DEFINITION AND PROPERTIES OF

MEAT
Curriculum of Food Hygiene lectures
Part Number of Topics
hours
General Food 4 Introduction, basic terms, foodborne
Hygiene hazards and diseases
(40 hours) 12 Food microbiology: fundamentals, main
pathogens
8 Chemical-toxicological food safety
4 Spoilage, preservation and other
treatments of foods
4 Fundamentals of food hygiene regulation
4 General hygiene rules, food safety
assurance system (HACCP)
4 Food hygienic significance of zoonoses
Curriculum of Food Hygiene lectures
Part Number of Topics
hours
Milk Hygiene 12 Hygiene of milk production: milking,
(20 hours) handling of raw milk at the farm,
microbiology raw milk, milk hygienic
importance of mastitis and zoonoses,
chemical contamination of milk
8 Technological hygiene of milk product’s
manufacture: heat treated drinking milk,
fermented milk products, butter, cheese,
milk powder
Curriculum of Food Hygiene lectures
Part Number of Topics
hours
Meat hygiene, 8 Meat ageing, basics of meat inspection
meat inspection,
8 Slaughter and meat inspection of swine
hygiene of other
and ruminants
products of animal
origin and foods 4 Slaughter and meat inspection of poultry
of plant origin and rabbit
(40 hours) 4 Meat inspection of game, hygiene and
official control of fishery products and live
bivalve molluscs
4 Hygiene of meat products, egg production,
egg products and foods of plant origin
12 Diagnosis and decisions in meat
inspection: organoleptic changes,
septicaemia, specific diseases
Curriculum of Food Hygiene lectures
Part Number of Topics
hours
Food hygiene 4 Official control of food: legal regulation,
administration organisation, risk-based approach
(20 hours) 16 Official food hygiene control activities:
food processing, distribution, retail,
international trade, catering, small-scale
operations
⚫ Semester 10 (valid from 2020)
▪ Duration of semester two weeks shorter
▪ Extra two weeks for exam preparation
▪ Lectures on Friday 3 hours (mostly)
▪ Two midterm tests
 Assessment
⚫ Forms of assessment
▪ written exam: semester 10
▪ written exam: semester 11 (after the extramural practices)
⚫ Requirements of the subject, exams, order of exams
❖ „visiting the lectures” and „active participation” in the practicals
obligatory
❖ condition of signature: „participation” in the lectures and practicals,
minimum 60% result of both midterm tests
❖ maximum number of missed practicals: 4 (2 must be supplemented)
❖ final exam (Semester 10)
 Exam information
⚫ Final exam: written test exam
⚫ Contents: subject matter of both lectures and practicals of semester 9 and 10
⚫ Way of performance:
- electronic test exam through the Neptun Unipoll system
- 30 multiple choice questions from the theoretical curriculum (textbook +
lectures) and 10 multiple choice questions from the practical material (practical
notes I-II)
- duration: 30 minutes
⚫ Evaluation:
- <65% = 1, unsatisfactory, 65-73% = 2, passing, 74-82% = 3, satisfactory, 83-91%
= 4, good, 92-100% = 5, excellent
⚫ Retake: minimum 3 days after the failed exam
 Example questions
Choose the correct statements:
A. Salmonellae are thermophilic bacteria that cannot grow below 20
°C.
B. The minimum temperature at which salmonellae can still grow is 6
°C.
C. Salmonellae produce enterotoxins in the food that cause vomiting
and diarrhoea in humans.
D. Water activity lower than 0.97 inhibits the growth of salmonellae.
E. Eggs may become infected with salmonellae usually through the
pores of the eggshell.
F. Salmonellae release a heat-labile enterotoxin and a cytotoxic protein
in the intestines of the consumers that cause diarrhoea.
Answers: B, E, F
 Example questions
Choose the incorrect statements
A. Salmonellae are mesophilic bacteria.
B. Salmonellae are psychrophilic bacteria that can even grow at
refrigerator temperature.
C. Under food production conditions, a heat treatment of 70 °C core
temperature for at least one minute is needed to render foodstuffs free
from salmonellae.
D. To destroy salmonellae in meat products a heat treatment of 90 °C for
at least 10 minutes is needed.
E. All serotypes of salmonellae causing typhus in animals are capable of
inducing disease in humans.
F. Salmonella Enteritidis is the most common serotype causing disease
in humans.
Answers: B, D, E
 Example questions
Which food cannot be contaminated during the primary production?

