Abstract
This study investigated the effects of l-arginine and l-lysine on the water holding capacity, shear force, color, and protein denaturation of frozen porcine Longissimus lumborum. Four batches were prepared, each corresponding to samples of an experimental treatment: without a cryoprotective solution, injecting a 0.3% sodium tripolyphosphate and 0.5% NaCl solution, a 0.5% l-arginine solution, or a 0.5% l-lysine solution. The results showed that both l-arginine and l-lysine decreased thawing loss, cooking loss, shear force, L⁎ values, b⁎ values, and surface hydrophobicity, but they increased pH values, a⁎ values, percentages of peak areas for T21 relaxation times, and Ca2+-ATPase activity. Additionally, both histological and transmission electron microscopy images showed that l-lysine, and especially l-arginine could inhibit the formation of gaps between fiber bundles, alleviate the disruption of intracellular spaces, and maintain the structural integrity of sarcomeres. Overall, the results showed that both l-arginine and l-lysine hindered the structural damage of muscle fibers during freezing and protected myofibrillar proteins from denaturation, ultimately contributing to superior quality attributes.
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