Unit 12 - Conversion of Muscle into Meat and Meat Quality Flashcards

1
Q

How DFD meat occur?

A

no decline of pH
- stressed preslaughter (long-term)
- glycogen stores are used up because of constant stress so when they are slaughtered, there is no more glycogen, therefore no lactate produced postmortem, and therefore the pH remains high
- observed more in beef

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

How does PSE meat occur?

A

sudden drop in pH postmortem
- stressed preslaughter (short-term)
- causes breakdown of glycogen for fight or flight and the system is triggered to produce lots of lactate and as the animal is being slaughtered, this causes the continuation of lactate production, therefore large drop in pH
- the thing that actually causes PSE is the denaturation of the proteins in the muscle due to acidity (low pH) mixed with the fact that the carcass body temp is very hot
- seen in pork

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is WHC?

A

water holding capacity - of myofibre proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is pl?

A

isoelectric point (number of - and + charges are equal)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Explain the Meat pH vs WHC graph

A

pl of the majority of the myofibrillar proteins is approx 5.1-5.4
at the isoelectric point - the + and - charged groups within a protein attract each other and the ability of the protein to attract and hold water is minimal
high WHC when pH is high or low

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What happens to WHC during postmortem?

A

declines during postmortem decrease the availability on the muscle proteins that bind water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

How does preslaughter stress occur?

A

release of stress hormones such as epinephrine
once released these hormone initiate a series of biochemical reactions designed to mobilize energy to meet the demands of the stressors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What does epinephrine activate?

A

glycogen phosphorylase which enhances glycogen breakdown

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is the activation process of the body during acute stress?

A

acute stress (short-term) -> accelerates the glycogenolysis -> rapidly declines pH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is the activation process of the body during chronic stress?

A

chronic stress (long-term) -> anticipate the glycogen consumption -> lack of sources for glycolysis postmortem

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What are two conditions associated with low muscle temperature prior to onset rigour?

A

thaw rigour
cold-shortening
happen because of the same mechanism but happen differently

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

How does cold temperature affect meat quality?

A

lowering the temperature will cause changes in the capacity of SR to control the Ca2+ in the sarcoplasm, the sarcoplasm becomes overloaded with Ca, more Ca in sarcoplasm, more contractions
if it occurs before the glycogen is depleted, a more severe contraction will occur
more contraction affects the tenderness

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What occurs to cause thaw rigour?

A
  • occurs when muscle is frozen before going into rigor, then thawed
  • during freezing: ice crystals grow and penetrate the sarcoplasmic reticulum. Subsequent thawing of the crystals enables a rapid release of Ca2+ into the sarcoplasm
  • upon thawing the muscle, Ca is rapidly released causing a massive contraction (because ATP is produced due to presence of glycogen)
    this causes an increase in meat toughness
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What occurs to cause cold shortening?

A
  • less severe than thaw rigor and occurs when muscle is chilled to less than 14 C before rigor
  • low temp prompts Ca release from sarcoplasmic reticulum, and at colder temps, the SR Ca ATPase cannot bind and resequester Ca effectively
  • resulting increase in cytosolic Ca concentration in the presence of ATP leads to muscle contraction and shortening
  • increase in meat toughness - less severe than thaw rigor
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What makes a carcass more susceptible to cold shortening?

A
  • red muscle is more susceptible to cold shortening than white muscle
  • red muscle has less developed SR
  • more subcutaneous fat insulates carcass and prevents drop in temp so carcasses with less subcut fat will be more susceptible
  • cold shortening is not seen in pig carcass
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

How to prevent cold shortening

A

use of electrical stimulation, accelerations glycolysis and ATP utilization -> permits onset of rigor to occur (burning through of glycogen) earlier and at greater temps than those that induce cold shortening
- when carcass enter cold environment, less glycogen will be available to produce ATP
- although calcium will be released in sarcoplasm, it won’t affect contraction intensity due to lack of ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Explain the graph showing lower pH in stimulated muscle at slaughter

A

lower pH in the first hour of a carcass that was stimulated shows that glycogen is being depleted to prevent cold shortening

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What is proteolysis

A

process of breaking proteins into peptides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

When is the aging time for meat?

A

between the slaughter and the meat consumption

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Where does aging typically occur?

A

under refrigeration at 4C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Is aging of meat good?

A

yes, it is necessary to improve meat tenderness

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

How does aging cause better tenderness?

A

caused by proteolysis -> breakdown of proteins into smaller constituents comprised of polypeptides or AA
as meat ages, structural changes occur in myofibril, one of the changes is the breakage or structural damage near the Z-line band in the sarcomere are targeted by enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What causes proteolysis in aging of meat?

A

proteases (enzymes) that are naturally present in muscle
- have access to structural proteins in the sarcomere

24
Q

Where are proteases for proteolysis found?

A

localized within the skeletal muscle

25
Q

What are the two main types of protease enzymes involved in meat tenderization?

A

calpain/calpstatin system
proteasome and caspase system

26
Q

What does calpain break down?

