In the second of a series of four articles

Chemistry in the Peter Bayliss examines the meat quality

aspect of texture. A background to the
kitchen: the chemistry general structure and the rigor process is
of flesh foods II provided in “Chemistry in the kitchen:
the chemistry of flesh foods I” (NFS,
No. 1, January/February 1995).
Consumer surveys reveal that meat texture
Peter Bayliss (i.e. the degree of toughness or tenderness) is
the most important eating quality attributed
to meat. Texture is therefore ranked by con-
sumers above the other two most desirable
characteristics, which are colour and flavour.
This article examines the major factors which
influence meat texture: pre-slaughter, post-
slaughter, and processing factors.

The author
Peter Bayliss is Senior Lecturer in Food Science and
Technology at Manchester Metropolitan University,
Manchester, UK.
Abstract
The meat quality attribute of texture is ranked as the most
important by consumers. Details the mechanism of the
major causes of meat toughness. Examines pre-slaughter,
post-slaughter and processing factors that influence the
texture of meat.
Pre-slaughter factors
Age of the meat animal
Traditionally, meat traders have held the
erroneous belief that meat from older animals
was tough because they had exercised more
than their younger counterparts and therefore
would have developed more connective tissue.
A more appropriate explanation is provided
by the development of “mature cross links”
between adjacent collagen fibres in connective
tissue. These mature cross links are heat
stable and are not easily broken down during
heat processing. Hence, when meat is cooked,
the collagen fibres do not hydrolyse into liquid
gelatine but remain within the meat causing
toughness. This increase in texture is referred
to as “background toughness”, and the actual
chemical nature of the mature cross link has
not yet been characterized.
This explanation is illustrated by quantifi-
cation of collagen, the principal component of
connective tissue. Veal (meat from young
cattle, about 12 weeks of age) has a greater
proportion of collagen compared with beef
from an 18-month old bullock, and yet veal is
never tough, whereas beef often can be.
Moreover, pork has a greater amount of
connective tissue than all the other meat
species but is usually tender. This gives rise to
the expression that it is the “quality of the
collagen and not the quantity” that is respon-
sible for the toughness of meat.

Variability in the connective tissue

content of muscles
Each muscle in an animal’s body has a partic-
Nutrition & Food Science
Number 2 · March/April 1995 · pp. 21–26 ular physiological function (i.e. locomotion,
© MCB University Press · ISSN 0034-6659 support, etc.) and differs in the amount of
21
 The chemistry of flesh foods II Nutrition & Food Science
Peter Bayliss Number 2 · March/April 1995 · 21–26

connective tissue it contains. This gives rise to Figure 1 Myofibrillar filament lattice illustrating
varying texture profiles for differing muscles. sarcomere
The amino acid hydroxyproline is unique
I band A band I band
to collagen and it can be ascertained from
Z-line Z-line
Table I that collagen is abundant in shin beef, Myosin
making it tough (low-grade meat, normally
Actin
moistly cooked). In comparison, tender fillet
steak (high-grade meat, normally cooked by
grilling) has a low collagen content.
Sarcomere
The silverside joint of beef (M. semitendi-
nosus) is comparatively tough, and tradition-
ally slow roasted or pickled. This muscle is
Figure 2 Influence of sarcomere length on toughness
unique in that up to 37 per cent of its connec-
tive tissue is made up of the other connective 160
tissue protein elastin that does not hydrolyse
140 Maximum
on cooking.

Shear force (arbitrary units)

toughness
120
Husbandry and breed
100
Meat from rapidly grown animals tends to be
comparatively tender. Late-maturing breeds 80

