scholarly journals Calorimetric Study of Thermal Denaturation of β-Lactoglobulin

1984 ◽  
Vol 67 (8) ◽  
pp. 1699-1706 ◽  
Author(s):  
Kwan Hwa Park ◽  
Daryl B. Lund
Keyword(s):  
Thermal Denaturation ◽  
Calorimetric Study ◽  
Β Lactoglobulin

scholarly journals A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate

1977 ◽  
Vol 44 (3) ◽  
pp. 509-520 ◽  
Author(s):  
M. Rüegg ◽  
Ursula Moor ◽  
B. Blanc
Keyword(s):  
Heat Treatment ◽  
Xanthine Oxidase ◽  
Conformational Changes ◽  
Thermal Denaturation ◽  
Whey Proteins ◽  
Calorimetric Study ◽  
Thermal Transitions ◽  
Scanning Calorimetry ◽  
Β Lactoglobulin ◽  
Dsc Thermograms

SummaryDifferential scanning calorimetry (DSC) was used to study thermal transitions of the following whey proteins and enzymes in milk ultrafiltrate solution: β-lactoglobulin, α-lactalbumin, serum albumin, γ-globulin, apo- and Fe-lactoferrin, lysozyme, ribonuclease, α-chymotrypsin and xanthine oxidase. Denaturation enthalpies (ΔHD), denaturation temperatures (TD) and the half width of the denaturation peaks in DSC thermograms (ΔT½D) were determined and the degree of renaturation was estimated by rescanning previously denatured samples. A fair correlation between the results obtained by DSC and other more classical methods was found in general. However, for some proteins (α-lactalbumin, lysozyme, ribonuclease and xanthine oxidase), which have so far been considered relatively thermostable, calorimetry reveals conformational changes starting at temperatures as low as about 45 °C. In these cases thermostability observed after heat treatment of milk should be interpreted in terms of renaturation and not of high temperatures of denaturation.

Thermal denaturation of bovine β-lactoglobulin in different protein mixtures in relation to antigenicity

2019 ◽  
Vol 91 ◽  
pp. 89-97 ◽  
Author(s):  
Dimuthu Bogahawaththa ◽  
Jayani Chandrapala ◽  
Todor Vasiljevic
Keyword(s):  
Thermal Denaturation ◽  
Β Lactoglobulin

Spectroscopic and Calorimetric Study of 2,2′-Dibipyridin Cu(II) Chloride Binding to Bovine β-Lactoglobulin

2013 ◽  
Vol 42 (4) ◽  
pp. 705-715 ◽  
Author(s):  
Adeleh Divsalar ◽  
Ali A. Saboury ◽  
Thomas Haertlé ◽  
Lindsay Sawyer ◽  
Hassan Mansouri-Torshizi ◽  
...  
Keyword(s):  
Calorimetric Study ◽  
Chloride Binding ◽  
Β Lactoglobulin

Assessment of the Thermal Treatment of Milk during Continuous Microwave and Conventional Heating

1996 ◽  
Vol 59 (8) ◽  
pp. 889-892 ◽  
Author(s):  
ROSINA LOPEZ-FANDIÑO ◽  
MAR VILLAMIEL ◽  
NIEVES CORZO ◽  
AGUSTIN OLANO
Keyword(s):  
Heat Treatment ◽  
Continuous Flow ◽  
Thermal Denaturation ◽  
Microwave Treatment ◽  
Conventional Heating ◽  
Treatment Intensity ◽  
Heat Distribution ◽  
Conventional System ◽  
Effective System ◽  
Β Lactoglobulin

The effect of continuous-flow microwave treatment of milk was estimated by using indicators of the heat treatment intensity (β-lactoglobulin denaturation, inactivation of alkaline phosphatase and lactoperoxidase). Results were compared with those obtained using a conventional process having the same heating, holding, and cooling phases. Continuous microwave treatment proved to be an effective system for pasteurizing milk, with the inclusion of a holding phase to maintain the time and temperature conditions required. At high pasteurization temperatures, the extent of thermal denaturation observed with the microwave treatment was lower than that obtained with the conventional system. This result could be attributed to a better heat distribution and the lack of hot surfaces contacting the milk in the case of the microwave unit.

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