Meat Science 91 (2012) 364368

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Meat Science
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Meat quality comparison between fresh and frozen/thawed ostrich M. iliofibularis

Coleen Leygonie

a, b

, Trevor J. Britz , Louwrens C. Hoffman

Department of Food Science, University of Stellenbosch, Stellenbosch 7600, South Africa

Department of Animal Sciences, University of Stellenbosch, Stellenbosch 7600, South Africa

article

info

Article history:
Received 2 November 2011
Received in revised form 14 February 2012
Accepted 16 February 2012
Keywords:
Ostrich
Freezing
Thawing
Meat quality
Lipid oxidation
Protein oxidation

b,

abstract
A pairwise comparison of the meat quality between fresh and frozen/thawed Musculus iliofibularis was con-ducted. Thirty-two
(16 left; 16 right) muscles were collected and allocated to two treatments: fresh and fro-zen/thawed. Frozen vacuum-packed
samples were stored for 1 month at 20 C before thawing. The fresh samples had higher pH (P b 0.05), water binding
capacity (P b 0.05), CIE L* (P b 0.0001), CIE a* (P b 0.05) and Chroma values (P b 0.05) than the frozen/thawed samples,
indicating the fresh samples were bright red in ap-pearance and had minimal exudate. The frozen/thawed samples lost 5.09
0.21% moisture during thawing and had a greater drip loss (P b 0.0001) and shear force (P b 0.001). No differences were
obtained with regard to cooking loss, CIE b*, hue and TBARS. Protein oxidation (mM carbonyls/mg protein) was lower (P b
0.05) in the frozen/thawed samples, which was attributed to the higher (P b 0.0001) protein concentration negating the higher
(P b 0.001) carbonyl content. Industrial freezing and thawing regimes negatively affected the qual-ity of ostrich meat.

2012 Elsevier Ltd. All rights reserved.

0309-1740/$ see front matter 2012 Elsevier Ltd. All rights reserved.
doi:10.1016/j.meatsci.2012.02.020

1. Introduction
The South African ostrich meat industry has grown considerably over the
past years, predominantly in the export sector, which ex-ports approximately
90% of all meat produced (Anonymous, 2011). Frequently, the meat is
exported in a frozen state and thawed on ar-rival before being processed
further. The latter normally consists of cutting the muscles into steaks and
packaging them in various forms (MAP, oxygen permeable) for retail sales.
Freezing the meat is economically feasible as it increases the shelf-life of the
product and allows less expensive transportation options (e.g. ship) to be
used, compared to chilled meat (air transport).
Freezing and thawing of meat has been found to reduce its quality (Vieira,
Diaz, Martnez, & Garca-Cachn, 2009). During freezing, ice crystals are
formed between and within the fibres that physically damage the ultrastructure of the meat because as water freezes out it leads to an increase in the
concentration of the solutes surrounding the sensitive protein structure. The
ice crystals that form draw water from the intracellular spaces to the
intercellular spaces that lead to excessive moisture loss during thawing,
causing changes in the sen-sory profile as well as influencing the tenderness
(An & Calvelo, 1980; Ngapo, Babare, Reynolds, & Mawson, 1999). The
moisture loss further increases, as the damage to the ultra-structure of the
meat fi-bres does not allow uptake of moisture into the intracellular spaces

Corresponding author. Tel.: + 27 21 808 4747; fax: + 27 21 808 4750. E-mail

address: lch@sun.ac.za (L.C. Hoffman).

