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"hsp20" - 1 õppematerjal

Liha töötlemine
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Liha töötlemine

decreases with time postmortem (Underwood increasingly being investigated as potential et al. 2008). In this study, pro-caspase 3 was factors influencing the conversion of muscle not activated during postmortem storage and to meat and meat quality. In living muscle caspase 3 activity was not correlated with tissue, HSP such as alpha β-crystallin, Warner-Bratzler shear force in beef longis- HSP20, and HSP27 have a homeostatic func- simus. The data from one study using muscle tion in which they stabilize unfolded pro- from callipyge and normal lambs indicated teins, help refold denatured proteins, and that caspase 3/7 and caspase 9 activities prevent protein aggregation (Liu and decreased between 1 and 21 days postmor- Steinacker 2001). Due to their abilities to tem but did not directly support or reject the protect cellular proteins from denaturation

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