Foaming Properties of Acylated Rapeseed (Brassica napus L.) Hydrolysates

Emulsifying properties of acylated rapeseed (Brassica napus L.) peptides

“…These values were much lower than those for BSA (57.7 mN/m) but closer to SDS (44.0 mN/m), indicating that acylated peptides behave more like a detergent than like a protein at the air-water interface, which is consistent with both a low molecular weight and an amphiphilic character like that of detergents. Grafting of C 10 or C 12 alkyl chains to peptides resulted in molecules more effective than C 14 in decreasing the surface tension, which is in agreement with the foaming properties previously observed for these acylated peptides [6]. The influence of the hydrophobic chain of a molecule on the surface tension has been evaluated in alkylglycosides [3,4] and in proteins [9,10].…”

“…In this way, it is possible to generate amphiphilic molecules constituted of the hydrophilic region of the peptide and the hydrophobic fatty acid chain, a structure comparable to other surfactants such as, for example, sugar surfactants [3,4]. Previous results suggested that this type of lipophilized peptides could be of interest as surfactants in nonfood applications such as detergents, cosmetics or pharmaceutical products because of their good foaming properties [5,6]. In this present work, surface tension values at the air-water interface and the emulsifying behaviors of acylated peptides are investigated and compared to bovine serum albumin (BSA) and sodium dodecyl sulfate (SDS) as standard protein and surfactant-like emulsifiers, respectively.…”

Composition, functional properties and in vitro antioxidant activity of protein hydrolysates prepared from sardinelle (Sardinella aurita) muscle

“…Foaming properties are physicochemical characteristics of proteins, allowing them to form and stabilize foams. In the case of surfactants, the stability of foams is a consequence of the well-ordered orientation of the molecules at the interface, where the polar head is located in the aqueous phase and the hydrophobic chain faces the apolar component (Sanchez-Vioque et al 2001). …”

Green Production of Anionic Surfactant Obtained from Pea Protein

“…After hydrolysis of pea proteins, peptides do not longer produce foam under stirring. Due to their small length, the hydrophobic and hydrophilic parts cannot be distinguished in the peptide as it happens in proteins [36]. As a consequence, they do not have an amphiphilic character and do not adsorb at the water/air interface.…”