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Veterinary Quarterly

ISSN: 0165-2176 (Print) 1875-5941 (Online) Journal homepage: https://www.tandfonline.com/loi/tveq20

Sensory meat quality and its assessment

F. J. M. Smulders

To cite this article: F. J. M. Smulders (1986) Sensory meat quality and its assessment, Veterinary
Quarterly, 8:2, 158-167, DOI: 10.1080/01652176.1986.9694035

To link to this article: https://doi.org/10.1080/01652176.1986.9694035

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Published online: 01 Nov 2011.

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Sensory meat quality and its assessment


F. J. M. Smulders'

SUMMARY Several aspects of meat quality are briefly discussed, outlining the complex of parame-
ters affecting meat quality as a whole. Particular attention is paid to the main sensory meat quality
characteristics, which can be assessed analytically, and are known to be related to consumers'
appreciation, when buying, preparing and consuming meat. After some compositional and structural
characteristics of muscle have been outlined, the major physiologicalfactors effecting the conversion of
muscle into meat are discussed. Finally commonly used methods for the assessment of sensory meat
quality are reviewed.

INTRODUCTION the complex of factors that constitute meat


Veterinarians play an important part in the quality in general, to discuss sensory meat
production of meat. They are frequently quality in particular and to summarise the
consulted on problems related to growth, impact of post-mortem physiology on the
health, breeding and reproduction of farm main sensory quality characteristics of
animals. This requires a thorough knowl- fresh meat. Finally methods are described
which may be used for assessing these char-
edge of physiology, pathology and micro-
biology. Consequently the main interest of acteristics in meat research practice.
the veterinarian-clinician concerns these
disciplines. The veterinarian-meat inspec- MEAT QUALITY CONCEPTS
tor once again pays particular attention to In daily slaughterhouse usage the term
pathology and microbiology. meat quality is frequently confused with
However, the interesting field of post-mor- carcass quality, which includes carcass-
tern physiology is generally left for the composition characteristics such as weight,
meat scientists and the technologists to ex- meat percentage and fat cover score. These
plore. This is not surprising in view of the factors constitute an important part of the
task and responsibilities of the veterinarian economical value of the carcass in market-
to safeguard public health. Generally meat ing. The carcass grading procedures and
inspection services are well informed on the associated price policy are indeed based
potential microbiological hazards to pub- on the consideration that carcass build-and
lic health and outstanding overviews on the -composition will generally coincide with a
subject have been published for the veterin- better potential quality of the meat. Yet,
arian readership. Their allegiance to this too many other quality determinants are
particular concept of meat quality has re- relevant in the meat industry to justify the
sulted in the tendency of veterinarians to, use of this simple concept of meat quality.
unjustly, regard the term meat quality sy- Hofmann (25) catagorised factors of meat
nonymous to wholesomeness. Yet meat quality and he proposed the following defi-
producers as well as consumers are as nition: 'meat quality is the sum of all sen-
much concerned with many other aspects sory, food physiological, hygienic/toxicol-
of meat quality which are tightly coupled ogical and technological factors of meat'
to physiological processes shortly before, (26). Table 1 presents a simplified list of the
during and after death of the animal. separate subfactors constituting the qual-
Purpose of this contribution is to outline ity categories (25).

1 Department of the Science of Food of Animal Origin, Faculty of Veterinary Medicine, the University of
Utrecht, Utrecht, The Netherlands.

158 THE VETERINARY QUARTERLY, VOL. 8, No. 2, APRIL 1986


These subfactors may well be looked upon
c4 F. differently by different professional groups.
LL r, -
H< Nutritionists, meat technologists and the
U a.
f
LL J
H
veterinarian/microbiologists will some-
times attach the same values to certain sub-
Z ci)
p E Z factors and generally their professional in-
14Z0 ,u terests will not be conflicting. However,
Z u Z0 their individual interests may occasionally
Z
OZ lead to paradoxes. A well known example
U 8 nc-
is the dark firm and dry (DFD-) meat
zz
w0 < which on account of its high pH is consider-
LLHL) 3
ed potentially hazardous by microbiol-
ogists whereas technologists recognise the
excellent waterbinding properties and con-
sider DFD meat particularly fit for the
production of some types of sausages.
0 The consumers' conception of meat quality
LL
0 include factors from several of the cat-
'5 5 egories mentioned in Table 1. His expecta-
tions with regard to meat quality were re-
I. X
U
cently summarised as 'meat that is safe,
wholesome and hygienic, perceived as good
O v, quality (worth its price), that is nutritious
0
0 and is produced through aesthetical and
<
a. U
< morally acceptable methods' (17).
Q.11

