Journal
MEAT SCIENCE
Volume 119, Issue -, Pages 32-40Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.meatsci.2016.04.020
Keywords
PSE; Heat denaturation; Protein aggregation; Water-holding capacity; X-ray diffraction
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Funding
- Kyllikki ja Uolevi Lehikoisen saatio
- Swedish Research Council [2009-4302]
- Max IV Laboratory, Lund, Sweden
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The role of heat-denatured sarcoplasmic proteins in water-holding is not well understood. Here we propose a new hypothesis that in PSE-like conditions denatured sarcoplasmic proteins aggregate within and outside myofilaments, improving the water-holding of denatured myofibrils. The process is compartmentalized: 1) within the filaments the denatured sarcoplasmic proteins shrink the lattice space and water is expelled; and 2) between the myofibrils and in the extracellular space, the coagulated sarcoplasmic proteins trap the expelled water from interfilamental space. The effect of sarcoplasmic proteins on the water-holding of myofibrils following incubation for 1 h at 21 to 44 degrees C was investigated. Our results were consistent with the new hypothesis. Myofibrils without sarcoplasm had the poorest water-holding. With increasing amount of denatured sarcoplasmic proteins, the water-holding of heat-denatured myofibrils improved proportionally. X-ray diffraction was used to measure the lattice space between the filaments. Precipitated sarcoplasmic proteins shrank (P < 0.001) the lattice spacing by 63% at 44 degrees C. (C) 2016 Elsevier Ltd. All rights reserved.
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