upon thawing. In addition, the increase in solute concentration in-creases the

susceptibility for protein denaturation. Myoglobin is one of the proteins that
denatures during freezing and thawing. The glo-bin fraction of the myoglobin
denatures leading to a loss in colour sta-bility (An & Calvelo, 1980; Jeong,
Kim, Yang, & Joo, 2011). As freezing does not cause all biological processes
to stop, oxidation is a major contributor to quality deterioration in
frozen/thawed meat. Lipid oxidation tends to accelerate post thawing due to
peroxidation during frozen storage that yields reactive oxygen species (ROS),
which in turn also increases protein oxidation (Leygonie, Britz, & Hoffman,
2011a; Xiong, 2000).
The majority of the studies on the effect of freezing and thawing of meat
have been conducted on traditional red meat species such as pork and beef.
These species differ considerably from ostrich meat, primarily in the
distribution, content and composition of fat and the amino acid composition
(Paleari et al., 1998; Sales, 1998). The myoglobin content and the pH of the
ostrich meat are also higher than in other red meat species (Sales & Hayes,
1996). These proper-ties influence the overall characteristic of the meat,
potentially causing the meat to be more or less sensitive to freezing and
thawing.
The aim of this study was to establish if ostrich fillets (Musculus
iliofibularis) that are frozen and thawed, using commercial parameters, differ
from the fresh fillets from the same bird. This ensures that the bird effect is
constant and only the treatment effect is measured. The differences
investigated include the fillets'

physical properties (pH,

moisture retention, colour and shear force) and
the muscles' lipid oxidation (TBARS) and free
carbonyl production (protein oxidation).

C. Leygonie et al. / Meat Science 91 (2012) 364368

2. Materials and methods

2.1. Sample preparation
2.1.1. Birds, slaughter and transport
Sixteen South African Black (Struthio camelus var. domesticus) ostriches
raised in the Oudsthoorn district were slaughtered at 14 15 months of age at
the EU approved Klein Karoo ostrich abattoir. Al-though all the birds
weighed 90 kg, they were reared by different producers and under different
feeding regimes. The objective of the investigation was to source birds that
would be representative of commercial ostriches slaughtered and therefore
common animal pro-duction factors that are known to influence the chemical
composition of ostrich muscle were not included as main effects. The dressed
car-casses were cooled within ca. 45 min after exsanguination in a cooling
chamber at 04 C for 24 h before deboning.
The M. iliofibularis (Fan Fillet) was removed from the left and right leg of
the carcass, and after removal of the external fat and epimysial connective
tissue, the samples were vacuum packaged and trans-ported (ca. 5 h) under
chilled (0 C) and hygienic conditions to the Department of Animal Sciences
(University of Stellenbosch). Im-mediately upon arrival, the muscles were
split into two groups, left and right. The left M. iliofibularis was allocated to
the freezing treat-ment and the right to the fresh treatment. It was assumed
that the left and the right side's muscles were homogenous. The samples allocated to the freezing treatment were immediately frozen and the samples
allocated to the fresh treatment were prepared for analysis.
In preparation for analysis (drip loss; cooking loss and shear force; colour,
pH, water binding capacity and oxidation) of the fresh and fro-zen/thawed
muscles, three 1.5 cm thick steaks were cut perpendic-ularly to the muscle
fibres. These steaks were cut from the centre of each muscle and packaged in
a polystyrene tray wrapped with air permeable cling wrap (10 micron
Versafilm (Crown National, Monta-gue Gardens, Cape Town, South Africa))
with a moisture vapour transfer rate of 585 g/m/24 h/atm, O 2 permeability
25,000 cm/m/ 24 h/atm and a CO2 permeability of 180,000 cm/m/24 h/atm
to allow blooming and to minimise desiccation before analysis.

2.1.2. Freezing and thawing

The left M. iliofibularis was frozen in a blast freezer set at 20 C with a
wind speed of 2.6 m/s. Thermocouples were inserted at two sites in the
muscles (prior to freezing), the thermal centre and 1 cm below the surface
(EBI-6, Ebro Electronic GmbH & Co. KG, In-golstadt data logger with
thermocouple attached). Freezing was stopped when the thermal centre
reached a temperature of 20 C. The samples were stored for 1 month at 20
C before thawing. Prior to thawing, one thermocouple was inserted in up to
the thermal centre (using an electric drill) and the frozen muscles were placed
in a refrigeration unit at 4 C with a wind speed of 1.2 m/s until the ther-mal
centre reached 0 C. The muscles were then packaged as noted above and
prepared for analysis.

