This study aimed to quantify the effect of muscle, ageing and cooking temperature on the texture, cooking loss and shrinkage of cooked beef. Cuboids from unaged (1 day post mortem) and aged (14 days post mortem) semitendinosus, biceps femoris and psoas major muscles, from both sides of five beef carcasses, were cooked at four different cooking temperatures (50, 60, 70 and 80 °C) for 30 min. and their Warner–Bratzler shear force (WBSF), cooking loss and shrinkage (longitudinal and transverse) were quantified. The WBSF was reduced by ageing in the muscles at the specific cooking temperatures: psoas major (cooked at 50, 60 and 80 °C), semitendinosus (70 and 80 °C) and biceps femoris (80 °C). The cooking loss was 3% greater in aged compared to unaged muscles. The longitudinal shrinkage was greatest in psoas major at 80 °C amongst the muscle types and it was reduced by ageing in psoas major (70 and 80 °C) and biceps femoris (80 °C). The transverse shrinkage was reduced by ageing only in biceps femoris, across all temperatures; and the diameter of homogenized fibre fragments from semitendinosus and biceps femoris was reduced more by cooking at 50 °C in unaged compared to aged condition. WBSF was related to transverse shrinkage, and cooking loss was related to longitudinal shrinkage. The effect of muscle type on the physical changes occurring during cooking of beef is dependent on ageing and cooking temperature.

An in-depth proteomic study of sheep milk whey is reported and compared to the data available in the literature for the cow whey proteome. A combinatorial peptide ligand library kit (ProteoMiner) was used to normalize protein abundance in the sheep whey proteome followed by an in-gel digest of a 1D-PAGE display and an in-solution digestion followed by OFFGEL isoelectric focusing fractionation. The peptide fractions obtained were then analyzed by LC-MS/MS. This enabled identification of 669 proteins in sheep whey that, to our knowledge, is the largest inventory of sheep whey proteins identified to date. A comprehensive list of cow whey proteins currently available in the literature (783 proteins from unique genes) was assembled and compared to the sheep whey proteome data obtained in this study (606 proteins from unique genes). This comparison revealed that while the 233 proteins shared by the two species were significantly enriched for immune and inflammatory responses in gene ontology analysis, proteins only found in sheep whey in this study were identified that take part in both cellular development and immune responses, whereas proteins only found in cow whey in this study were identified to be associated with metabolism and cellular growth.