scholarly journals Conformational changes of β-lactoglobulin induced by shear, heat, and pH—Effects on antigenicity

2015 ◽  
Vol 98 (7) ◽  
pp. 4255-4265 ◽  
Author(s):  
Toheder Rahaman ◽  
Todor Vasiljevic ◽  
Lata Ramchandran
Keyword(s):  
Conformational Changes ◽  
Ph Effects ◽  
Β Lactoglobulin

pH Effects on the Molecular Structure of β-Lactoglobulin Modified Air–Water Interfaces and Its Impact on Foam Rheology

Langmuir ◽  
2013 ◽  
Vol 29 (37) ◽  
pp. 11646-11655 ◽  
Author(s):  
Kathrin Engelhardt ◽  
Meike Lexis ◽  
Georgi Gochev ◽  
Christoph Konnerth ◽  
Reinhard Miller ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Ph Effects ◽  
Β Lactoglobulin ◽  
Foam Rheology

scholarly journals Recognition of Conformational Changes in β-Lactoglobulin by Molecularly Imprinted Thin Films

2007 ◽  
Vol 8 (9) ◽  
pp. 2781-2787 ◽  
Author(s):  
Nicholas W. Turner ◽  
Xiao Liu ◽  
Sergey A. Piletsky ◽  
Vladimir Hlady ◽  
David W. Britt
Keyword(s):  
Thin Films ◽  
Conformational Changes ◽  
Molecularly Imprinted ◽  
Β Lactoglobulin

Conformational changes of β-lactoglobulin induced by anionic phospholipid

2006 ◽  
Vol 121 (3) ◽  
pp. 218-223 ◽  
Author(s):  
Xiaohua Liu ◽  
Li Shang ◽  
Xiue Jiang ◽  
Shaojun Dong ◽  
Erkang Wang
Keyword(s):  
Conformational Changes ◽  
Anionic Phospholipid ◽  
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.

Sign in / Sign up

Export Citation Format

Share Document