The differentiation of curd made from heated and raw milk

1973 ◽  
Vol 40 (1) ◽  
pp. 1-6 ◽  
Author(s):  
K. C. Guha ◽  
B. R. Roy
Keyword(s):  
Heat Treatment ◽  
Activation Energy ◽  
Microbial Growth ◽  
Whey Proteins ◽  
Raw Milk ◽  
First Order ◽  
Heat Treated ◽  
Native Whey ◽  
Indian Law ◽  
Kinetics Of

SummarySince Indian law requires curds to be made from heat-treated milk, a means for distinguishing between curds made from raw and from heat-treated milks was sought. Curds contain whey proteins that are partly or completely denatured by heat treatment; the kinetics of the reaction are first order. The concentrations of native whey proteins in raw and heat-treated milks and in curds made from those milks were measured. No difference was found between the concentrations in heattreated milk and in the curds made from it, so that identical values were obtained for the half-life on heating and for the activation energy of denaturation. The acidity and microbial growth occurring during the production of curd did not affect the whey proteins. On electrophoresis, curd from raw milk gave a few whey protein bands, but curd from milk boiled for 10 min gave none, showing complete denaturation of the whey proteins.

Effects of heat treatment and acidification on the dissociation of bovine casein micelles

1996 ◽  
Vol 63 (1) ◽  
pp. 35-48 ◽  
Author(s):  
Andrew J. R. Law
Keyword(s):  
Heat Treatment ◽  
Whey Proteins ◽  
Raw Milk ◽  
Serum Concentrations ◽  
Casein Micelles ◽  
Heat Treated ◽  
Decreasing Ph ◽  
The Individual ◽  
Almost All

SummaryThe effects of heat treatment and subsequent acidification of milk on the distribution of proteins, Ca and Pi, between the serum and micellar phases were examined using ultracentrifugation. After heating milk at 85 °C for 10 min, and storing for 22 h at 4, 20 or 30 °C, there was a marked increase in the concentration of κ-casein in the serum. At 4 and 20 °C there was also slightly more β-casein in the serum from heat-treated milk than in that from the corresponding raw milk. The whey proteins were extensively denatured, and were almost equally distributed between the supernatants and micellar pellets. After storage for 22 h the distribution of Ca and Pi between soluble and colloidal phases in heat-treated milk was similar to that in raw milk. After acidifying heat-treated milk by the addition of glucono-δ-lactone and storing for 22 h at 4, 20 or 30 °C there was progressive solubilization of colloidal calcium phosphate with decreasing pH, and at pH 5·0 almost all of the Ca and Pi was present in the serum. At 20 °C, and even more so at 4 °C, serum concentrations of the individual caseins increased considerably with decreasing pH, reaching maximum levels of about 25 and 40% of the total casein at pH 5·7 and 5·5 respectively, and then decreasing rapidly at lower pH. Compared with raw milk, maximum dissociation in heat-treated milks stored at 4 and 20 °C occurred at higher pH, and the overall levels of dissociation of individual caseins from the micelles were lower. At 30 °C, the concentrations of individual caseins in the serum of heat-treated milk decreased steadily as the pH was reduced, and did not show the slight increase found previously for raw milk. The role of the denatured whey proteins in interacting with κ-casein and in promoting aggregation of the micelles on acidification is discussed.

Vulcanization of Elastomers. 23. The Chemical Kinetics of Vulcanization Reactions and The Physical Properties of The Vulcanizates. I

1960 ◽  
Vol 33 (2) ◽  
pp. 335-341
Author(s):  
Walter Scheele ◽  
Karl-Heinz Hillmer
Keyword(s):  
Activation Energy ◽  
Physical Properties ◽  
Chemical Kinetics ◽  
Kcal Mole ◽  
First Order ◽  
Equilibrium Swelling ◽  
Kinetics Of ◽  
Kinetics Of Vulcanization ◽  
Limiting Value ◽  
Good Agreement