A) Raw milk
B) Sausage
C) Vegetable
D) Honey

Answer: B
 Definition of meat
 General definition
 striated skeletal muscle of animals for slaughter, together with
the fat, connective tissue, lymph nodes, nerves and blood vessels
 Food law:
 edible parts of the body of bred and game animals which
serve for human nutrition, the meat products made from it and
the foods that are typically prepared by the use of meat
 Edible parts: the tongue, liver, heart, lungs, spleen, stomach (in
ruminants the parts of the compound stomach without the
abomasum), brain and kidneys, some slaughter by-products (e.g.
rind of bacon, poultry skin, blood for consumption, the non-
lactating udder)
 Ageing of meat
 Immediately after the slaughtering of animals, the
sensory and physical properties of their muscle tissue
greatly differ from those of what will be consumed
later as meat
 The process during which meat assumes the favourable
properties characterising it (colour, odour, tenderness,
etc.) is called the ageing (or maturation) of meat
 Ageing of meat
 Direct source of energy necessary for muscle function is
ATP, which is supplied by the body primarily through the
degradation of carbohydrates, first of all glucose
 Under aerobic conditions
 the oxidation of one glucose molecule will lead to the
generation of 36 ATP molecules via a complex reaction series
consisting of three closely interrelated reactions (glycolysis,
oxidative decarboxylation and oxidative phosphorylation)
 Under anaerobic conditions
only the first step of the reaction series takes place, and the
resulting pyruvate is reduced to lactic acid by the lactate
dehydrogenase enzyme
 in the living organism this occurs only in the case of strenuous
physical exercise
 Glycogen corresponding to one glucose molecule will be
converted into two molecules of lactic acid :

 (C6H10O5)n + n H2O → 2n C3H6O3

glycogen lactic acid

 This type of energy generation cannot be maintained for a

very long time, as the accumulating lactic acid markedly
decreases the pH of blood as well
 Concentration of ATP is relatively low in the muscle tissue (5–7
mmol/kg). The ATP used up is regenerated from creatine
phosphate (CP) and ADP through the action of the enzyme
creatine kinase (CK) while creatine (C) is formed:

CP + ADP ↔ C + ATP
 Biochemistry of meat ageing

 Biochemical procedures continue to go on for some time under

altered conditions
 Blood circulation and consequently the oxygen supply of muscle
tissue cease, resulting in the rapid decrease of the redox
potential and the development of anaerobic conditions
 Two biochemical processes take place in the muscle tissue:
 pH reduction occurring as a result of anaerobic glycolysis
 rigor mortis (stiffness of death) developing because of the lack of ATP
 Stages
 pre-rigor stage lasting until stiffness of death (rigor mortis) sets in,
which is biochemically characterised by the dominance of anaerobic
processes, the decreasing ATP and creatine phosphate content as well as
the declining pH of the muscle tissue,
 rigor mortis and the subsequent post-rigor state, during which the final
pH of the meat is reached and, primarily through the degradation of
certain proteins, the sensory properties typical of aged meat develop.
 Onset of rigor mortis and reduction of
pH
 As a consequence of oxygen deficiency, oxidative decarboxylation and
phosphorylation cease and thus ATP can be generated via anaerobic
glycolysis, through the degradation of glycogen
 The quantity of ATP is only a small fraction of that produced via the
aerobic pathway + decreased further by the continuous operation of the
sarcoplasmic ATPase enzyme
 If there is still enough creatine phosphate in the muscle tissue after
slaughter, the regeneration of ADP into ATP still remains possible for some
time
 Within a short time ATP level starts to decrease
 Rate of pH decline increases as the ATP degradation products (ADP,
AMP) have a regulatory effect on the rate of glycolysis
 Binding of actin and myosin becomes irreversible, as the lack of ATP
makes it impossible for actomyosin to dissociate, and thus rigor mortis sets
in
 pH
 pH of muscle tissue decreases from its physiological value of around 7.2 to
the generally typical value of around 5.5
 pH reduction
 within 4–8 hours in pigs