of cattle (e.g. large continental beef breeds 60

such as Charollais) that are fed on high
protein diets are slaughtered at an earlier age,
hence they have muscles with fewer mature
cross links. In addition, the larger muscles
provide a high muscle-fibre volume to a low
endomysium surface area ratio (hence less
connective tissue).
Post-slaughtered factors
Sarcomere length
As illustrated in Figure 1, the length of the
sarcomere is the measurement between adja-
cent z-lines. At the end of rigor, the “resting
length” of the sarcomere is 2.1µm. Reduction
of this length causes meat to become tough.
Although not well understood, the increase
in toughness associated with shortened
muscle fibres is thought to be due to the
connective tissue sheath that surrounds the
myofibril, the endomysium, which becomes
more relaxed. On chewing there is an
increased amount of endomysium to shear
(due to bunching and thickening) providing
the sensation of increased toughness.
Sarcomeres shorten as a result of “cold
toughening” or being unrestrained during
rigor mortis , or a combination of both. It can
be seen from Figure 2 that when the sarco-
Table I Connective tissue content of two retail cuts of beef
Collagen
Cut of meat Muscle (hydroxyproline mg/g)
Fillet steak Psoas major
Hind shin Superficial
digital flexor
40
20
0 10 20 30 40 50 60 70
Percentage shortening
mere reaches 40 per cent of its resting length,
meat toughness reaches a maximum. A pos-
sible explanation for this phenomenon is that
the majority of myosin heads will be attached
to the actin filaments. Increases and decreases
of sarcomere length either side of 40 per cent
result in less myosin cross bridge attachment
and ensuing tenderness.
Cold toughening
Low temperatures during rigor mortis cause
the sarcomere to shorten and produce tough
meat. This is known as cold toughening (or
cold shortening) and is predisposed by chill-
ing the carcass after slaughter too early or too
quickly. More precisely, if the carcass is
chilled to below 10°C within ten hours of
slaughter while ATP is still present in the
muscle fibres, the sarcomeres will excessively
shorten (see Figure 3).
Sheep meat (particularly loin chops) is
most commonly cold toughened owing to the
comparatively small carcass mass that cools
quickly, while in beef it tends to occur in
superficial muscles, especially the Longissimus
dorsi muscle of the sirloin. Cold toughening is
not common in pigs and poultry (except
turkeys) owing to the rapid post mortem gly-
colytic rate of their muscle.
350 Although the actual physiology of cold
toughening is not well understood, it is
1,430 generally accepted that it is a result of low
22
 The chemistry of flesh foods II
Peter Bayliss
Figure 3 Shortening of muscle at various temperatures
during rigor
50
Cold toughening
40
Percentage shortening
Hot toughening
30
20
10
0 10 20
Temperature ˚C
temperatures rendering Ca++ pumps ineffec-
tive, that in turn trigger sarcomere shortening.
A method of overcoming cold toughening
is by electrically stimulating the carcass. An
electric current is passed through the animal’s
carcass after it has been humanely slaughtered
and prior to the commencement of rigor to
use up ATP. The carcass then enters into rigor
mortis more quickly and rapid chilling
regimes will not produce toughened meat.
Carcass hanging method
If muscles are physically prevented from
shortening during rigor, the meat will be more
tender. Some muscles are prevented from
shortening by being firmly attached by their
insertion ligaments on to bones, e.g. fillet
steak (psoas muscle).
Normally, carcasses are suspended by a
hook passed through the Achilles tendon at
the distal part of the hind limb (see Figure 4).
In this position muscles located on the dorsal
aspects are not held taut and are free to short-
en during rigor. These muscles include
groups within the expensive retail cut of
“topside of beef ”.
Figure 4 Normal method of carcass suspension
Carcass
suspended
from Achilles
tendon
Muscle
relaxation
Nutrition & Food Science
Number 2 · March/April 1995 · 21–26
The UK meat industry has been slow to take
up posture hanging of the carcass, but many
of the major multiples are now including it
(along with electrical stimulation) in their raw
material specifications.
One method developed in the USA (Ten-
derstretch) suspends the carcass from the
pelvic bone, allowing the hind limb to bend
into a standing position (see Figure 5). This
has the effect of stretching the muscles catego-
rized in the topside, silverside and down
through part of the sirloin. This hanging
30 40 50 method does not affect the muscles of the fore
quarter. It also allows the psoas muscle to
relax so that the fillet steak can, on occasions,
be slightly tougher than normal.
New Zealand researchers found that if the
carcass was suspended from the pelvic bone
and the front and hind legs were attached so
that the carcass was in a more “natural stand-
ing position”, a net increase in tenderization
in both hind and forequarter joints of meat
occurred.
Ultimate post mortem acidity levels
The ultimate pH (pHu) of the carcass affects
the water-holding capacity (WHC) of the
meat. Muscle consists of about 85 per cent
water that is held in the myofibril surrounding
the thick and thin filaments. Losses or gains in
water results in the myofibrils shrinking and
swelling. Generally, meat with a high WHC
will have less muscle fibre per unit area and
therefore when chewed will be perceived as
being more tender by the consumer (and
more “juicy”). This is illustrated in Figure 6
where tenderness decreases until pH 6.0 and
then increases again as the pH rises and falls.
The pH of meat
The isoelectric point of the myofibrillar pro-
teins is pH c. 5.0. This is when the myofibril-
lar proteins will have a net zero charge.
Figure 5 Methods of carcass posture hanging
USA
method
Muscle
tension
New Zealand
method
= Direction of
muscle tension
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 The chemistry of flesh foods II Nutrition & Food Science
Peter Bayliss Number 2 · March/April 1995 · 21–26

Figure 6 Relationship between tenderness and pHu cally, that little degradation of the connective
tissue proteins occur, while in the myofibril
6 there are gaps at the I-Z junctions and frac-
ture sites around the Z-lines (see Figure 7).
Mean tenderness score

