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 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

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.

scholarly journals Epicatechin-induced conformational changes in β-lactoglobulin B monitored by FT-IR spectroscopy

SpringerPlus ◽  
2013 ◽  
Vol 2 (1) ◽  
pp. 661 ◽  
Author(s):  
Alessandro Nucara ◽  
Paola Maselli ◽  
Valeria Giliberti ◽  
Marina Carbonaro
Keyword(s):  
Ir Spectroscopy ◽  
Conformational Changes ◽  
Ft Ir ◽  
Β Lactoglobulin ◽  
Ft Ir Spectroscopy

scholarly journals Antigenicity and functional properties of β-lactoglobulin conjugated with fructo-oligosaccharides in relation to conformational changes

2013 ◽  
Vol 96 (5) ◽  
pp. 2808-2815 ◽  
Author(s):  
J.Z. Zhong ◽  
Y.J. Xu ◽  
W. Liu ◽  
C.M. Liu ◽  
S.J. Luo ◽  
...  
Keyword(s):  
Functional Properties ◽  
Conformational Changes ◽  
Β Lactoglobulin
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