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https://open.uns.ac.rs/handle/123456789/12114
Title: | Structure of beef Longissimus dorsi muscle frozen at various temperatures: Part 2-ultrastructure of muscles frozen at -10, -22, -33, -78 and -115°C | Authors: | Rahelić, S. Gawwad, A. Puač, S. |
Issue Date: | 1-Jan-1985 | Publisher: | Elsevier | Journal: | Meat Science | Abstract: | The changes in electron micrographs of muscles frozen at -10, -22, -33, -78 and -115°C were analyzed. The ultrastructure of muscle successively changed with decreasing freezing temperature whereas light microscopy indicated anomalous behaviour at -22°C. It appeared that, in muscles frozen at -10°C, there was no freezing of water intracellularly; in those frozen at -22°C, water was frozen intracellularly (but only in the I-band region); whereas, in muscles frozen at -33°C, water was frozen inside the fibres, both in the I- and the A-bands. In muscles frozen at -78 and -115°C, water is frozen intracellularly. These findings can be explained on the basis that, in the I-band region, the major protein is actin, which has a relatively high proportion of non-polar residues and holds water weakly, whereas the predominant protein in the A-band is myosin, which contains many polar residues and has a high water-holding capacity. © 1985. | URI: | https://open.uns.ac.rs/handle/123456789/12114 | ISSN: | 03091740 | DOI: | 10.1016/0309-1740(85)90083-X https://doi.org/10.1016/0309-1740(85)90083-X |
Appears in Collections: | TF Publikacije/Publications |
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