Abstract As a complement to earlier investigations, and in order to examine more closely the connection between the chemical kinetics and the changes with vulcanization time of the physical properties in the case of vulcanization reactions, we used thiuram vulcanizations as an example, and concerned ourselves with the dependence of stress values (moduli) at different degrees of elongation and different vulcanization temperatures. We found: 1. Stress values attain a limiting value, dependent on the degree of elongation, but independent of the vulcanization temperature at constant elongation. 2. The rise in stress values with the vulcanization time is characterized by an initial delay, which, however, is practically nonexistent at higher temperatures. 3. The kinetics of the increase in stress values with vulcanization time are both qualitatively and quantitatively in accord with the dependence of the reciprocal equilibrium swelling on the vulcanization time; both processes, after a retardation, go according to the first order law and at the same rate. 4. From the temperature dependence of the rate constants of reciprocal equilibrium swelling, as well as of the increase in stress, an activation energy of 22 kcal/mole can be calculated, in good agreement with the activation energy of dithiocarbamate formation in thiuram vulcanizations.

Magnetic Properties, Nanostructure, and Ordering Kinetics of Nb Additive FePtCu Films

2010 ◽  
Vol 638-642 ◽  
pp. 1743-1748
Author(s):  
G.J. Chen ◽  
Y.H. Shih ◽  
Jason S.C. Jang ◽  
S.R. Jian ◽  
P.H. Tsai ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Activation Energy ◽  
Magnetic Properties ◽  
Heating Rates ◽  
Fept Alloy ◽  
Ordering Kinetics ◽  
Nb Content ◽  
Kinetics Of ◽  
Nb Addition ◽  
Microstructure And Magnetic Properties

In this study,the (FePt)94-xCu6Nbx (x=0, 2.87, 4.52, 5.67) alloy films were prepared by co-sputtering. The effects of Nb addition content and heat treatment on the microstructure and magnetic properties of the polycrystalline FePtCu films are reported. Our previous experiments showed that the ordering temperature of the (FePt)94Cu6 films reduced to 320 °C, which is much lower than that of the FePt alloy. However, the grain growth after heat treatment limited the practical application in recording media. By adding the Nb content in the (FePt)94Cu6 film, the grain sizes of the films can be adjusted from 50 to 18nm, even for the films annealed at temperature as high as 600°C. DSC traces of as-deposited disorder films at different heating rates, to evaluate the crystallization of the order phase, revealed that the addition of Nb enhanced the activation energy of ordering from 87 kJ/mol to 288 kJ/mol for the (FePt)94-xCu6Nbx (x=0 and 2.87, respectively) films. The reduction of the grain size and the corresponding increase in the activation energy of the Fe-Pt-Cu-Nb films might result from the precipitation of the Nb atoms around the ordering FePt phase. The (FePt)94-xCu6Nbx (x=2.87) film showed a coercive force of 13.4 kOe and the magnetization of 687 emu/cc.

scholarly journals Improvement of recovered activity and stability of the Aspergillus oryzae β-galactosidase immobilized on duolite A568 by combination of immobilization methods

2017 ◽  
Vol 23 (4) ◽  
pp. 495-506 ◽  
Author(s):  
Larissa Falleiros ◽  
Bruna Cabral ◽  
Janaína Fischer ◽  
Carla Guidini ◽  
Vicelma Cardoso ◽  
...  
Keyword(s):  
Activation Energy ◽  
Aspergillus Oryzae ◽  
Physical Adsorption ◽  
Cross Linking ◽  
Thermal Deactivation ◽  
Order Model ◽  
First Order ◽  
Immobilized Biocatalyst ◽  
The Stability ◽  
Kinetics Of

