperature to ensure partial inactivation of pectin methylesterase. This process produces juice with longer shelf life than fresh squeezed orange juice, preserved sensory attributes and better acceptance by consumers when compared with commercially pasteurized OJ. This study can contribute for quality evaluation of minimally pasteurized OJ under refrigeration. [source] THERMAL INACTIVATION KINETICS OF ALKALINE PHOSPHATASE IN BUFFER AND MILKJOURNAL OF FOOD PROCESSING AND PRESERVATION, Issue 3 2006S. FADILO ABSTRACT A detailed kinetic study on the thermal inactivation of alkaline phosphatase (ALP) added into buffer and pasteurized milk and for ALP naturally present in raw cow's milk has been performed. Kinetic parameters (rate constant, k; decimal reduction time, D; activation energy, Ea; and z value) were evaluated based on the first-order rate model at 50,80C. The temperature sensitivity of the kinetic parameters was evaluated considering the Arrhenius-type Ea model. All kinetic behaviors were well described by the first-order model (r2 > 0.91). The D values increased with increasing temperature. Higher temperatures resulted in higher rates of enzyme inactivation as indicated by lower D values and higher k values. There are significant differences (P < 0.01) among the D values for ALP in buffer and milk at treated temperatures. The rate of enzyme inactivation was much more rapid in buffer than in pasteurized milk. The evaluated Ea values for ALP added into the buffer and pasteurized milk, and for ALP naturally present in raw milk were 97.2, 149.9 and 207.8 kJ/mol, respectively. The inactivation kinetics of ALP during heat treatment was found to be dependent on the composition of the medium, and the time and temperature of the heat treatment. [source] A PREDICTIVE MODEL FOR HIGH-PRESSURE CARBON DIOXIDE INACTIVATION OF MICROORGANISMSJOURNAL OF FOOD SAFETY, Issue 2 2009S. BUZRUL ABSTRACT The Weibull model, which is commonly used for thermal inactivation of microorganisms in literature, was used to describe microbial inactivation by high-pressure carbon dioxide (HPCD). The number of parameters of the model was reduced from two to one in order to avoid interrelationship of these parameters with a slight loss of goodness-of-fit. A second-order polynomial function fulfilling a number of constraints was proposed for the secondary modeling of the time-constant parameter of the reduced Weibull model. This function consists of both pressure and temperature and therefore can be used for HPCD treatments. PRACTICAL APPLICATIONS The application of any new technology in food preservation requires a reliable model that accurately describes and predicts the inactivation data of microorganisms. In principle, the methodology presented here could be used to describe and predict the survival data for high-pressure carbon dioxide inactivation of microorganisms at least for some pressure and temperature ranges if the isobaric/isothermal survival curves of these microorganisms are linear, concave upward or downward. [source] Inactivation of Escherichia coli K-12 in Apple Juice Using Combination of High-Pressure Homogenization and ChitosanJOURNAL OF FOOD SCIENCE, Issue 1 2009S. Kumar ABSTRACT:, Apple juice and apple cider were inoculated with Escherichia coli K-12 and processed using a high-pressure homogenizer to study bacterial inactivation. Seven levels of pressure ranging from 50 to 350 MPa were used in the high-pressure homogenizer. Two types of chitosan (regular and water soluble) with 2 levels of concentration 0.01% and 0.1% were investigated for synergistic effect with high-pressure homogenization for the bacterial inactivation. E. coli K-12 inactivation was evaluated as a function of homogenizing pressure at different concentration of 2 types of chitosan in apple juice and cider. High-pressure homogenization (HPH) induced significant inactivation in the range of 100 to 200 MPa, while thermal inactivation was the primary factor for the bacterial inactivation above 250 MPa. Significant (P < 0.05) 2-way interactions involving pressure and type of substrate or pressure and chitosan concentration were observed during the study. The homogenization pressure and the incremental quantity of chitosan (both