 12–24 hours in sheep

 18–36 hours in cattle

 10-15 min in poultry

◼ higher glycogen content and more intensive glycolytic activity of white

muscles, pH reduction is faster in the white muscles
◼ the final pH-value is often higher in the white muscles (pH 5.8)
 pH
 Proteins are denatured and their water-holding (water-binding) capacity
decreases
 Amount of water bound by the muscle fibres decreases, water leaks into the
interfibrillar space and then, through the channels of the perimysium, onto
the surface, resulting in drip loss
 Due to the altered light absorption property of proteins and the decreased
water content of fibres, the colour of meat becomes paler and more
opalescent
 Processes are the most pronounced near the isoelectric point of the
contractile proteins
 Rigor mortis
 Sets in when the quantity of ATP decreases below the level
necessary for eliciting muscle fibre relaxation (≈5 mmol/kg)
 Time of onset of rigor mortis is influenced by the quantity of
glycogen and creatine phosphate in the muscle at the time of
slaughter and the rate of their metabolism after slaughter
 Sets in sooner in animals that had lower amounts of glycogen
at the time of slaughter because of pre-slaughter stress or
heavy muscular exertion
 Rapid cooling of the carcase delays the onset of rigor mortis
 Onset of rigor mortis is exclusively dependent on the quantity
of ATP and is not influenced by the change of pH-value
 Rigor mortis sets in also if the pH reduction is limited; moreover,
in this case the onset of rigor mortis is even faster
 Time of onset of rigor mortis: between 4 hours and 24 hours
 Resolution of rigor mortis

 After a certain period of time the meat becomes increasingly soft and
tender
 Primarily catalysed by proteolytic enzymes
 Some enzymes are active at an acidic pH (cathepsins)
 Stronger proteolytic activity at neutral pH and need calcium for their
activity (calpains)
 Calpains: mammalian and poultry meat
 Cathepsins: fish and meat stored at higher temperatures
 Cathepsins can be found in the lysosomes of the sarcoplasm, and their
pH optimum is 5.5; they mainly catalyse the degradation of sarcoplasmic
proteins and hardly affect the myosin-actin complex or the connective
tissue proteins
 Calpains are activated by calcium ions, which release these enzymes
from their binding to calpastatin; they mainly result in the disintegration
of the Z-lines and catalyse the degradation of connective tissue proteins
 Time requirement for achieving 80 %
tenderness
During ageing, meat reaches the desired level of tenderness within a time varying by
animal species; thus, the recommended time of ageing before use (cooking, frying) – which
also includes the time needed for wholesale and retail distribution

In frozen condition the ageing of meat stop but they are resumed after thawing if the
freezing of meat interrupted the ageing process.

Species 80 % tenderness Recommended duration of

ageing
Swine 4 4-7
Lamb 7 7-10
Cattle 10 10-14
poultry 0.3 <1
 Abnormal meat ageing processes

 One of the fundamental biochemical processes involved in the ageing of

meat is the pH reduction of muscle tissue

 Adequate pH reduction is important primarily for ensuring good meat

quality but sometimes also for guaranteeing the safety of meat

 pH reduction markedly deviating from that typical of the given animal

species may result in meat quality defects or faster spoilage. Abnormal
pH reduction may occur in the form of a faster-than-average pH
decrease (PSE-type ageing) or as a less-than-average drop of pH
(DFD-type ageing)
 PSE meat

