2006
DOI: 10.1016/j.idairyj.2005.06.010
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Peptide–peptide and protein–peptide interactions in mixtures of whey protein isolate and whey protein isolate hydrolysates

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Cited by 59 publications
(62 citation statements)
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“…Applying enzymatic hydrolysis, functional properties of proteins are modified (Were et al 1997;De la Barca et al 2000;Ortiz and Wagner 2002). Enzymatic hydrolysis decreases the molecular weight and increases the number of ionizable groups in proteins and expose hydrophobic groups which change the physical and chemical interactions (Creusot et al 2006). Soybean proteins glycinin and βconglycinin mainly reflect the functional properties of SPI and show considerable differences in functional properties such as emulsifying due to their diverse molecular structure (Utsumi and Kinsella 1985).…”
Section: Effects On the Technofunctionality Of Spimentioning
confidence: 99%
“…Applying enzymatic hydrolysis, functional properties of proteins are modified (Were et al 1997;De la Barca et al 2000;Ortiz and Wagner 2002). Enzymatic hydrolysis decreases the molecular weight and increases the number of ionizable groups in proteins and expose hydrophobic groups which change the physical and chemical interactions (Creusot et al 2006). Soybean proteins glycinin and βconglycinin mainly reflect the functional properties of SPI and show considerable differences in functional properties such as emulsifying due to their diverse molecular structure (Utsumi and Kinsella 1985).…”
Section: Effects On the Technofunctionality Of Spimentioning
confidence: 99%
“…It was suggested that the high viscosity was caused by aggregation of the peptides causing a gelation. 27,28 Detailed study of this surprising effect revealed that hydrolysis of the α-lactalbumin fraction by this enzyme in the presence of calcium leads to strong gel formation, 29 and further studies on this gel showed hollow linear filaments similar to microtubules. 25 A very detailed description of the self-assembly of hydrolyzed α-lactalbumin into nanotubes resulted from the work of Graveland-Bikker and is described in her PhD thesis.…”
Section: Viscositymentioning
confidence: 97%
“…This increases peptide attractions/aggregation interactions producing a decrease in solubility. A high grade of hydrophobicity and sulfhydryl disulfide interactions increases protein insolubility, even after a high percentage of hydrolysis (Creusot and others ; Paraman and others ; Creusot and Gruppen ). However, the optimal grade of hydrolysis is determined by the final goal.…”
Section: Protease Applicationsmentioning
confidence: 99%