The immobilization and stabilization of Aspergillus oryzae ?-galactosidase on Duolite??A568 was achieved using a combination of physical adsorption, incubation step in buffer at pH 9.0 and cross-linking with glutaraldehyde and in this sequence promoted a 44% increase in enzymatic activity as compared with the biocatalyst obtained after a two-step immobilization process (adsorption and cross-linking). The stability of the biocatalyst obtained by three-step immobilization process (adsorption, incubation in buffer at pH 9.0 and cross-linking) was higher than that obtained by two-steps (adsorption and cross-linking) and for free enzyme in relation to pH, storage and reusability. The immobilized biocatalyst was characterized with respect to thermal stability in the range 55-65 ?C. The kinetics of thermal deactivation was well described by the first-order model, which resulted in the immobilized biocatalyst activation energy of thermal deactivation of 71.03 kcal/mol and 5.48 h half-life at 55.0 ?C.

scholarly journals Germination, Outgrowth, and Vegetative-Growth Kinetics of Dry-Heat-Treated Individual Spores ofBacillusSpecies

2018 ◽  
Vol 84 (7) ◽  
Author(s):  
Lin He ◽  
Zhan Chen ◽  
Shiwei Wang ◽  
Muying Wu ◽  
Peter Setlow ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Spore Germination ◽  
Differential Interference Contrast Microscopy ◽  
Content Type ◽  
Dry Heat ◽  
Heat Treated ◽  
Contrast Microscopy ◽  
Interference Contrast Microscopy ◽  
Dry Heat Treatment ◽  
Kinetics Of

ABSTRACTDNA damage kills dry-heated spores ofBacillus subtilis, but dry-heat-treatment effects on spore germination and outgrowth have not been studied. This is important, since if dry-heat-killed spores germinate and undergo outgrowth, toxic proteins could be synthesized. Here, Raman spectroscopy and differential interference contrast microscopy were used to study germination and outgrowth of individual dry-heat-treatedB. subtilisandBacillus megateriumspores. The major findings in this work were as follows: (i) spores dry-heat-treated at 140°C for 20 min lost nearly all viability but retained their Ca2+-dipicolinic acid (CaDPA) depot; (ii) in most cases, dry-heat treatment increased the average times and variability of all major germination events inB. subtilisspore germination with nutrient germinants or CaDPA, and in one nutrient germination event withB. megateriumspores; (iii)B. subtilisspore germination with dodecylamine, which activates the spore CaDPA release channel, was unaffected by dry-heat treatment; (iv) these results indicate that dry-heat treatment likely damages spore proteins important in nutrient germinant recognition and cortex peptidoglycan hydrolysis, but not CaDPA release itself; and (v) analysis of single spores incubated on nutrient-rich agar showed that while dry-heat-treated spores that are dead can complete germination, they cannot proceed into outgrowth and thus not to vegetative growth. The results of this study provide new information on the effects of dry heat on bacterial spores and indicate that dry-heat sterilization regimens should produce spores that cannot outgrow and thus cannot synthesize potentially dangerous proteins.IMPORTANCEMuch research has shown that high-temperature dry heat is a promising means for the inactivation of spores on medical devices and spacecraft decontamination. Dry heat is known to killBacillus subtilisspores by DNA damage. However, knowledge about the effects of dry-heat treatment on spore germination and outgrowth is limited, especially at the single spore level. In the current work, Raman spectroscopy and differential interference contrast microscopy were used to analyze CaDPA levels in and kinetics of nutrient- and non-nutrient germination of multiple individual dry-heat-treatedB. subtilisandBacillus megateriumspores that were largely dead. The outgrowth and subsequent cell division of these germinated but dead dry-heat-treated spores were also examined. The knowledge obtained in this study will help understand the effects of dry heat on spores both on Earth and in space, and indicates that dry heat can be safely used for sterilization purposes.