 In pigs, but occasionally also in chickens and turkeys

 Pale, soft and exudative (PSE)
 Most often in the valuable meat parts such as the loin (m. longissimus
dorsi), round of beef (m. semitendinosus, m. semimembranosus, m.
gluteus medius) and pectoral muscles (mm. pectorales)
 Meat loses its water-holding and water-binding capacity, gives off
juice, and shows a high cooking loss and poor emulsion-forming
properties. As a result of salting, the colour and taste of PSE meat may
change
 Most of the glycogen is degraded within 45 minutes, and thus the
muscle has high lactic acid content and consequently a low pH-value
(≤5.8–6.0)
 Simultaneously, the temperature of the muscle tissue temporarily rises
and is higher than normal, together with the rapid pH decrease, leads
to the more intense denaturation and lower water-holding capacity of
proteins
 PSE meat

 From the muscle fibres, a large volume of water gets into the
interfibrillar space and from there onto the surface of meat
 Meat gives off plenty of juice, assumes an exudative, mushy texture and,
due to the shrinkage of fibres, a paler colour
 Final pH of the meat is also slightly lower than the average which also
decreases the water-holding and water-binding capacity of meat (5.2-
5.3)
 Limits the usability of the meat for the manufacture of certain meat
products, e.g. raw-cooked sausages, cold cuts or canned products
 PSE meat is less suitable for use as carcase meat either, and can mostly
be recommended for industrial processing (high drip loss)
 Pig breeds (e.g. the Hampshire) can accumulate and degrade a higher
quantity of glycogen in their muscles than other breeds, which results in
a greater-than-average pH reduction
PSE meat
 DFD meat

 Meat ageing of DFD (dark, firm, dry) type may occur in any animal species
 Low amounts of glycogen in the muscle, resulting in a limited pH reduction
 DFD meat is usually due to physical exertion and the lack of rest before slaughter,
but occasionally a chronic disease may also result in a decrease of muscle
glycogen content during the animal’s life
 DFD meat is dark, of firm texture, does not give off juice and is sticky to the
touch
 Final pH is generally well above 6.0
 More prone to spoilage and its shelf-life is shorter
 the higher pH, which is closer to the neutral range, generally favours the growth of
bacteria,
 because of the ante-mortem decrease in the amount of glycogen, the carbohydrate
content of the muscle tissue is very low, which does not favour the lactic acid bacteria
but enables the growth of proteolytic Gram-negative bacteria (e.g. pseudomonads),
resulting in surface sliminess and unpleasant odour of the meat
 Recommended for industrial processing
 water-binding capacity is good
 during the curing process the desired colour and the desired taste develops more slowly
and to a lesser extent
 The properties of meat

 Sensory properties
 The external appearance of meat is determined by the quality of
muscle fibres, the properties (quantity, colour and distribution) of
adipose and connective tissue, and the myoglobin and glycogen content
 Fresh meat
 reddish colour, unique odour, a glassy shine, is compact and inelastic to the
touch and is infiltrated with more or less connective tissue and fat
◼ influenced by the species, breed, age, sex, body region, nutrition and
preparation for slaughter, etc.
 Aged meat
 the normal reddish colour typical of fresh meat, also bright red or a paler
brownish
 stronger odour emanating the odour of lactic acid
 lustreless, soft and sometimes pasty to the touch, occasionally fragile, and
gives off a small volume of juice only
 The colour of meat

 Colour has an outstanding importance in consumers’

expectation related to the quality of meat
 Depends on the concentration and chemical status of
pigments
 Myoglobin contained by the muscle tissue
 pH
 Physical characteristics related to the colloid-chemical
structure of meat
 Characteristics of meat colour include:
 colour shade determined by myoglobin and its derivatives,
 saturation associated with the concentration of these pigments,
 lightness (paleness) influenced by the physical characteristics
associated with the colloid-chemical structure
 The colour shade of meat

