In order to study the effect of protein oxidation on the structure of myofibrils, extracted myofibrils from porcine longissimus dorsi muscle were incubated with different concentrations of the oxidant NaClO (0, 5, 10, 20 and 40 mM) at 5 ºC for 16 h. Increasing concentrations of NaClO led to a greater loss of free thiols and a larger particle size (in terms of D(v, 0.1), D(v, 0.5), D(v, 0.9), D(3, 2) and D(4, 3)) of myofibrils. Light microscope imaging showed that the myofibrils oxidized in 40 mM NaClO were less broken as compared to the non-oxidized group (0 mM NaClO). The increased structural integrity of myofibrils is likely caused by oxidation-induced protein cross-links, which resulted in a larger particle size when the myofibrils were subjected to homogenization.
|Titel på gästpublikation||Proceedings of 62nd International Congress of Meat Science and Technology|
|Status||Publicerad - jul 2016|
|MoE-publikationstyp||D3 Professionella konferenshandlingar|
|Evenemang||62nd international congress of meat science and technology - Bankok, Thailand|
Varaktighet: 14 aug 2016 → 19 aug 2016
- 416 Livsmedelsvetenskap