Improved Emulsifying Properties of β-Barrel Domain Peptides Obtained by Membrane-Fractionation of a Limited Tryptic Hydrolysate of β-Lactoglobulin

1996 ◽  
Vol 44 (11) ◽  
pp. 3437-3443 ◽  
Author(s):  
Xiaolin L. Huang ◽  
George L. Catignani ◽  
Harold E. Swaisgood
Keyword(s):  
Emulsifying Properties ◽  
Membrane Fractionation ◽  
Tryptic Hydrolysate ◽  
Β Lactoglobulin

Effect of high pressure homogenization on the structure and the interfacial and emulsifying properties of β-lactoglobulin

2018 ◽  
Vol 537 (1-2) ◽  
pp. 111-121 ◽  
Author(s):  
Ali Ali ◽  
Isabelle Le Potier ◽  
Nicolas Huang ◽  
Véronique Rosilio ◽  
Monique Cheron ◽  
...  
Keyword(s):  
High Pressure ◽  
High Pressure Homogenization ◽  
Emulsifying Properties ◽  
Β Lactoglobulin

Selective separation of cationic peptides from a tryptic hydrolysate of β-lactoglobulin by electrofiltration

2006 ◽  
Vol 94 (2) ◽  
pp. 223-233 ◽  
Author(s):  
Jean-François Lapointe ◽  
Sylvie F. Gauthier ◽  
Yves Pouliot ◽  
Christian Bouchard
Keyword(s):  
Selective Separation ◽  
Cationic Peptides ◽  
Tryptic Hydrolysate ◽  
Β Lactoglobulin

scholarly journals Occurrence of Peptide-Peptide Interactions during the Purification of Self-Assembling Peptide f1-8 from a β-Lactoglobulin Tryptic Hydrolysate

Molecules ◽  
2021 ◽  
Vol 26 (5) ◽  
pp. 1432
Author(s):  
Mathilde Pimont-Farge ◽  
Amélie Bérubé ◽  
Véronique Perreault ◽  
Guillaume Brisson ◽  
Shyam Suwal ◽  
...  
Keyword(s):  
Membrane Filtration ◽  
Hydrophobic Interactions ◽  
Covalent Bond ◽  
Peptide Profile ◽  
Hydrophobic Peptides ◽  
Self Assembling ◽  
Peptide Interactions ◽  
Tryptic Hydrolysate ◽  
The Impact ◽  
Β Lactoglobulin

Self-assembling peptides have gained attention because of their nanotechnological applications. Previous work demonstrated that the self-assembling peptide f1-8 (Pf1-8) that is generated from the tryptic hydrolysis of β-lactoglobulin can form a hydrogel after several purification steps, including membrane filtration and consecutive washes. This study evaluates the impact of each processing step on peptide profile, purity, and gelation capacity of each fraction to understand the purification process of Pf1-8 and the peptide-peptide interactions involved. We showed that peptide-peptide interactions mainly occurred through electrostatic and hydrophobic interactions, influencing the fraction compositions. Indeed, the purity of Pf1-8 did not correlate with the number of wash steps. In addition to Pf1-8, two other hydrophobic peptides were identified, peptide f15-20, and peptide f41-60. The gelation observed could be induced either through peptide-peptide interactions or through self-assembling, both being driven by non-covalent bond and more specifically hydrophobic interactions.

Membrane fractionation of a β-lactoglobulin tryptic digest: Effect of the pH

2013 ◽  
Vol 114 (1) ◽  
pp. 83-89 ◽  
Author(s):  
Ayoa Fernández ◽  
Adrián Suárez ◽  
Yishen Zhu ◽  
Richard J. FitzGerald ◽  
Francisco A. Riera
Keyword(s):  
Membrane Fractionation ◽  
Tryptic Digest ◽  
Β Lactoglobulin
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