From Figure 8 it can be ascertained that

5 conditioning has three phases, consisting of A
4 tender (position A). However, if meat is
3
5.4 5.6 5.8 6.0 6.2
pH
Increases or decreases in pH either side of
this value cause an increase in the meat’s
WHC. Food animals with a low level of glyco-
gen at the time of slaughter will produce
meat that has a high pH and will have an
increased WHC. Moreover, meat with a high
water-holding capacity loses little exudate or
“drip”.
Influences affecting the water-holding capacity
of meat
The drop in pH accompanying rigor results in
the filament lattice shrinking in a transverse
direction as the isoelectric point of myosin is
approached at pH 5.0. At this value, negative
or positive charges on the thin and thick
filaments are at a minimum. This shrinkage
has the effect of putting pressure on the sar-
coplasm and if the muscle fibres are cut the
fluid is forced out under pressure as drip at
the cut surface.
High pH conditions result in an increased
donation of negative ions to the filament
lattice, producing increased electrostatic
repulsion and swelling of the filament lattice
in a transverse direction so that the compart-
ment in which water is held is increased.
The manufacturers of meat products take
advantage of this effect by using polyphos-
phate in their products. Polyphosphate has a
pH c. 9.0 and is often added to produce alka-
line conditions to facilitate increased take-up
of water, while in Germany some manufactur-
ers now use pre-rigor meat that is high in pH.
pre-rigor, B rigor and C post-rigor. Prior to
rigor commencing, meat is comparatively
cooked prior to attainment of the ultimate
pH, toughening occurs owing to “hot short-
6.4 6.6 ening”. Toughness increases as rigor ensues
until it peaks at C, when the myosin heads
have formed permanent cross bridges. During
the time indicated by B there is a gradual
increase in tenderness as proteolysis occurs.
This period is generally referred to as the
conditioning period. It should be noted that
meat is tougher in the first eight days than it is
in the pre-rigor period. Normally, meat is
conditioned or tenderized in the carcass form
or in vacuum packs, both under chilled stor-
age conditions so as to maintain the cold
chain.
Proteolytic enzymes involved in conditioning
All organic matter undergoes “autolysis” after
death (i.e. enzymic tissue disintegration).
Game animals, for example, are traditionally
Figure 7 Tensile testing of conditioned muscle fibre
Muscle
fibre
Meat fibres with
long axis parallel
Fracture to the fibre
line Tension direction are
direction pulled apart until
they break
Figure 8 Changes in meat texture during storage (<4°C)
A C B
60
50
(or toughness)
Shear force

Conditioning of meat 40
The final conversion of muscle into meat 30
occurs after rigor when the meat is condi- 20
tioned or “hung”. Although the subject of
10
intensive research, the actual physiology as to
0
how meat becomes tender has not been eluci- 1 2 3 4 5 6 7 8
dated. It has been found in conditioned Time (days)
muscle fibres which are pulled apart mechani-
24
 The chemistry of flesh foods II
Peter Bayliss
held for an extended period in order to
improve texture and develop a “gamey”
flavour, e.g. pheasants with their viscera
intact, can be “hung” for up to c. 28 days.
Two enzymes have been identified as being
involved in the conditioning process, i.e.
proteolysis of the myofibrillar and cyto skele-
tal proteins. The basic proteolytic enzyme
systems involved are the calcium-activated
neutral proteinases (calpains I and II) and the
lysosomal acidic proteinases (cathepsins B, D
and L). For optimum proteolytic activity,
calpain I and II require 1-2mM and 50-20µM
Ca++ respectively, and degrade myofibrillar
and cytoskeletal proteins. Cathepsins from
the so-called “suicide bags” present in the
muscle fibre have an optimum pH activity of
3-4, hydrolysing myofibril and isolated pro-
teins.
Summary of enzymic action involved with meat
tenderization
It is hypothesized that cathepsins are the most
important enzymes involved in meat condi-
tioning, even though they mainly degrade
actin and myosin. Calpains start the degrada-
tion of proteins during the commencement of
rigor, and at a pHu of c. 5.5 become inhibited
by the acidic conditions. Cathepsins then
become activated and continue to be so
throughout the conditioning period.
Traditional butchers hang their meat in
carcass form for two or three weeks while
most large multiples specify ten days (80 per
cent of maximum tenderization) in wholesale
cuts that are vacuum packed.
Processing factors
Enzyme treatment of meat using
tenderizing enzymes
Meat can be artificially tenderized by treat-
ment with proteolytic enzymes such as papain
(paw paw plant), bromelin (pineapples), ficin
(figs) and bacterial and fungal enzymes.
The enzyme can be dissolved or used in a
powder form to dust, dip or spray cuts of meat
such as steaks, etc. Larger primal joints of
meat usually have the enzyme injected in.
Heat processing of meat
Certain cooking methods and cooking
regimes can result in an increase in meat
toughness. The effects of heat on meat are:
• degradation of proteins, e.g. solubilization
of collagen and coagulation of myosin;
• changes in toughness and eventual tender-
ization;
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Nutrition & Food Science
Number 2 · March/April 1995 · 21–26
• liquefaction of fat;
• shrinkage due to loss of sarcoplasmic fluid
(and fat);
• flavour development;
• reduction/elimination of micro-organisms;
• development of cooked meat colour.
It has now been established that there are two
distinct phases during cooking that are
common to both methods and a further third
phase with a wet cooking method (see
Figure 9). Each muscle protein has a particu-
lar temperature at which it denatures.
Phase one: 40-50°C
During this initial phase there is an increase in
toughness due to the denaturation of myosin.
This is a structural change involving the
rearrangement of the myosin protein chains.
The result is a net shrinkage of the muscle
fibre in the transverse direction. Collagen is
unaffected at this temperature.
Illustrated in Figures 10 and 11 is the
denaturation of the myosin in the muscle fibre
that results in shrinkage and an increased
widening of the annular channel first formed
during rigor. The collagen fibre network in
the endomysium exerts pressure on the sar-
coplasmic fluid within the channel, forcing it
out of the cut ends of the muscle fibres. This
loss of drip results in:
• shrinkage at the joint of meat in a trans-
verse direction to its grain; and
• toughening of the meat.
Figure 9 Effect of heat on meat texture
70
Phase 3
60
Shear force (arbitrary units)
Phase 2
50
40
Phase 1
30
20
10
0
0 20 40 60 80 100 120
Cooking temperature (ºC)
Figure 10 Muscle fibre illustrating shrinkage effects of
myosin (longitudinal section)
Drip loss
Endomysium
Muscle fibre
Longitudinal section
 The chemistry of flesh foods II Nutrition & Food Science
Peter Bayliss Number 2 · March/April 1995 · 21–26

