Aggregation properties of aqueous casein hydrolysate solutions at different pH

Influence of aggregation on the antioxidative capacity of milk peptides

“…Aggregation of food peptides during enzymatic hydrolysis has been reported earlier (Creusot, Gruppen, van Koningsveld, de Kruif, & Voragen, 2006;Liu & Guo, 2008;Otte et al, 1997;Su, He, & Qi, 2008). The present study further suggested that, at acidic pH values, milk peptides were prone to aggregation caused by the low z-potential and hydrophobic interactions, which led to the formation of covalent bonds among milk peptides.…”

“…The presence of electrostatic charges of the aggregates was thus likely responsible for the antioxidant capacity of aggregates, in addition to the reactive groups such as SH group, aromatic amino acid residues. Liu and Guo (2008) showed that aggregation of casein hydrolysates resulted in aggregates having compact structure at pH 2.0 and looser structure at higher pH. The present study further suggested that reduction in antioxidant capacity of milk peptides freeze-dried at pH 2.0 occurred due to the formation of micrometer-sized particles that had a compact structure, and the reduction of cysteine, which was involved in covalent bond formation during aggregation.…”

“…The aggregation of milk peptides could occur during enzymatic hydrolysis of whey proteins and caseins (Liu & Guo, 2008;Otte et al, 1997). The self-assembling process of amphiphilic peptides from caseins having a molecular masses of 2e6 kDa was shown to involve chemical interactions such as hydrophobic interactions, H-bond and the cation-p action, leading to the formation of macroaggregates (Liu & Guo, 2008).…”

A combination of soybean and skimmed milk reduces osteoporosis in rats

“…Proteins are a nutritionally important source of both nitrogen and essential amino acids (Liu & Guo, 2008). The modification of soy and skimmed milk proteins by fermentation usually results in structural changes and results in loss of protein solubility and increased viscosity and essential amino acid content.…”

Characterization of the Spindle Morphology Nanomicelles Assembled from Sericin and Gelatin

“…Not only can protein chain segment, temperature, time, and pH affect the assembling process, but also the multilevel structure of protein can have significant influence. Research showed that some protein can be assembled into spherical micelles [23][24][25][26][27]. But there were seldom reports on assembling different morphology of complex micelles based on using different proteins by controlling assembling conditions.…”