A

titin and desmin proteins in muscle fibre

27
Q

What do calpains require for activity?

A

calcium

28
Q

What are the two types of calpains?

A

u-calpain
m-calpain

29
Q

How many Ca ions do the two calpains bind to?

A

u-calpain - binds to 5-8 Ca2+ ions
m-calpain - binds to 11-20 Ca2+ ions

30
Q

What percentage of calpain is reduced at pH 5.5-5.8 and 4C?

A

activity is reduced to 28%

31
Q

What are the two types of calpain enzymes inhibited by?

A

enzyme known as calpastatin - breaks down calpains and therefore decreases tenderness - inhibits calpains

32
Q

Do calpains work on muscle when the animal is alive?

A

yes, however this will have no effect on the muscle because the animal can repair the damage done while it is still alive

33
Q

What does calpastatin require for its activity?

A

calcium

34
Q

How does calpastatin inhibit calpains?

A

preventing the calpain proteolytic activation, when calpastatin binds to calpain, it causes conformational changes in the calpains blocking its active sites

35
Q

Explain the meat aging graph showing instrumental measurement of meat tenderness

A

instrumental measurement goes down as we age the carcass - because there is less resistance of the meat as time goes on due to action of enzymes

36
Q

Explain the meat aging graph showing measurement of the intensity of myofibrillar protein breakdown

A

intensity of myofibrillar protein breakdown measures integrity of sarcomere - goes up because more breakdown of myofibrillar protein overtime due to calpain

37
Q

Why is fresh meat colour important?

A
  • to an average consumer - meat colour is the first sensory experience of the product
  • variations from the expected colour cause reduced sales at the retail counter
  • colour is the primary quality traits evaluated by a final consumer upon purchase
38
Q

What are the two ways of measuring meat colour?

A

subjectively evaluated by meat graders
instrumentally measured

39
Q

What are the letters for instrumental measuring of meat colour?

A

L = lightness
a = redness
b = yellowness

40
Q

What makes beef red meat and pork white meat?

A

muscle fibre type change the redness
oxidative metabolism - requires oxygen needs myoglobin therefore more red
glycolytic fibres don’t require as much myoglobin therefore not red
more myoglobin - more oxidation therefore darker colours

41
Q

Why can fat be yellow?

A

fat can store compounds that have a yellow tinge from grains and grass that give colour

42
Q

What is variation in meat colour influenced by?

A

pigment protein myoglobin

43
Q

What is myoglobin?

A

metalloprotein (contains a metal ion cofactor)
its function in the muscle is to serve as an oxygen storage molecule oxidative metabolism

44
Q

What is the myoglobin content in the different muscles?

A

oxidative muscles: high myoglobin content
glycolytic muscles: low myoglobin content

45
Q

How does myoglobin content vary depending on animals age?

A

muscle from older animals contains greater myoglobin concentration than young animals

46
Q

How can myoglobin be affected by pH postmortem?

A

changes in myoglobin solubility also affects its concentration
high temperature and low pH that causes denaturation of myofibrillar proteins also cause denaturation of myoglobin - it decreases the redness of meat

47
Q

What is deoxymyoglobin?

A

meat is a dark purple colour
myoglobin is exposed to low oxygen environment
(vacuum packaged meat)
lack of oxygen means that iron is not bound to gas

48
Q

What is the state of iron in deoxymyoglobin and oxymyoglobin?

A

Fe2+

49
Q

What happens if deoxymyoglobin meat comes into oxygenated environment?

A

oxymyoglobin (“normal meat”)

50
Q

What is oxymyoglobin meat?

A
  • bright red colour of beef and pork
  • when myoglobin is exposed to oxygen
  • when iron is in ferrous state Fe2+, the molecule has a high affinity for oxygen
  • observed in traditional retail meat packages with oxygen permeable wraps
51
Q

What is the iron state of metmyoglobin?

A

Fe3+

52
Q

What causes metmyoglobin?

A

oxidation of the heme iron results in a transition from the ferrous iron Fe2+ to ferric iron Fe3+
Fe3+ does not have high affinity for oxygen
the oxidized pigment caused by Fe3+ is a gray or gray/greenish brown colour to the meat
if the meat is exposed to oxygen for long enough this occurs - not spoiled just oxidized

53
Q

How can myoglobin transition between the various forms?

A

deoxymyoglobin -> oxymyoglobin through addition of oxygen

oxymyoglobin -> deoxymyoglobin
through removal of oxygen

oxymyoglobin -> metmyoglobin
through electron loss (oxidation)

metmyoglobin -> oxymyoglobin
through e- gain (reduction)

metmyoglobin -> deoxymyoglobin
through e- gain (reduction)

deoxymyoglobin -> metmyoglobin
through e- loss (oxidation)

54
Q

What is metmyoglobin caused by?

A

catalyzed by high temp
occurs when meat is exposed to oxygen for long time

55
Q

Why can metmyoglobin be bad?

A

negatively impacts the retail sales of meat as consumers will associate it with poor handling