LQ U Quality factors that are perceptible to the


O c7)
Z
senses have particular economic relevancy
as these factors may be experienced by the
UH consumers themselves. Yet, the frequently
Z
quoted approach 'the best definition of
quality is that which the public likes best'
(24) is incorrect as it suggests quality to be
synonymous with popularity. However, as
extensively discussed by Jellinek (33), these
conceptions are fundamentally different.
The popularity of meat is subject to con-
stant changes and shows considerable differ-
ences from nation to nation. The con-
sumers' appreciation of intramuscular fat
in Northern America (15) as opposed to
that in Western Europe (5) may illustrate
this.
It is not intended to give an exhaustive
discussion on muscle composition, chem-
istry and physiology. Detailed information
may be found in textbooks (21, 38) or in
more elaborate reviews (2). The present
article will focus on the main sensory meat
quality characteristics that are measurable
in the laboratory and that are known to be
related to the consumers' appreciation
.0 when buying, preparing and consuming
E2 meat.

THE VETERINARY QUARTERLY, VOL. 8, No. 2, APRIL 1986 159


SOME COMPOSITIONAL AND STRUCTURAL globular G-actin. The actin helix is associat-
FEATURES OF MUSCLE ed with tropomyosin, a double helix of
Muscle is composed of 75% water, 19% two unidentical peptide chains, and the
protein, 2.5% fat and 3.5% soluble non- troponin complex which cements the tro-
protein substances (57). pomyosin to the actin helix. Fig. 1 schema-
Not more than 5% of the total water of tically presents this arrangement.
muscle is directly bound to hydrophilic The troponin complex is thought to turn
groups of the proteins. The rest of the on the contraction process by binding,
water is divided between the so-called 'free the calcium ions that are released from the
water', which is immobilised by the physi- sarcoplasmic reticulum after a nervous
cal configuration of the proteins but not stimulus (57). The thick myofilament myo-
bound to them, and the so-called 'loose sin is composed of a helical tail and a head
water' which is expressed when the water consisting of two globular units. The myo-
holding capacity drops (21). sin heads contain a site with ATPase activ-
Fat content varies in quantity and compo- ity and a site which forms cross bridges that
sition between muscles and species, males interact with actin to form actomyosin dur-
having less than females. Much of the in- ing muscle contraction. Fig. 2a shows a
tracellular lipids are associated with mem- diagrammatic representation of the main
brane structures. In addition considerable ultrastructural features of muscle.
amounts of lipids are present in the peri- The I band mainly consists of actin fila-
mysium surrounding myofibre bundles. ments that are attached to a transverse
Macroscopically this is perceived as structure called Z-lines. The spacing be-
'marbling'. tween Z-lines is referred to as sarcomere
Muscle proteins may be classified as sarco- length. Myosin fills the entire length of the
plasmic, myofibrillar and stroma proteins. A-band. A clear central H-zone contains
Sarcoplasmic proteins are soluble in water the M-line representing the cross bridges
or salts of low ionic strength. Many of them between separate myosin filaments. Near
are enzymes involved in the breakdown of the boundaries of A- en I-band thin so
glycogen. Myofibrillar proteins, which con- called N-lines are seen that may be sites of
stitute the major part of the contractile calcium ion accumulation (57). Relying on
mechanism, are only soluble in solvents ultrastructural studies some investigators
with higher ionic strength than required for (40, 41) suppose the presence of so-called
the extraction of sarcoplasmic proteins. gap-filaments that are assumed to be an-
The main myofibrillar proteins are myosin, chored inside the myosin as a 'core-pro-
actin and the troponin-tropomyosin com- tein' and, running through the Z-lines,
plex. Stroma proteins include collagen, re- interconnect myosin filaments of adjacent
ticulin and elastin, all present in connect- sarcomeres. These structures may play a
ive tissue, and the proteins which are role in tenderness (39).
found in the membrane system of the Transverse sections through that part of
muscle cell organelles such as mitochon- the A-band including both actin and myo-
dria and sarcoplasmic reticulum. sin have revealed that actin is arranged
The myofibrillar proteins are arranged in hexagonally around myosin. Near the Z-
repeating units of actin and myosin known lines actin is arranged as a tetragonal net-
as sarcomeres. The thin myofilament actin work. Possible the N-lines play a role in
is composed of a double stranded helix of guiding this array (39).
actin tropomyosin troponin
-