types) acted synergistically with the pressure to give higher inactivation. Significantly (P < 0.05) higher inactivation was observed in apple juice than apple cider at same homogenizing pressure. No effect of type of chitosan was observed on the bacterial inactivation. [source] Detergent and Sanitizer Stresses Decrease the Thermal Resistance of Enterobacter sakazakii in Infant Milk FormulaJOURNAL OF FOOD SCIENCE, Issue 3 2008T.M. Osaili ABSTRACT:, This study determined the effect of acid, alkaline, chlorine, and ethanol stresses on the thermal inactivation of Enterobacter sakazakii in infant milk formula. Unstressed or stressed cells were mixed with reconstituted powdered infant milk formula (PIMF) at temperatures between 52 and 58 °C for various time periods or mixed with PIMF prior to reconstitution with hot water between 50 and 100 °C. D - and z -values were determined using liner regression analysis. In general, detergent and sanitizer stresses decreased the thermal resistance of E. sakazakii in infant milk formula. The results of this study may be of use to regulatory agencies, manufacturers, and infant caregivers to design heating processes to eliminate E. sakazakii. [source] Thermal Inactivation of Salmonella Senftenberg and Listeria innocua in Beef/Turkey Blended Patties Cooked via Fryer and/or Air Convection OvenJOURNAL OF FOOD SCIENCE, Issue 5 2002R.Y. Murphy ABSTRACT: Beef/turkey blended patties, containing 107 to 108 cfu/g of Salmonella Senftenberg or Listeria innocua, were battered and breaded. The effect of frying (177 °C) and air convection cooking (288 °C) on thermal inactivation of S. Senftenberg and L. innocua was evaluated. A model was obtained to correlate product internal temperature with frying and oven cooking time. Cooking method significantly affected thermal history and subsequently the thermal inactivation of S. Senftenberg and L. innocua. The effect of frying time interacted with oven cooking time. Increasing frying time reduced the oven cooking time. Mathematical models were developed to correlate the survival rate of S. Senftenberg or L. innocua with frying and oven cooking time. [source] Technical Approach to Simplify the Purification Method and Characterization of Microbial Transglutaminase Produced from Streptoverticillium ladakanumJOURNAL OF FOOD SCIENCE, Issue 1 2000M.-L. Ho ABSTRACT: In order to fast and economically purify MTGase from Streptoverticillium ladakanum, a stepwise elution method was developed and compared with linear gradient elution method. MTGase was purified to electrophoretical homogeneity by using CM Sepharose CL-6B and Blue Sepharose Fast Flow chromatographies by linear gradient or stepwise methods. The recovery of MTGase by linear gradient and stepwise methods were 68.4% and 81.0%, respectively. The optimal temperature and pH were 40 °C and 5.5, respectively. It was stable at pH 5.0 to 7.0 and had a rate constant (KD) of 6.21 °o 10 -5 min -1 for thermal inactivation at 45 °C. The purified MTGase was activated by K+ Na+, Ca2+, Mn2+, and Mg2+, not affected by Fe3+, EDTA, but inhibited by Cu2+, Zn2+, Hg2+, Ni2+, Co2+, Cd2+, PCMB, NEM, IAA, and PMSF. A simple stepwise method was developed for the purification of MTGase from S. ladakanum. [source] Combined Pressure,temperature Inactivation of Alkaline Phosphatase in Bovine Milk: A Kinetic StudyJOURNAL OF FOOD SCIENCE, Issue 1 2000L. Ludikhuyze ABSTRACT: A detailed kinetic study on pressure-temperature inactivation of alkaline phosphatase has been performed in the pressure range 0.1 to 725 MPa at temperatures between 25 and 63 °C. Inactivation could be accurately described by a first order kinetic model, allowing D-values to be calculated. According to the thermal death time terminology, zr - and zp -values were calculated, expressing temperature and pressure dependence respectively. However, at high temperature, pressure dependence could not be calculated unambiguously. D-values firstly increased with increasing pressure up to 300 MPa and then decreased with further pressure increase, showing thermal inactivation to be counteracted by low pressure. Finally, a global model describing the D-value as a function of pressure and temperature has been formulated. [source] | ||||||||||