2.2. Physical analysis

2.2.1. Surface colour
The surface colour of the ostrich steaks was measured according to the
CIE L*a*b* colour system using a Color-guide D65/10 (daylight
illumination, aperture opening) 45/0 colorimeter (BYK-Gardner GmbH,
Gerestried, Germany). Five measurements were taken on the steaks after
allowing the cut steaks to bloom for 4.5 h after packaging, under fluorescent
light illumination (L 58 W/20, Osram, Germany; 870 lux (MT 940, Major) at
4 C (Leygonie, Britz, & Hoffman, 2010). The average of the five readings

365

2.2.2. pH
The pH of the centre of the steak was measured using a Testo 205 pH
meter (Testo AG, Germany) fitted with a glass meat probe (auto-matic
adjustment for temperature) that was inserted into the steak perpendicular to
the muscle fibres.
2.2.3. Moisture loss
For thawing, the whole frozen muscles were placed in a refrigera-tion unit
at 4 C with a wind speed of 1.2 m/s until the thermal centre reached 0 C.
Thaw loss was determined by weighing each whole muscle prior to freezing
and again after thawing and blotting dry with tissue paper. Thaw loss of the
whole muscle was expressed as a percentage of initial weight prior to
freezing.
The water holding capacity (or expressible water, WHC) was de-termined
using one of the steaks in the package using the press meth-od. A cube of
meat weighing 500 mg was cut from the centre of the steak, diced with a
sharp scalpel and placed on a filter paper (What-man #2), sandwiched
between two Perspex plates and pressed at a standard pressure (588 N) for 1
min. The WHC was calculated by de-termining the ratio of meat area to the
liquid area after compression. The measurement was taken in duplicate.
Photos taken of the two areas were used to measure the two circumferences
by means of the Image J 1.41 computer package (Trout, 1988). The ratio of
the expressed water area over the meat area was used as an indication of
WHC of the meat.
Drip loss was determined by suspending the weighed second steak in
inflated polyethylene bags (taking care that samples did not touch the sides of
the bags) for 24 h at 4 C. After 24 h, samples were removed, blotted dry
and weighed; drip loss was calculated as the percentage of weight lost
(Honikel, 1998).
To determine cooking loss, the third steak was weighed and cooked in a
polyethylene bag in a water bath at 80 C for 60 min (Honikel, 1998).
Samples were then removed from the water bath, the water drained from the
bags and the samples (still in the bags) cooled under running water to 20 C
after which they were blotted dry with tissue paper and weighed. Cooking
loss was calculated as the percentage of weight lost.

2.2.4. Shear force

Meat tenderness was determined on the cooking loss-steaks. Meat
tenderness was evaluated using a Warner Bratzler device (load cell of 2.000
kN) attached to a model 4444 Instron texture machine (Apollo Scientific cc,
South Africa). The machine has a measuring speed of 200.0 mm/min. Five
core samples (1.27 cm in diameter) were cut with a core-borer parallel to the
muscle fibre axis to ensure the blade of the Warner Bratzler device cuts at
right angles to the fibres. The mean values (N) attained from the five samples
were used in the statistical analysis.

2.3. Lipid oxidation

Lipid oxidation was assessed by the 2-thiobarbituric acid (TBARS)
extraction method of Lynch and Frei (1993). Core samples (1.0 1.0 1.0 cm
meat block from the centre of the steak) from each sample, wrapped in tinfoil
and snap frozen in liquid nitrogen, were kept frozen (20 C) until analysed
(btwo weeks). Analysis was conducted on 1 g of frozen core sample and the
TBARS concen-trations were calculated using 1,1,3,3-tetramethoxypropane
(020 M) as a standard and expressed as milligram malonaldehyde (MDA)
per kilogram of meat.