44,
--
*Ow Ara
N114111

Fig. 1. The attachement of the troponin-tropomyosin complex to the actin filaments (adapted from Cohen
(11)).

160 THE VETERINARY QUARTERLY, VOL. 8, No. 2, APRIL 1986


The location of two important cell organel- stimulate myosin ATP-ase.
les, i.e., mitochondria and sarcoplasmic re- Muscle relaxation also requires ATP as
ticulum, is indicated in Fig. 2a. Mitochond- myosin rods will only be allowed to shift
ria are the site of ATP synthesis. The out of the sheaths formed by the actin fila-
amount of mitochondria is an important ments provided ATP is present in its func-
criterion in fibre-typing muscle as 'white' tion of 'plasticizer' (3). Under anaerobic
(few mitochondria) and 'red' (more mito- conditions ATP is synthesised via the com-
chondria). The sarcoplasmic reticulum mem- paratively inefficient glycolysis leading to
branes release or concentrate calcium ions lactate which may be resynthesised to gly-
during muscle action. cogen in the liver via the Cori cycle (gluco-
neogenesis).
PHYSIOLOGICAL FACTORS EFFECTING THE When an animal is slaughtered it is subject-
CONVERSION OF MUSCLE TO MEAT
ed to a state of shock which acts upon the
Before discussing the assessment of sen- muscle as a complex of nervous stimuli.
sory meat quality some physiological Since carbohydrate and oxygen supply
events that underlie the conversion of have ceased the muscles are dependent on
muscle to meat should be looked into. Fig. glycolysis for their energy synthesis from
3 presents a diagram outlining these pro- the moment CP reserves have been deplet-
cesses with special reference to their impact ed. Consequently comparatively little ATP
on sensory quality characteristics such as is re-synthesised. Moreover, the enzymes
colour, waterbinding, tenderness and fla- catalysing glycolysis and ATP breakdown
vour. are activated and lactate and metabolites
In the living animal the blood circulation such as adenosine monophosphate (AMP)
provides the muscle fibres with oxxygen are formed. As a result the muscle pH gra-
and glucose. Whenever muscle action is dually falls. Rigor mortis sets in when too
required nervous stimuli effect a depolaris- little ATP is available to keep the actin and
ation of the sarcoplasmic reticulum mem- myosin filaments apart in a relaxed state.
brane. This results in a release of calcium This occurs when the ATP residue is ap-
ions which activate the enzymes that con- proximately 20% of its initial concentra-
vert glycogen into pyruvate and eventually tion (22).
into carbondioxide and water in the mito- The biochemical reactions in the period
chondria. In the course of this process ade- before rigor mortis, which is generally re-
nosine diphospate (ADP) is phosphorylat- ferred to as 'conditioning', have a great
ed to adenosine triphosphate (ATP). Initial- impact on sensory meat quality character-
ly the muscle relies on the muscle-specific istics. The actomyosin formation effects a
creatine phosphate (CP) to supply the high tenderness decrease. Temperature condi-
energy phosphate. The conversion of ATP tions during storage may affect the degree
to ADP directly supplies the energy needed of contraction in the rigor state. This is
for muscle contraction and metabolic activ- particularly observed in lean lightweight
ities. This is effected by calcium ions, releas- lamb, veal and beef carcasses subjected to
ed by the sarcoplasmic reticulum, which rapid chilling while there is still a consider-
A al. I A

a. ; H ; H

ZN M NZN M NZ

actin
myosin
' mitochondrion
. . h . . . s a rco plasmic
reticulum
glycogen
jgranula
CP
; c6G ly sosome
sarcolemma
b.

