Gelation of milks of different species (dairy cattle, goat, sheep, red deer, and water buffalo) using glucono-δ-lactone and pepsin.

Dynamic low-amplitude oscillatory rheology was used to study the gelation properties of skim milk gels made at 37°C, using glucono-δ-lactone alone (acid gels) or a combination of glucono-δ-lactone and porcine pepsin ("combination gels"). The protein contents of the skim milks increased in the order goat milk < cattle milk < buffalo milk < sheep milk < deer milk, whereas the average casein micelle diameters increased in the order cattle milk < buffalo milk < goat milk < sheep milk ≃ deer milk. The gelation pH (4.55-4.73) of all milks were close to the isoelectric pH (4.6) of casein, except for buffalo milk, which had a significantly higher gelation pH (5.72). The storage moduli (G') of the acid gels increased with time in the milks of all species except for buffalo milk, for which a double peak in G' was observed. The final storage moduli after 6 h (G'final) increased in the order goat milk < cattle milk < sheep milk < deer milk < buffalo milk. In general, for the combination gels, the G'final values and the gelation pH increased to variable extents, except for goat milk. Confocal scanning laser microscopy showed that goat milk and cattle milk formed gels with more open protein networks compared with the dense clustered protein networks of the milks with high protein content (buffalo, sheep, and deer milks). This study indicates that milks from different species respond differently under the action of an acid precursor and pepsin. These results can be used to provide a better understanding of curd making and the digestion properties of noncattle milks.