Figure 11 Muscle fibre illustrating shrinkage effects of In the collagen of meat derived from older
myosin (transverse section) animals the heat-stable “mature cross links”
will have developed. The collagen in meat
from younger animals containing heat labile
Heat-induced shrinkage cross links is solubilized to gelatine during
of myosin increases cooking, making the meat tender. In collagen
diameter of annular
channel fibres containing a high proportion of heat-
stable cross links, heating results in derange-
ment of the fibres, but tenderness does not
Transverse ensue owing to the formation of covalent cross
section links that result in greater shrinkage, drip loss
and toughness (see Figure 14).

Phase two: 60-70°C Phase three: > 80°C (wet cooking)

During this temperature increment a second
toughening occurs with a net shrinkage in the
longitudinal direction. This is due to:
• a further denaturation of myosin resulting
in a longitudinal shrinkage; and
• denaturation of collagen in the endomysi-
um with the shrinkage in the tranverse and
longitudinal direction.
Illustrated in Figures 12 and 13 is the
endomysial collagen arranged in a laminated
cross ply, hence the shrinkage direction. The
net overall shrinkage direction with cooking
phase-one and two is in a longitudinal direc-
tion, but in order, physically, to reduce further
in size, the fluid or drip has to be squeezed
out.
Figure 12 Shrinkage of endomysial collagen fibres
(longitudinal section)
Direction of shrinkage
Wet cooking procedures result in slow tender-
ization that increases with time. This slow
hydrolysis is thought to be a result of breaking
heat-stable cross links and does not involve
any shrinkage.
During the solubilization, collagen frag-
ments are released into the surrounding
cooking solution. The wet cooking method
facilitates hydrolysis of the collagen and
because of its high heat coefficient is more
thorough in heat transfer. Hence poor quality
cuts of meat (high collagen content, e.g. shin)
are wet cooked or “stewed”.
Mechanical processing methods
All size reduction operations will have the
effect of increasing the tenderness of the
meat, e.g. bowl chopping, mincing, flaking,
etc. Some chefs advocate the “hammering” of
grilling steak or braising steak using a culinary
bat. Tenderization machines are available that
lacerate the surface of poorer quality steak-
like slices of meat to upgrade them. Normally
meat is cut or carved at right angles to the
longitudinal grain of the muscle so that it
fragments more easily when chewed.

Longitudinal
section
Figure 14 Heat-induced rearrangement of mature cross
links in collagen
Figure 13 Shrinkage of endomysial collagen fibres
(transverse section)
Heat-stable cross
links maintain
continuity of the
collagen, even
Direction of when dearranged
by heat
shrinkage

Linear Heat Random structure which shrinks

Transverse structure to 14 of its original length
section

26