Role of Pyridoxamine in the Formation of the Amadori/Heyns Compounds and Aggregates during the Glycation of β-Lactoglobulin with Galactose and Tagatose

2010 ◽  
Vol 58 (1) ◽  
pp. 500-506 ◽  
Author(s):  
Marta Corzo-Martínez ◽  
F. Javier Moreno ◽  
Agustín Olano ◽  
Mar Villamiel
Keyword(s):  
Β Lactoglobulin

scholarly journals Evidence for β-lactoglobulin involvement in vitamin D transportin vivo- role of the γ-turn (Leu-Pro-Met) of β-lactoglobulin in vitamin D binding

FEBS Journal ◽  
2009 ◽  
Vol 276 (8) ◽  
pp. 2251-2265 ◽  
Author(s):  
Ming Chi Yang ◽  
Nai Chi Chen ◽  
Chun-Jung Chen ◽  
Chin Yun Wu ◽  
Simon J. T. Mao
Keyword(s):  
Vitamin D ◽  
Β Lactoglobulin

scholarly journals β-Lactoglobulin-linoleate complexes: In vitro digestion and the role of protein in fatty acid uptake

2013 ◽  
Vol 96 (7) ◽  
pp. 4258-4268 ◽  
Author(s):  
Solène Le Maux ◽  
André Brodkorb ◽  
Thomas Croguennec ◽  
Alan A. Hennessy ◽  
Saïd Bouhallab ◽  
...  
Keyword(s):  
Fatty Acid ◽  
In Vitro Digestion ◽  
Fatty Acid Uptake ◽  
Acid Uptake ◽  
Β Lactoglobulin

scholarly journals Binding of CML-Modified as Well as Heat-Glycated β-lactoglobulin to Receptors for AGEs Is Determined by Charge and Hydrophobicity

2020 ◽  
Vol 21 (12) ◽  
pp. 4567 ◽  
Author(s):  
Hannah E. Zenker ◽  
Malgorzata Teodorowicz ◽  
Arifa Ewaz ◽  
R.J. Joost van Neerven ◽  
Huub F.J. Savelkoul ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Tertiary Structure ◽  
Glyoxylic Acid ◽  
Native Page ◽  
Galectin 3 ◽  
Carboxymethyl Lysine ◽  
Antigen Presenting ◽  
Age Receptors ◽  
Β Lactoglobulin

Intake of dietary advanced glycation end products (AGEs) is associated with inflammation-related health problems. Nε-carboxymethyl lysine (CML) is one of the best characterised AGEs in processed food. AGEs have been described as ligands for receptors present on antigen presenting cells. However, changes in protein secondary and tertiary structure also induce binding to AGE receptors. We aimed to discriminate the role of different protein modifications in binding to AGE receptors. Therefore, β-lactoglobulin was chemically modified with glyoxylic acid to produce CML and compared to β-lactoglobulin glycated with lactose. Secondary structure was monitored with circular dichroism, while hydrophobicity and formation of β-sheet structures was measured with ANS-assay and ThT-assay, respectively. Aggregation was monitored using native-PAGE. Binding to sRAGE, CD36, and galectin-3 was measured using inhibition ELISA. Even though no changes in secondary structure were observed in all tested samples, binding to AGE receptors increased with CML concentration of CML-modified β-lactoglobulin. The negative charge of CML was a crucial determinant for the binding of protein bound CML, while binding of glycated BLG was determined by increasing hydrophobicity. This shows that sRAGE, galectin-3, and CD36 bind to protein bound CML and points out the role of negatively charged AGEs in binding to AGE receptors.

Role of calcium as trigger in thermal β-lactoglobulin aggregation

2002 ◽  
Vol 406 (2) ◽  
pp. 143-152 ◽  
Author(s):  
Jan-Willem F.A Simons ◽  
Hans A Kosters ◽  
Ronald W Visschers ◽  
Harmen H.J de Jongh
Keyword(s):  
Β Lactoglobulin

scholarly journals Role of Sulfhydryl Groups in the Interaction of κ-Casein and β-Lactoglobulin

1963 ◽  
Vol 46 (6) ◽  
pp. 564-565 ◽  
Author(s):  
W.H. Sawyer ◽  
S.T. Coulter ◽  
Robert Jenness
Keyword(s):  
Sulfhydryl Groups ◽  
Β Lactoglobulin

Role of β-lactoglobulin in the fouling of stainless steel surfaces by heated milk

2017 ◽  
Vol 66 ◽  
pp. 18-26 ◽  
Author(s):  
Tuan H. Truong ◽  
Ken Kirkpatrick ◽  
Skelte G. Anema
Keyword(s):  
Stainless Steel ◽  
Heated Milk ◽  
Steel Surfaces ◽  
Β Lactoglobulin

Improvement of rheological properties of firm acid gels by skim milk heating is conserved after stirring

2003 ◽  
Vol 70 (4) ◽  
pp. 423-431 ◽  
Author(s):  
P Cayot ◽  
J-F Fairise ◽  
B Colas ◽  
D Lorient ◽  
G Brulé
Keyword(s):  
Storage Modulus ◽  
Skim Milk ◽  
Rheological Parameters ◽  
Water Retention Capacity ◽  
Gel Structure ◽  
Casein Micelles ◽  
Retention Capacity ◽  
Β Lactoglobulin

The enhancement of the strength of set acid gels by heating milk was related to rheological parameters (water retention capacity, storage modulus) of corresponding stirred gels. To obtain accurate rheological data from stirred gel it was necessary to maintain a constant granulometry of gel particles and to recognize time after stirring as a contributing factor. Two hours after stirring, the gel exhibited a higher storage modulus when milk was heated above 80 °C. A measurement of viscosity of just-stirred yoghurt was sufficient to predict correctly the quality of a stirred gel analysed by viscoelastic measurements. Increased resstance to syneresis of just-stirred gels was related to higher viscosity. The quantity of β-lactoglobulin (β-lg) bound to casein micelles explains the improvement of these gel qualities. We have considered that the structure of the initial firm gel (mesostructure level) was conserved in fragments within the stirred gel. Consequently, the explanation given by various authors for the effect of heating milk on the properties of set gels can also be applied to stirred gels. The same mechanism, described in literature for structure formation of set gels from acidified milk is purposed to explain the role of heating milk on the recovery of gel structure after stirring. The β-lg association with casein micelles during heating favoured micelle connections during the acidification. It also favoured the association of gel fragments after stirring during the recovery in gel structure.

Key role of cysteine residues and sulfenic acids in thermal- and H 2 O 2 -mediated modification of β-lactoglobulin

2016 ◽  
Vol 97 ◽  
pp. 544-555 ◽  
Author(s):  
Anna C. Krämer ◽  
Peter W. Thulstrup ◽  
Marianne N. Lund ◽  
Michael J. Davies
Keyword(s):  
Cysteine Residues ◽  
Sulfenic Acids ◽  
Β Lactoglobulin
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