Thermal transitions of king fish whole muscle, fat and fat-free muscle by differential scanning calorimetry

2007 ◽  
Vol 462 (1-2) ◽  
pp. 56-63 ◽  
Author(s):  
S.S. Sablani ◽  
M.S. Rahman ◽  
S. Al-Busaidi ◽  
N. Guizani ◽  
N. Al-Habsi ◽  
...  
Keyword(s):  
Differential Scanning Calorimetry ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Whole Muscle

Comparison of the Thermal Transitions of Spray-Dried and Freeze-Dried Egg Whites by Differential Scanning Calorimetry

2020 ◽  
Vol 13 (8) ◽  
pp. 1329-1343
Author(s):  
Jin-Hong Zhao ◽  
Li-Sha Liu ◽  
Shyam S. Sablani ◽  
Yi-Jiao Peng ◽  
Hong-Wei Xiao ◽  
...  
Keyword(s):  
Differential Scanning Calorimetry ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Freeze Dried ◽  
Spray Dried

Thermotoga neapolitana Homotetrameric Xylose Isomerase Is Expressed as a Catalytically Active and Thermostable Dimer in Escherichia coli

1998 ◽  
Vol 64 (7) ◽  
pp. 2357-2360 ◽  
Author(s):  
J. Michael Hess ◽  
Vladimir Tchernajenko ◽  
Claire Vieille ◽  
J. Gregory Zeikus ◽  
Robert M. Kelly
Keyword(s):  
Escherichia Coli ◽  
Differential Scanning Calorimetry ◽  
Gel Filtration ◽  
Xylose Isomerase ◽  
Thermotoga Neapolitana ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Catalytically Active ◽  
The Stability ◽  
Tetrameric Form

ABSTRACT The xylA gene from Thermotoga neapolitana5068 was expressed in Escherichia coli. Gel filtration chromatography showed that the recombinant enzyme was both a homodimer and a homotetramer, with the dimer being the more abundant form. The purified native enzyme, however, has been shown to be exclusively tetrameric. The two enzyme forms had comparable stabilities when they were thermoinactivated at 95°C. Differential scanning calorimetry revealed thermal transitions at 99 and 109.5°C for both forms, with an additional shoulder at 91°C for the tetramer. These results suggest that the association of the subunits into the tetrameric form may have little impact on the stability and biocatalytic properties of the enzyme.

Thermal Analysis of Fresh and Mature Oil Paint Films: The Effect of Pigments as Driers and the Solvent Leaching of Mature Paint Films

1990 ◽  
Vol 185 ◽  
Author(s):  
Christopher W. McGlinchey
Keyword(s):  
Thermal Analysis ◽  
Differential Scanning Calorimetry ◽  
Linseed Oil ◽  
Glass Transitions ◽  
Lead White ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Titanium White ◽  
Drying Properties ◽  
Paint Films

AbstractThe effect of titanium white, zinc white and lead white on the drying properties of poppy, walnut and linseed oil are analyzed by differential scanning calorimetry (DSC). All of the fresh films undergo complex thermal transitions between -100 and O°C. For some of the dried films subambient transitions that resemble glass transitions occur at about -30 O°C. After exposure to certain solvents, these sub-ambient transitions disappear or are reduced significantly. It is suggested that samples with diminished sub-ambient transitions become more brittle as a result of the loss of materials that act as plasticizers.