collagen
Fig. 2a. Diagrammatic presentation of the ultrastructure of muscle.
Fig. 2b. Transverse section through the A-band, including both actin and myosin.
THE VETERINARY QUARTERLY, VOL. 8, No. 2, APRIL 1986 161
LIVER MUSCLE
.
lactate lactate . lactate
N
/
Car-activated enzymes anaerobically
glucose 6 tv glucose 6 ® pyruvate
t
glucose i i
/------
02 ADP ItCi --a. H20
The aerobically V
ATP .----rd02 + H20
11 glucose
glycogen Iglycogen CP C ,.../ 0
ENERGY

slaughter
V
glucose 6 ® ca2
4

4,
activation
of enzymes

ADP C
®
pyruvate H20 ATP 0
5
E
conditioning
lactate + H H + ADP 0
ADP
T
90%1 110 V.

pH -fal irreversible AMP


actomyosin - - - [ATP] 20%
formation: of initial
concentration
RIGOR
MORTIS

1 1
COLOUR *--WATER TENDERNESS I
LIGHTER RETENTION
enzymatic CAF IMP
proteolysis:
PROTEIN
aging CHARGE ..---degradation
1 11
COLOUR WATER TENDERNESSI FLAVOUR I
LIGHTER RETENTION

Fig. 3. Diagrammatic presentation of the physiological factors effecting the conversion of muscle to meat.

able supply of ATP available. The low loss of water retention (21). Moreover, the
temperatures result in an increased release loss of ATP and the consequent formation
of calcium ions from the mitochondria of actomyosin will cause a loss of the water
whereas the facility with which the sarco- retention at any pH. This arises from the
plasmic reticulum withdraws calcium ions fact that the water holding capacity of ac-
from the sarcoplasm is reduced. The in- tomyosin is less than that of myosin and
creased calcium ion concentration stimu- actin from which it forms. Furthermore,
lates the contractile mechanism of the lower ATP levels may initiate denaturation
muscle and causes an increased toughness of those proteins whose integrity in vivo is
known as cold shortening. Since 'red' particularly dependent on the provision of
muscles contain more mitochondria than energy (38). A result of the. loss of water
'white' muscles the former are particularly retention is that the muscle pigment myo-
prone to cold shortening (57). globin will be seen through a denser mesh
The accumulation of hydrogen ions pro- of water molecules and the meat colour will
duced during glycogen and ATP break- appear lighter.
down results in a pH fall. The decreased When glycogen reserves are severely deplet-
repulsive forces between proteins, which ed ante-mortem the post-mortem muscle
are brought about by the low pH result in a pH will stay high which results in dark,

