Untersuchungen zur Reaktionskinetik der Molkenprotein‐Denaturierung und deren technologischer Bedeutung

Combined effect of dynamic heat treatment and ionic strength on the properties of whey protein foams – Part II

“…Although Ibanoglu and Karatas (2001) found that overrun and foam stability were reduced when buffer molarity was increased from 50 to l00 mM, sodium chloride is usually reported to improve the stability of white egg protein foams (Raikos et al, 2007). Aggregated proteins have been reported to possess a higher water binding capacity than native whey proteins (Dannenberg, 1986;Spiegel, 1999). According to Leman and Dolgan (2004), a limited thermal denaturation of proteins caused by heating promotes the formation of depolymerised and unfolded b-Lg macromolecules that can quickly diffuse and adsorb to form a thick interfacial film by refolding through numerous interactions at the interface.…”

Inactivation of bacteriophages by thermal and high-pressure treatment

“…High heat treatment of milk impairs the cheese-making properties of milk (Walstra, Geurts, Noomen, Jellema, & van Boekel, 1999). For instance, in a UHT-treated milk, 80% of the whey proteins are denatured (Dannenberg, 1986) and associate with the casein micelles. In consequence, casein aggregation is hindered and, therewith, the rennet coagulation properties of the milk are impaired (Lucey, Gorry, & Fox, 1993).…”

Effects of heat-treatment on insulin-like growth factor-1 in bovine milk

“…Heat treatments above pasteurization temperature denature whey proteins (Dannenberg, 1986;Kessler, 2002) and in particular cause b-lactoglobulin to form a complex with k-casein (Dalgleish, 1990). Heating at 90 C for 15 s denatures 45% of b-lactoglobulin (Dannenberg, 1986). It would have been preferable to express the IGF-1 concentrations as ng g À1 protein in each fraction.…”

“…It can also be concluded that acid precipitation at pH 4.6, which was used for the separation of casein from whey, did not activate the growth factor, because the same result was obtained by ultracentrifugation. Heat treatments above pasteurization temperature denature whey proteins (Dannenberg, 1986;Kessler, 2002) and in particular cause b-lactoglobulin to form a complex with k-casein (Dalgleish, 1990). Heating at 90 C for 15 s denatures 45% of b-lactoglobulin (Dannenberg, 1986).…”