Subpasteurization Heat Treatment to Inactivate Lipase and Control Bacterial Growth in Raw Milk

1982 ◽  
Vol 45 (6) ◽  
pp. 513-515 ◽  
Author(s):  
G. F. SENYK ◽  
R. R. ZALL ◽  
W. F. SHIPE
Keyword(s):  
Heat Treatment ◽  
Lipase Activity ◽  
Raw Milk ◽  
Heat Treatments ◽  
Plate Count ◽  
Psychrotrophic Bacteria ◽  
Standard Plate Count ◽  
Heat Treated ◽  
Standard Plate ◽  
And Control

Raw milk was heat-treated under subpasteurization and suprapasteurization conditions, cooled and stored for up to 72 h at 4.4 and 6.7°C. Milk lipase activity and bacteria counts were monitored in both unheated and heated milks. Inhibition of milk lipase activity ranged from 42 to 98% for treatments of 57.2°C for 10 sec to 73.9°C for 10 sec, respectively. The logs of Standard Plate Count after 72 h of storage at 6.7°C were 6.56, 4.86, 4.31, 4.00 and 2.82 for unheated and 10-sec heat treatments at 57.2, 65.6, 73.9 and 82.2°C, respectively. Psychrotrophic Bacteria Counts were also lower in the heated milks than in the unheated milk. The logs of Psychrotrophic Bacteria Counts after 72 h of storage at 6.7°C were 6.21, 2.45, 2.27, 1.33 and 1.00 for unheated and 10-sec heat treatments at 57.2, 65.6, 73.9 and 82.2°C, respectively. Heat treatment of raw milk supplies would result in limiting action of the milk lipase system and growth of bacteria.

Kinetics and Activation Parameters for the Alkaline Aqueous Rearrangement of Trichorfon [O,O-Dimethyl-(2,2,2-Trichloro-1-Hydroxyethyl) Phosphonate] to Dichlorvos [O,O-Dimethyl-O-(2,2-Dichloroethenyl)Phosphate]

2001 ◽  
Vol 36 (3) ◽  
pp. 589-604 ◽  
Author(s):  
Julian M. Dust ◽  
Christopher S. Warren
Keyword(s):  
Activation Energy ◽  
High Pressure ◽  
Activation Parameters ◽  
Base Catalysis ◽  
Rearrangement Product ◽  
Exponential Factor ◽  
First Order ◽  
Pseudo First Order ◽  
Order Plot ◽  
Kinetics Of

Abstract The kinetics of the alkaline rearrangement of O,O-dimethyl-(2,2,2-trichloro-1- hydroxyethyl)phosphonate, (trichlorfon, 1), the active insecticidal component in such formulations as Dylox, was followed at 25±0.5°C by high pressure liquid chromatography (UV-vis detector, 210 nm). The rearrangement product, O,Odimethyl- O-(2,2-dichloroethenyl)phosphate (dichlorovos, 2), which is a more potent biocide than trichlorfon, undergoes further reaction, and the kinetics, consequently, cannot be treated by a standard pseudo-first-order plot. A two-point van't Hoff (initial rates) method was used to obtain pseudo-first-order rate constants (kѱ) at 25, 35 and 45°C: 2.6 × 10-6, 7.4 × 10-6 and 2.5 × 10-5 s-1, respectively. Arrhenius treatment of this data gave an activation energy (Ea) of 88 kJ·mol-1 with a pre-exponential factor (A) of 5.5 × 109 s-1. Kinetic trials at pH 8.0 using phosphate and tris buffer systems show no buffer catalysis in this reaction and indicate that the rearrangement is subject to specific base catalysis. Estimates are reported for pseudo-first-order half-lives for trichlorfon at pH 8.0 for environmental conditions in aqueous systems in the Corner Brook region of western Newfoundland, part of the site of a recent trichlorfon aerial spray program.