 The concentration of myoglobin depends on the breed, the muscle type and the
age.
 horse meat: 7–8 mg/g
 beef: 4 mg/g
 Pork: 1–1.5 mg/g muscle tissue
 concentration increases with age: the myoglobin content of forerib is 1–2 mg/g in
calves and 4–8 mg/g in cows.
 Myoglobin (Mb) is a purplish-red pigment which occurs only at very low O2
concentrations, inside the meat.
 At higher oxygen pressure, oxygenation of this molecule leads to the formation of
a bright red oxymyoglobin (MbO2).
 At lower oxygen tension, the bivalent iron of myoglobin is oxidised into a trivalent
iron, and a pale brown metmyoglobin (MetMb) is formed
 Metmyoglobin formation is the most pronounced at an oxygen tension of 5.3 hPa
(4 mmHg); at a lower oxygen tension the proportion of myoglobin while at a
higher oxygen tension the proportion of oxymyoglobin increases
 Reactions among the three myoglobin derivatives are reversible, and these give
the meat its normal, acceptable colour shades.
 The colour shade of meat
 Fresh cut surface of meat : purplish-red (Mb) and then turns into bright
red because of the formation of MbO2
 Depending on the diffusion of oxygen, this bright red layer gradually
becomes thicker (2–6 mm)
 This phenomenon, which takes about 15–60 minutes, is called ‘blooming’
 Beneath the bright red layer a thin, brownish line appears, indicating the
MetMb formed by the oxidation of myoglobin. In round of beef (m.
semitendinosus) stored at a temperature between 0 and 7 °C, this occurs
approximately 6–7 mm beneath the surface)
 Over time, the MbO2 layer becomes thinner and usually after 2–3 days
the MbO2 present on the surface of meat is also gradually oxidised into
MetMb, which gives the meat a pale brownish colour
 The ability of meat to keep its attractive bright red colour for the longest
time possible during storage is called colour stability
The colour shade of meat
 MYOGLOBIN (deoximyoglobin): purplish
 Colour of meat when myoglobin is in its native state, or
immediately after cutting and before blooming
 purple is the color of meat in the middle of a steak (when
you cut across a raw, fresh steak that’s red on the surface, it
should be purple in the middle. If you let the steak sit for a
bit exposed to air, that color will change, or bloom, to
cherry red)
 In the presence of oxygen fresh meat blooms and turns
its characteristic red colour: OXYMYOGLOBIN
 After prolonged exposure to oxygen: METMYOGLOBIN,
which appears brown
Colour shade of meat
 Colour stability
 Depends on
 the temperature of storage (the lower the temperature, the more stable the colour)
 the pH (at a higher pH the colour is more stable because of the higher activity of the
enzyme reducing MetMb),
 on drying
 the presence of metal traces and the lipid oxidation.
 Can be increased by
 the use of vacuum packaging and modified atmosphere packaging procedures
 supplementing the diet of animals for slaughter with antioxidants (e.g. with vitamin E)

 Retained haemoglobin also influences the colour of meat

 notable only after imperfect bleeding
 Quantity of adipose and connective tissues and their distribution within the muscle
tissue
 decrease the intensity and increase the lightness of meat colour
 Lightness