162 THE VETERINARY QUARTERLY, VOL. 8, No. 2, APRIL 1986


firm and dry (DFD) meat. DFD is observ- The scientific principles of sensory analysis
ed in meat such as pork, mutton and beef by such panels have been documented ex-
and is associated with excitation or stress- tensively (1) and procedures for training
ful conditions ante-mortem. In contrast, and testing panelists for meat evaluation
certain breeds of susceptible pigs produce have been proposed (12).
pale, soft, exudative (PSE) meat (10). In Although not considered a complete sub-
PSE carcasses there is a very rapid early stitute for taste panel evaluation, the re-
post-mortem pH-fall and onset of rigor sults of objective tests to assess quality are
mortis. The decreased water holding capac- promising for some of the criteria particu-
ity of such meat is related to the denatura- larly colour, tenderness and juiciness.
tion of sarcoplasmic proteins as well as
lower ultimate pH. pH and temperature measurement
Already starting before completion of rigor Two basic methods for pH measurement
mortis (dependent of species varying from are available. The first and most simple is
8-48 h post-mortem) the aging process con- the use of indicator paper. Between the two
tinues progressively in the post rigor extreme pH values the paper acquires
period. Due to progressing damage of in- different colours that are compared with a
tracellular membranes, particularly those colour scale. This method is rather impre-
of the lysosomes, enzymes such as acid ca- cise. The second and more commonly used
thepsins are released and autolysis of the method is the potentiometric pH determi-
myofibrillar proteins starts (44). Addition- nation. Its principle is the measurement of
ally a so-called 'calcium-activated factor' a potential difference between a glass and a
(CAF), not located in a membrane-bound reference electrode (generally combined
subcellular particle, contributes to the de- into one single probe) which
are placed in
gradation of proteins in the Z-line (49). the muscle at a depth of at least 2 cm (31).
Consequently tenderness is re-increased The rapidity of pH fall in carcasses is often
while water retention is adversely affected. measured in the longissimus muscle. This
Products of glycogen and protein degrada- seems justified because of the commercial
tion (lactic acid, peptones, amino acids) value of this muscle, its tendency to de-
together with ATP metabolites, particu- velop high pH values and the greater range
larly inosin monophosphate (IMP), deter- of pH values of the muscle as compared
mine the typical meat flavour (2). with others (53). In the laboratory the pH
can also be measured in a slurry of equal
THE ASSESSMENT OF SENSORY MEAT parts of muscle and isotonic saline. A re-
QUALITY PARAMETERS
presentative sample should at least weight
The consumers' inclination to buy fresh 200 g (31). Recently a plug sampling tech-
meat is determined by two main groups of nique has been developed which enables an
factors. The first group may be described accurate pH measurement in a homogen-
as appearance (including texture and col- ate of only 2 g, causing minimal damage to
our), the second one as eating quality (in- the carcass (45). Factors that affect the ac-
cluding tenderness, juiciness and flavour). curacy of measurement of pH have been
Conditions such as pH and temperature summarised by Van Logtestijn (42). Par-
which were shown to have a major impact ticularly environmental conditions such as
on these factors, can only be determined temperature and relative humidity appear
with objective methods. However, many to have major effects.
meat quality traits may be assessed both Intermittent temperature measurements in
subjectively and objectively. carcasses are usually performed with needle
Subjective quality evaluation relies on the type probes that may be inserted deep into
physical senses of a panel of judges. These the muscle tissue. Continuous temperature
may be 'house-hold' type panels composed monitoring is realised through insertion of
of untrained panelists, or trained panels thermocouples connected to a recorder. In
consisting of judges whose ability to differ- both cases differences are measured as
entiate correctly for different quality at- electric signals which are translated as de-
tributes has previously been ascertained. grees Celsius. .