THE KINETICS OF CUPRENE GROWTH

1950 ◽  
Vol 28b (7) ◽  
pp. 358-372
Author(s):  
Cyrias Ouellet ◽  
Adrien E. Léger
Keyword(s):  
Nitric Oxide ◽  
Activation Energy ◽  
Carbon Monoxide ◽  
Apparent Activation Energy ◽  
Copper Catalyst ◽  
Maximum Velocity ◽  
Static System ◽  
Reaction Velocity ◽  
First Order ◽  
Kinetics Of

The kinetics of the polymerization of acetylene to cuprene on a copper catalyst between 200° and 300 °C. have been studied manometrically in a static system. The maximum velocity of the autocatalytic reaction shows a first-order dependence upon acetylene pressure. The reaction is retarded in the presence of small amounts of oxygen but accelerated by preoxidation of the catalyst. The apparent activation energy, of about 10 kcal. per mole for cuprene growth between 210° and 280 °C., changes to about 40 kcal. per mole above 280 °C. at which temperature a second reaction seems to set in. Hydrogen, carbon monoxide, or nitric oxide has no effect on the reaction velocity. Series of five successive seedings have been obtained with cuprene originally grown on cuprite, and show an effect of aging of the cuprene.

CHANGES IN MILK, WHEY, AND BLUE CHEESE AS INDUCED BY BENZOYL PEROXIDE1,2

1974 ◽  
Vol 37 (5) ◽  
pp. 244-249 ◽  
Author(s):  
C. J. Washam ◽  
G. W. Reinbold ◽  
E. R. Vedamuthu ◽  
R. Jorgensen
Keyword(s):  
Heat Treatment ◽  
Benzoyl Peroxide ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Whey Proteins ◽  
Milk Proteins ◽  
Bleaching Process ◽  
Blue Cheese ◽  
Milk Whey ◽  
Heat Treated

Milk proteins were subjected to treatment with various levels of benzoyl peroxide, with and without heating at 60 C for 2 h. Heating had a pronounced effect on whey proteins, but polyacrylamide gel electrophoresis revealed changes in proteins not attributable to heat alone. The effect on proteins was reflected in an increased tendency for the benzoyl peroxide-heat treated cheeses to expel moisture during leakage tests. Use of 17.8 ppm benzoyl peroxide resulted in a markedly whiter cheese than that made using 5.9 ppm and reflectance studies indicated this to be true even when no heat treatment accompanied the benzoyl peroxide. Use of benzoyl peroxide in the bleaching process did not decrease mold development in ripening loaves nor was acid production by lactic cultures diminished. In addition, proteolysis of milk proteins by rennet was not reduced by the presence of benzoyl peroxide.

Determination of Thermal Inactivation Kinetics of Microorganisms with a Continuous Microflow Apparatus

2004 ◽  
Vol 67 (11) ◽  
pp. 2560-2564 ◽  
Author(s):  
C. R. LOSS ◽  
J. H. HOTCHKISS
Keyword(s):  
Thermal Inactivation ◽  
Capillary Tube ◽  
Raw Milk ◽  
Heating Time ◽  
Inactivation Kinetics ◽  
Weibull Function ◽  
Stainless Steel Capillary ◽  
Heat Treated ◽  
Native Microflora ◽  
Kinetics Of

Use of a continuous microflow submerged microcoil (CSMC) apparatus was compared with the capillary tube (CT) method for measuring the thermal inactivation kinetics of Pseudomonas fluorescens at 61°C for 3 to 29 s. Inocula were continuously pumped through a microbore (≤0.0762 cm inside diameter) thin-walled stainless steel capillary tube submerged in a heated oil bath. The heating time was set by changing the flow rate, tube dimensions, or both. With the use of microthermo-couples, the time for the inocula to reach within 1°C of the set temperature was <3 s, and shorter than that with capillary tubes or vials. Inactivation curves (61°C) for P. fluorescens prepared by the CSMC method were not different from curves prepared by the CT method, as determined by analysis of variance (P > 0.05). Inactivation of Bacillus cereus spores (105°C) and native microflora found in raw milk (72°C) over heating times of 3 to 42 s were determined by CSMC. CSMC can measure thermal inactivation kinetics of microorganisms efficiently and simply at high temperatures and in short times. Survivors can be enumerated in 1-ml volumes of heat-treated samples, making it useful for determining inactivation kinetics of low numbers of microorganisms, such as those found in high-quality raw milk. Inactivation kinetics were generally more accurately described by the Weibull function (R2 ≥ 0.97) than the linear kinetic model.

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