Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin

Formation of a structured clot during the gastric digestion of milk: Impact on the rate of protein hydrolysis

“…It has been shown that the processing treatment can affect the digestion of milk proteins, particularly whey proteins, by enzymes (Chobert, Briand, Grinberg, & Haertl e, 1995;Dalgalarrondo, Dufour, Chobert, Bertrand-Harb, & Haertl e, 1995;Guo, Fox, Flynn, & Kindstedt, 1995;Li, Ye, Lee, & Singh, 2013;Peram, Loveday, Ye, & Singh, 2013;Zeece, Huppertz, & Kelly, 2008). Native b-lactoglobulin (b-lg), comprising 50% of the total whey protein in bovine milk, is resistant to some proteases, particularly to pepsin, because of its unique structural stability at low pH (Miranda & P elissier, 1983;Reddy, Kella, & Kinsella, 1988).…”

“…Most of the hydrophobic amino acids, which are potential cleavage sites for pepsin, are buried inside the hydrophobic core and are not readily accessible. Heating, the addition of alcohols and esterification and adsorption at an interface have been reported to increase the susceptibility of b-lg to hydrolysis by pepsin Dalgalarrondo et al, 1995;Guo et al, 1995;Li et al, 2013;Peram et al, 2013;Zeece et al, 2008). These treatments induce conformational changes in b-lg, resulting in increased exposure of peptic cleavage sites and thus increased susceptibility to pepsin action.…”

Hemoglobin hydrolysates from porcine blood obtained through enzymatic hydrolysis assisted by high hydrostatic pressure processing

“…For example, conformational changes in dairy proteins induced by HHP substantially increase the susceptibility of beta-lactoglobulin to hydrolysis by most enzymes (Stapelfeldt et al, 1996); thus suggesting that HHP could be used to reduce the allergenicity of whey proteins (Chicón et al, 2009;Zeece et al, 2008). Quirós et al (2007) proposed a method for the commercial production of bioactive peptides from ovalbumin, consisting on HHP treatment of egg white proteins followed by hydrolysis with proteases.…”

Emerging Technologies for Targeted Food Processing

“…For such a system, the pressure-induced gel matrix yields small particles in highly packed ß-lactoglobulin, unlike the gels after heating, which exhibit finely stranded aggregates. Furthermore, Zeece et al (2008) reported that a HP treatment from 400 to 800 MPa at 20 C considerably improved the digestibility of ß-lactoglobulin. Thus, pressure-induced protein gels open up the possibility of generating new textures as they additionally retain their original flavor and color accompanied by a glossy appearance.…”