THE VETERINARY QUARTERLY, VOL 8, No. 2, APRIL 1986 163


Muscle structure differences in reflectance of the red colour
Muscle texture is determined by structure, component. The Göfo equipment develop-
tenderness and juiciness. In fresh meat ed for fresh pork and beef is based on this
coarseness of grain (muscle fasciculi) is the principle. The more complicated tri-stimu-
only textural feature that may be assessed lus equipment is also based on the reflect-
by the consumer. The coarseness of grain is ance measurement of light which is thrown
primarily related to age and weight of the on the meat surface at an angle of 45°.
carcass (24) and it is considered an import- Colour coordinates shown in Figure 4, are
ant factor affecting the eating quality of recorded. A frequently used system is the
meat (24, 50, 51). The larger the fibre CIElab L*, a*, b* or the Hunter L, a, b
bundle diameter (the coarser the meat), the relative to light source C. L-values repre-
tougher it is. In practice this quality at- sent lightness (black-white continuum) and
tribute may be judged by passing the ball of a-value (red-green) and b-value (blue-yel-
the thumb over the cut transverse surface low) determine the colour tint (tg-t-) and
of a muscle and feeling its degree of saturation ( \/a2 + b2). Colour values thus
smoothness (24). assessed are absolute and reproducible.
The impact of cross sectional fibre diame-
ter which is assessed microscopically is re- Tenderness
garded a less reliable parameter for tender- The major part of muscles consists of the
ness (Berry et al. 1971, cited by 2, 55). myofibrillar proteins. The impact of pH
Colour and temperature fall in the early post-mor-
tem period on these proteins has already
The colour of fresh meat is determined been discussed. To reveal a possible though-
largely by the concentration of the chromo- ening by cold shortening sarcomere length
protein myoglobin and to some extent by should be assessed. This may be achieved
the concentration of hemoglobin. The dis- by microscopial techniques or by laser
tribution and above all the chemical state diffraction. The latter method is based on
of myoglobin have a major impact on the the fact that the alternating units of actin
perception of colour. The chemistry and and myosin act as a lattice. Consequently
related aspects of myoglobin have been the formulae for light diffraction are ap-
discussed in detail by Giddings (19). Of plicable (wave length of laser light = sar-
major importance is the relative propor- comere length x sine of the diffraction
tion of oxymyoglobin, myoglobin and met- angle) (37a, 56).
myoglobin. For this reason meat that has The myofibrillar proteins are enveloped
to be tested for colour should be exposed to by a number of connective tissue fibres.
air for at least an hour ('blooming'). More- Although these constitute only a small per-
over, the colour is determined by the reflect- centage of the total muscle protein the
ance of myoglobin, seen through a mesh strength of the collagen fibres is of such a
of water molecules the thickness of which is
pH dependent. Consequently simply assess- w
ing the heme pigment (30) often does not
yield results that are closely related to vis-
ual colour ratings.
Absolute colour scores cannot be provided .1.t)

through visual assessment since it is extrem- yekk9v4

ely difficult for humans to develop a col-


our 'memory'. Useful aids are colour
standards (16). For beef (47) and pork (43)
such standards are used jn slaughterhouse
practice.
The principles of objective colour measure-
ment have been reported by Klettner and
Stiebling (37). A simple colour measure- black
ment is achieved through measurement of Fig. 4. Colour coordinates.

164 THE VETERINARY QUARTERLY, VOL. 8, No. 2, APRIL 1986


magnitude that it is a major contributor to Several objective methods are available for
meat toughness. As an animal grows older tenderness assessment (36). Two devices
the amount of cross linking between col- are generally used i.e. the Warner Bratzler
lagen fibres increases and thus the connect- shear device and the Volodkevich bite ten-
ive tissue solubility is adversely affected derometer. The Warner Bratzler shear con-
(35). To attain a satisfactory tenderness in sists of a 1 mm thick stainless steel blade
meat of older animals heating methods and with a hole in which the sample is placed.
-temperatures have to be adapted. The blade is led through a slid between two
Buchter (9) summarised the influence of shear bars and the amount of shearing
heating temperature on meat tenderness. force is recorded. The Volodkevich device
From 40 to 50° C the increasing denatura- consists of rounded wedges or bars be-
tion of myofibrillar proteins results on a 3 tween which the meat samples are squeezed
to 4-fold toughening. In the 60-75° C tra- and sheared until they eventually break.
ject connective tissue- myofibrillar- and Both Warner Bratzler and Volodkevich
sarcoplasmic proteins shrink almost maxi- devices are usually mounted on a draw
mally resulting in yet another two-fold bench connected to a recorder which prints
toughening (14) or even a four-fold tough- the way-force diagram. A commonly used
ening in cold shortened meat (6). A tempera- draw bench is the Instron Universal Test-
ture of 70-80° will 'cook' the meat to the ing Machine. Sometimes low shear forces
extent that it is firm and well-done. Finally are found concomitantly with low panel
temperatures of 80-100° C will solubilise tenderness scores. This apparent contra-
the connective tissue and make myofibrils diction is attributed to a high connective
fragile. tissue resistance (46). Therefore both in-
The reference heating method for beef as strumental and sensory evaluation of ten-
agreed on by an EEC-working group on derness should be conducted.
meat quality recommends heating in a
thin-walled polythene bag in water of 75° C Juiciness
followed by cooling in running water for at The term water holding or water binding
least 40 min (4). The American reference capacity is confusingly used for three differ-
methods mention heating temperatures of ent conceptions of water binding which
70, 75 and 75° C for beef, lamb and fresh were recently recognised as water binding
pork respectively (13). The increase of the potential (WBP, referring to the ability to
core temperature is monitored by thermo- hold water in excess and under the in-
couples. fluence of an external force like salt), ex-
Samples from the cooked meat are excised pressible moisture (representing the
using cork bores. The meat cylinders with amount of liquid squeezed from a protein
an approximate diameter of 1 cm' may be system by the application of force) and
used both for sensory and instrumental finally free drip (referring to the amount of
tenderness evaluation. liquid lost by a protein system without the
Sensory evaluation is generally performed application of external force other than
by an experienced taste panel. For the pur- gravity) (32).
pose of assessment of differences the tradi- Drip loss is particularly effected by pres-
tional paired comparison tests (29, 54) are sure on the myofibrillar system in the
available. The main advantage of these course of rigor. Severe muscle shortening
methods is the simplicity which makes the (28, 52) as well as sarcoplasmic protein
results very reliable. Panel members are denaturation may enhance this. Another
asked to indicate preference within one parameter of water binding i.e. heating loss
pair of samples. Assigning scores to the primarily reveals the influence of pressure
samples may help to quantify the differen- resulting from heat coagulation. The latter
ces. Several scoring scales are possible. effect appears to be much higher than the
Numerical scales (a series of numbers rang- shrinking of the raw tissue during storage
ing from low to high and understood to (23).
represent successive levels of tenderness) Whereas water binding potential is rel-
are commonly used. evant in meat processing the expressible