 Associated with the light-reflecting and light-absorbing capacity

 Changes occurring in the colloid-chemical structure of meat
 The still ‘slaughter-warm’ meat closely resembling the muscle of live
animals and the DFD meat showing only a low degree of acidification
absorb the majority of light and, thus, are of darker colour
 The meat undergoing a normal degree of acidification and even more so
the PSE meat undergoing rapid acidification at a temperature above 40
°C, and consequently containing plenty of denatured sarcoplasmic
protein and occasionally also denatured myofibrillar proteins, reflect
more light
 precipitated sarcoplasm adheres to the surface of the myofibrils and
increases the light-reflecting capacity of the sarcoplasm/myofibril interface.
 water migrates from the myofibrils into the interfibrillar space, the myofibrils
shrink and their light absorption decreases.
◼ meat appears pale
The physical properties of meat
 Water-binding capacity
 Ability of meat to bind and immobilise its own water content as well as any extraneous water
added to it.
 Sensory (drip loss) and the technological (weight loss, texture and taste defects) aspects
 Striated muscles of animals for slaughter contain approximately 75% water.
 This water content can be increased further by adding extraneous water to the minced muscle
tissue.
 85–95% of water : intracellularly
 3–5% of this tissue water adheres closely to the surface of proteins (hydrate water),
 Free water : bound more or less strongly to the protein structure and is limited in its movement
(immobilised)
 This water is located mostly within the filaments constituting the myofibrils and in the
interfilamental space.
 Decrease of water-holding capacity is due to the shrinkage of the interfilamental space, as a
result of which a part of the water is expelled from it.
 rigor mortis
 the reduction of pH: alteration of the charge of myofibrillar proteins and their denaturation
 Water-holding capacity
 Lowest near their isoelectric point
 During the normal meat ageing process the pH decreases to a value near the
isoelectric point, and thus a minor drip loss can always occur.
 This drip loss is, however, much more intense during PSE-type meat ageing
because of the lower pH and the denaturation of proteins.
 Water-binding capacity can be increased by
 the addition of inorganic salts (e.g. NaCl, polyphosphates),
 pH-raising substances (e.g. sodium hydrogen carbonate, lactates)
 proteolytic enzymes
 As a result of heat treatment, the water-binding capacity can decrease markedly
because of the denaturation of proteins
 Rapid cooling after slaughter slows the processes leading to the onset of rigor
mortis in the muscle, and thus the decrease of the water-binding capacity will also
be slower
 Mincing of meat also increases the water-binding capacity (to a certain extent),
which is attributable to the loosening of the original protein structure
 Tenderness

 Meat is easy to crush or break up even with a few chewing movements

 Desired or expected degree of tenderness, an ageing time of a length varying by
animal species is required (this ranges from ≤1 day for poultry meat to 10–14
days recommended for beef)
 Vary also by muscle type, as they are influenced by the size of muscle fibres and
the connective and fat content of the muscles
 Muscles composed of thinner, 30–40 μm thick fibres (e.g. m. psoas maior) give a
softer and more tender meat, while those constituted by thicker fibres 50–60 μm in
diameter will yield a harder and tougher meat
 Within the muscle tissue, fat can be found partly in the connective tissue between
the muscle bundles (this gives the meat its marbled appearance) and partly within
the muscle fibres. This latter fat makes the meat softer and more tender (e.g. the
meat of milk-fed young animals)
 Softness of meat is markedly influenced by the quality and quantity of the
connective tissue. A higher amount of connective tissue (thick fibrous septa
between the muscle bundles) or the presence of a connective tissue containing much
collagen and little elastin will result in a harder, tougher meat
 Texture

 Texture is a physical characteristic of meat expressing

that it can be compressed by shear forces and its
volume decreases
 This shear force is always higher in the case of fresh
meat than aged meat
 This property and its degree are primarily related to
the structure of muscle proteins
 Texture can be measured instrumentally by shear tests,
e.g. using a Warner-Bratzler shear force measurement
device
 Chemical properties of meat

 Meat is constituted primarily by muscle tissue but it contains connective tissue, fat,
blood vessels, blood and nerves as well
 The biological value of proteins is determined by the essential amino acids
contained by them and their relative proportions. The biological value basically
expresses the ability of the given protein to maintain nitrogen balance; the lower
quantity is needed for this, the higher the biological value.
 Beef: 88-92
 Pork: 84
 Poultry: 82
 Fish: 80-92
 Egg: 100
 Meat is an important source of vitamin B, and offal (mainly the liver) contain
substantial amounts of vitamin A as well.
 The carbohydrate content of meat is low,
 Other organic compounds occurring in meat in low amounts are important in
giving the meat its characteristic taste and aroma
 Chemical composition
component %
Water 75.5
Muscle protein 16
Myofibrillar protein 10
Sarcoplasmic protein 6
Connective tissue protein 2
Fat 3.1
Non protein nitrogen containing compounds 1.6

carbohydrates 0.7
minerals 1
Trace elements 0.1