Journal Articles

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    Protein and Lipid Digestibility of Pasture-Raised and Grain-Finished Beef: An In Vitro Comparison
    (MDPI (Basel, Switzerland), 2023-03-14) Kaur L; Elamurugan A; Chian FM; Zhu X; Boland M; Gagaoua M
    This study compared the digestibility of protein and fat components of pasture-raised and grain-finished beef using an in vitro oral-gastro-small intestinal digestion model. Two commonly consumed beef cuts, tenderloin (Psoas major) and striploin (Longissimus dorsi) were selected for this study. There were no substantial differences between the pasture-raised and grain-finished cuts of meat in terms of protein digestibility, as shown by the protein and peptide breakdown (observed through SDS-PAGE) and the degree of hydrolysis as measured by free amino nitrogen. Tenderloin, however, showed significantly (p < 0.05) higher overall protein digestibility than striploin. Both striploin and tenderloin digests from pasture-raised beef released significantly (p < 0.05) higher total amounts of free long-chain n-3 PUFAs and lower amounts of many free saturated fatty acids, notably palmitic and myristic acids, than those from grain-finished animals. The results suggest greater health benefits from consuming pasture-raised beef, particularly tenderloin.
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    Endogenous Proteolytic Systems and Meat Tenderness: Influence of Post-Mortem Storage and Processing
    (Korean Society for Food Science of Animal Resources (KoSFA), 2021-07-01) Kaur L; Hui SX; Morton JD; Kaur R; Chian FM; Boland M
    Meat proteolytic systems play a crucial role in meat tenderisation. Understanding the effects of processing technologies and post-mortem storage conditions on these systems is important due to their crucial role in determining the quality characteristics of meat and meat products. It has recently been proposed that tenderisation occurs due to the synergistic action of numerous endogenous proteolytic systems. There is strong evidence suggesting the importance of μ-calpain during the initial post-mortem aging phase, while m-calpain may have a role during long-term aging. The caspase proteolytic system is also a candidate for cell degradation in the initial stages of conversion of muscle to meat. The role of cathepsins, which are found in the lysosomes, in post-mortem aging is controversial. Lysosomes need to be ruptured, through aging, or other forms of processing to release cathepsins into the cytosol for participation in proteolysis. A combination of optimum storage conditions along with suitable processing may accelerate protease activity within meat, which can potentially lead to improved meat tenderness. Processing technologies such as high pressure, ultrasound, and shockwave processing have been reported to disrupt muscle structure, which can facilitate proteolysis and potentially enhance the aging process. This paper reviews the recent literature on the impacts of processing technologies along with post-mortem storage conditions on the activities of endogenous proteases in meat. The information provided in the review may be helpful in selecting optimum post-mortem meat storage and processing conditions to achieve improved muscle tenderness within shorter aging and cooking times.