THE VETERINARY QUARTERLY, VOL. 8, No. 2, APRIL 1986


165
moisture and free drip particularly relate to Tinbergen, B. J., and Touraille, C. Procedures
fresh meat. Two basic methods are avail- for measuring meat quality characteristics in beef
able to measure expressible moisture. In production experiments; Report of a working
group of the Commission of the European
the filter press method by Grau and Hamm Communities (CEC), Beef production Program-
(20) a meat sample is pressed between plexi- me. Livestock Production Science 1981; 8: 385.
glass leaving a ring of water in the filter 5. Boer, H. de. Animal production systems to meet
paper the diameter of which is considered consumer demands-Western Europe in: K. R.
Franklin, H. R. Cross (eds) Proc. Meat Science
to be related to water binding. Modifica- and Technology Symposium, Lincoln-Nebraska,
tions of this method are the centrifugal Publ. National Livestock and Meat Board, Chi-
methods which essentially combine the cago (Ill.): p 17, 1982.
gravimetric adaptation of the press method 6. Bouton, P. E., Harris, P. V., and Ratcliff, D.
with the application of a centrifugal force Effect of cooking temperature and time on the
shear properties of meat. J. Food Sci. 1981; 46:
(7, 8, 32). 1082.
Free drip is measured by weighing samples. 7. Bouton, P. E., Harris, P. V., and Shorthose, W.
Recommended procedures agreed upon by R. Effect of ultimate pH upon the waterholding
an EEC working group on meat quality are capacity and tenderness of mutton. J. Food Sci.
1971; 36: 435.
in preparation. 8. Bouton, P. E., Ford, A. L., Harris, P. V., and
Hofmann's capillary volumeter (27) was Ratcliff, D. Objective assessment of meat juici-
developed to differentiate between watery ness. J. Food Sci. 1975; 40: 884.
and normal meat. It is based on the absorp- 9. Buchter, L. Measurement of meat texture. Slag-
tive capacity of a porous plaster shape. The teriernes Forskningsintitutet Manuskript nr. 571
E. Presented at DIEU-seminar on food texture
meat juice absorbed by capillary forces of and rheology, Copenhagen 23-24, November
the plaster pushes a corresponding quan- 1978.
tity of air out of the plaster shape which is 10. Cassens, R. G., Marple, D. N., and Eikelen-
indicated volumetrically by the liquid col- boom, G. Animal physiology and meat quality.
Adv. Food Res. 1975; 21: 71.
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