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Animal Phys L7
| Question | Answer |
|---|---|
| Factors influencing pH decline and meat quality | genetics nutrition environment handling and transport large (rest period before laughter) immobilisation (stunning method) chilling temperature and rate |
| muscle remains _____ after death for hours to weeks | metabolically active |
| conversion involves | energy metabolism shift from aerobic to anaerobic pH decline from Lactic acid accumulation ATP depletion -> rigor mortis enzymatic degradation -> tenderisation oxidation |
| Stunning methods | CO2 stunning (pigs) Electrical stunning (sheep, poultry) Captive bolt (cattle) |
| CO2 stunning | occurs in pigs only not cost effective for larger animals pigs stunned in groups (reduces stress) O2 deprivation, loss of consciousness |
| Electrical stunning | sheep and poultry induces tonic-clonic seizure followed by exsanguination |
| Tonic phase (electrical stunning) | rigid muscles, no breathing |
| Clonic phase (electrical stunning) | relaxation, kicking, vocalisation |
| Captive bolt | penetrating percussive stun causes irreversible brain trauma must be followed be exsanguination to ensure death |
| Exsanguination | cutting major blood vessels in neck causes extreme blood loss removes oxygen and nutrients |
| Order of tissue death | nerves: less than 15 mins muscle: several hours |
| Rigor mortis | occurs when ATP depleted -> muscles can't relax actin-myosin cross bridges form permanently defines sarcomere length, |
| Short sarcomeres | tougher meat |
| long sarcomeres | more tender meat |
| factors influencing rigor | temperature muscle fibre type pre-slaughter stress glycogen reserves |
| Postmortem energy metabolism Lack of O2 shifts metabolism to....... | Glycolysis, which produces lactate |
| Postmortem energy metabolism Lactate accumulation causes..... | pH to fall from approx 7.0 to 5.5 |
| Too rapid pH decline | protein denaturation, causing pale, soft exudative meat (PSE) |
| Too slow pH decline | dark, firm, dry (DFD) meat |
| ATP powers | ion pumps muscle relaxation and homeostasis |
| When ATP depletes | ion gradients collapse membranes lose integrity cellular compartments break down |
| What happens to the mitochondria when there is no oxygen? | mitochondria stop producing ATP Reactive oxygen species form, causing oxidative damage Antioxidant defences fail |
| ROS | Reactive oxygen species |
| Consequences of mitochondrial failure and oxidation | protein and lipid oxidation -> reduced meat colour and flavour Loss of membrane integrity -> drip loss (exudate) |
| Meat ageing | time dependent process postmortem that improves tenderness caused by protein degradation (not bacterial spoilage) |
| Warner-bratzler shear force (WBSF) | measure of meat tenderness lower WSBF = more tender, better consumer acceptance |
| meat tenderisation | structural myofibrillar proteins broken down |
| two main processes of meat tenderisation | enzymatic (protease driven) non-enzymatic (oxidative and physical) |
| Proteolytic systems in meat tenderisation (calpain system) | Main enzyme: calpain Activation: Ca2+ dependent Majo contributor to myofibrillar degradation acts early postmortem; responsible for Z-line breakdown |
| Proteolytic systems in meat tenderisation Lysosomal (endolysosomal) | Main enzyme: cathepsins Activation: acidic pH non-specific protein degradation limited due to neutral postmortem pH |
| Proteolytic systems in meat tenderisation Proteasome (ubiquitin) | Main enzyme: Proteasome Activation: ATP-dependent specific protein degradation limited postmortem (no ATP) |
| Calcium's role | Loss of SERCA activity leads to cytosolic Ca2+ increases high Ca2+ activates calpains and Z-line degradation (structural weakening) |
| Calpain system vs Protein turnover (live muscle) | Calpain "unpacks" myofibrils for further degradation by proteasome/lysosome |
| Calpain system vs Protein turnover (postmortem muscle) | Only calpain remains active (others need ATP of low pH) Therefore, cal pains drive tenderisation |
| Lipid peroxidation | Oxidation of membrane lipids causes cell leakage (drip loss) |
| Causes of lipid peroxidation | endogenous ROS production bacterial spoilage |
| Effects of lipid peroxidation | increased drip loss (less juicy meat) deterioration of flavour reduced shelf life |
| Deoxymyoglobin | reduced Fe2+ purple/red colour |
| Oxymyoglobin | oxygenated Fe2+ Bright red (the yummiest one) |
| Metmyoglobin | Oxidised Fe3+ Brown/ grey looks yucky but usually ok |
| what determines meat colour? | oxygen exposure and oxidation |
| pH and temp effects on meat quality | caracsses rapidly chilled for food safety controlled chilling balances pH decline and temp drop |
| cold shortening | cooling too quickly pre-rigor sarcomeres lock into shortened position results in tougher meat texture |
| muscle shortening postmortem | continues for up to 24 hours postmortem rate depends on temp and pH isometric tension increases and muscles contract and then stabilise in rigor |