Differential scanning calorimetry studies of rabbit cardiac sarcolemma

1987 ◽  
Vol 65 (5) ◽  
pp. 429-437
Author(s):  
A. L. Jacobson ◽  
H. Braun
Keyword(s):  
Differential Scanning Calorimetry ◽  
Dimethyl Sulfoxide ◽  
Enzymatic Degradation ◽  
Liquid Crystalline ◽  
Heat Denaturation ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Cardiac Sarcolemma ◽  
Small Magnitude ◽  
Lower Temperature

Thermal transitions were measured by differential scanning calorimetry for rabbit cardiac sarcolemma in 3-(N-morpholino)propanesulfonic acid buffer at pH 7.5, in glycerol–buffer and dimethyl sulfoxide – buffer mixtures, after heat denaturation, and after enzymatic degradation of the proteins. Specific solvent effects on the protein transitions were observed. Glycerol stabilized some of the four protein transitions, while dimethyl sulfoxide destabilized all protein transitions. The thermal transitions in the lower temperature range were studied for both the membranes and the lipid extracted from the membranes. A very small endotherm was observed for both the lipid extracted from the sarcolemma and the intact membrane (0.1–0.2 cal/g; 1 cal = 4.1868 J). A larger endotherm was observed in both the glycerol–buffer and dimethyl sulfoxide – buffer mixtures. Major perturbation of the protein by enzymatic degradation (papain or trypsin digestion), by heat denaturation, or by reaction with excess N-ethylmaleimide all produced larger endotherms near 20 °C. The very small magnitude of the endotherm near 20 °C suggests that it is not a typical gel – liquid crystalline transition of the bilayer. However, the occurrence of an endotherm in the extracted lipid suggests that some reorientation of lipid is involved.

scholarly journals A calorimetric study of human CuZn superoxide dismutase

1987 ◽  
Vol 248 (3) ◽  
pp. 981-984 ◽  
Author(s):  
C G Biliaderis ◽  
R J Weselake ◽  
A Petkau ◽  
A D Friesen
Keyword(s):  
Differential Scanning Calorimetry ◽  
Binding Sites ◽  
Specific Activity ◽  
Calorimetric Study ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Structural Units ◽  
Conformational Order ◽  
Higher Temperature ◽  
Cuzn Superoxide Dismutase

Structural alterations, as manifested by thermal transitions, caused by removal or binding of metal ions to human and bovine CuZn superoxide dismutases (SODs) were investigated by differential scanning calorimetry. Although holo forms of the two mammalian enzymes exhibited irreversible thermal transitions (delta Hcal. = 27.7 J/g and Td = 104 degrees C for bovine SOD; delta Hcal. = 23.6 J/g and Td = 101 degrees C for human SOD), only the bovine apoenzyme showed the presence of a less thermostable form (delta Hcal. = 10.7 J/g and Td = 63 degrees C). These observations suggested that human apo-SOD had considerably less conformational order than bovine apo-SOD. Reconstitution of human and bovine apoenzymes with Cu2+ and Zn2+ resulted in recovery of thermodynamic parameters and specific activity. Binding of Zn2+ alone to human apo-SOD resulted in the formation of two distinct structural units, detectable by differential scanning calorimetry, which underwent conformational disorder at 82 and 101 degrees C respectively. Saturation of binding sites with both Zn2+ and Cu2+ appeared to stabilize the enzyme structure further as shown by elimination of the low-temperature transition and the appearance of another thermal transition at a higher temperature.

A calorimetric study of the thermal transitions of Halobacterium cutirubrum

1982 ◽  
Vol 60 (4) ◽  
pp. 419-421 ◽  
Author(s):  
K. C. Cho ◽  
K. C. Chow ◽  
K. K. Mark
Keyword(s):  
Differential Scanning Calorimetry ◽  
Envelope Glycoprotein ◽  
Hydrophobic Interactions ◽  
Major Protein ◽  
Calorimetric Study ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Previous Proposal ◽  
Protein Components

The thermal transitions of Halobacterium cutirubrum have been examined by differential scanning calorimetry. Two distinct peaks corresponding to the denaturation of two major protein components were observed in the heating curves. One of the peaks has been assigned to the denaturation of the envelope glycoprotein. The variations of the denaturation temperatures with the addition of glucose, glycerol, NaNO3, and NaSCN are consistent with the previous proposal that hydrophobic interactions are essential in stabilizing the glycoprotein.

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