Effect of limited hydrolysis on the interfacial rheology and foaming properties of β-lactoglobulin A

New views on foams from protein solutions

“…As a result, there are also many reported examples where these relations are not found [66] [67,68 • ]. Ipsen et al studied the interfacial and foam properties of hydrolysates of β-lactoglobulin [67]. They found that the maximum foam stability was obtained for higher degrees of hydrolysis, even though for these samples the interfacial properties (Π, E d ) were lowest.…”

Enzymatic hydrolysis of ovomucin and effect on foaming properties

“…For example, foam overrun and stability of whey protein isolate was improved by limited hydrolysis with alcalase to a DH of 3% (Althouse, Dinakar, & Kilara, 1995). However, the foam overrun and foam stability of b-lactoglobulin did benefit from extensive hydrolysis by a B. licheniformis protease, where a DH of 19% resulted in highest foam OR and hydrolysis to a DH of 86% resulted in increased foam stability (Ipsen et al, 2001). Davis et al (2005) were able to relate a high foam yield stress of hydrolysed b-lactoglobulin (DH $ 15%) to high values of elastic modulus and essentially no viscous modulus, meaning that increased foam stabilization is promoted by an elastic interface of adsorbed proteins and peptides between the air and water phases.…”

“…However, enzymatic modification of whole egg albumen with pancreatin and thermitase (Behnke, Kiss, Nadudvari, & Ruttloff, 1986) or pepsin (Bamforth & Cope, 1987) apparently increases the foaming capacity of egg albumen. Furthermore, enzymatic hydrolysis of other proteins such as caseins (Panyam & Kilara, 1996), b-lactoglobulin (Davis, Doucet, & Foegeding, 2005;Ipsen et al, 2001), and a rapeseed isolate (Larre et al, 2006) also has resulted in altered foaming properties.…”

Surface accumulation of milk proteins and milk protein hydrolysates at the air–water interface on a time-scale relevant for spray-drying

“…Disaggregation of the globular structure of the second major whey protein, α-lactalbumin, has also been shown to increase the adsorption dynamics at the air-water interface (Cornec, Kim, & Narsimhan, 2001). Hydrolysis of ß-lactoglobulin leads to an increased exposure of hydrophobic areas (Ipsen et al, 2001) and explains the increase in surface activity of hydrolysed whey protein. However, Davis et al (2005) emphasized that in the case of enzymatic hydrolysis the type of enzyme might affect the surface activity of the hydrolysate and that too strong hydrolysis might negatively affect functional properties related to the surface activity like e.g.…”

“…Furthermore it has been described that protein hydrolysis increases the surface activity of proteins (Panyam & Kilara, 1996). Improved foaming properties, which are associated with an increase in surface activity, have been described for hydrolysed β-lactoglobulin (Davis, Doucet, & Foegeding, 2005;Ipsen et al, 2001) and sodium caseinate (Walsh, Russell, & FitzGerald, 2008). For soy protein hydrolysate the effect depended on the degree of hydrolysis (Miñones Conde & Rodríguez Patino, 2007) and no increase in surface activity has been reported for grain legume protein derivates (Tsoukala, Papalamprou, Makri, Doxastakis, & Braudo, 2006).…”