2.4. Protein oxidation

was used in the statistical analysis. The Hue angle (hab) () and the
1

Chroma (C*) were calculated using the a* and b* values: Hue = tan (b*/a*)
2

2 0.5

and Chroma = (a* + b* )

Protein oxidation was assessed by estimating the protein carbonyl content

with the derivatization of 2,4-Dinitrophenylhydrazine (DNPH) as described
by Oliver, Ahn, Moerman, Goldstein, and

366

C. Leygonie et al. / Meat Science 91 (2012) 364368

Stadtman (1987). Core samples (as defined under lipid oxidation) were
collected and wrapped in tinfoil and snap frozen in liquid nitro-gen, and
stored at 20 C until analysed (btwo weeks). The carbonyl content was
determined from 1 g of frozen core sample by subtract-ing the absorbance of
the HCl control sample from the DNPH sample at 320 nm
(Spectrophotometer, CE 2021, Cecil, Cambridge, England) and using 21.0
mM/cm as the absorption coefficient. The protein con-centration was
determined on the HCl control sample with a Bicin-chroninic acid (BCA)
protein assay kit and by reading the absorbance at 562 nm. The results were
expressed as nanomoles of DNPH fixed per milligram of protein.

2.5. Statistical analysis

Paired Student's t-least significant differences were calculated to compare
treatments using the pairwise t-test procedure of the SAS statistical software
version 9.1 (SAS, 2000). A probability level of 5% was considered significant
for all tests.
3. Results
The characteristic freezing (tc) and thawing times (td), defined as the time
to transverse from 1 C to 7 C and vice versa for thaw-ing (Bevilacqua,
Zaritzky, & Calvelo, 1979), were 73.3 min (surface) and 237.5 min for the
centre of the muscle for freezing, and 697.5 min at the thermal centre of the
muscle for thawing.
The mean values for all the parameters tested for the fresh and
frozen/thawed samples as well the P-values are depicted in Table 1. The fresh
meat had a higher (0.09 0.13 units) (P b 0.05) pH than the frozen/thawed
meat. The percentage drip loss of the frozen/ thawed meat was greater (P b
0.0001) than the fresh. The ratio of the area of expressed fluid over area of
meat (WHC) from the fresh meat was smaller (P b 0.05) than the
frozen/thawed meat, implying that the water holding capacity was stronger in
the fresh meat. The fluid lost during cooking did not reveal any significant
differences be-tween the two treatments. The shear force or toughness of the
frozen/ thawed meat was greater (P b 0.001) than the fresh, with an average
difference of 7.64 7.48 N. The colour of the meat differed for the CIE L* (P
b 0.0001), CIE a* (P b 0.05) and chroma (P b 0.05) values. The average
difference between the fresh and the frozen/thawed samples were 2.65 0.98
units for the CIE L*, 1.02 1.89 units for the CIE a* and 1.12 2.05 units for
the chroma. The CIE b* and hue angle did not differ (P > 0.05) and hence can
be regarded as being the same for the fresh and the frozen/thawed meat.

Table 1
Mean values for the physical meat quality parameters (mean standard error, s.e.) as measured
in M. iliofibularis muscle for fresh and frozen/thawed samples.
Parameter

pH
Thaw loss (%)
Drip loss (%)
Cooking loss (%)
Water holding capacity
(ratio water: meat)
Shear force (N)
CIE L*
CIE a*
CIE b*
Hue
Chroma
TBARS (mg MDA/kg meat)
Free Carbonyls (mM/mg protein)
Carbonyls (mM/g meat)
protein (mg/g meat)
(mM Carbonyls/mg protein)

Fresh

Frozen/Thawed

Mean s.e

Mean s.e

P > |t|

6.08 0.0373

1.26 0.106
40.27 0.379
0.86 0.06

6.00 0.028
5.09 0.206
2.22 0.181
39.43 0.623
1.15 0.05

b0.05

b0.0001
0.191
b0.05

50.16 1.390
28.47 0.312
19.62 0.447
14.28 0.263
36.22 0.562
24.32 0.480
1.76 0.031

57.79 2.147
25.82 0.315
18.61 0.159
13.86 0.193
36.62 0.180
23.21 0.239
1.74 0.088

b0.001
b0.0001
b0.05
0.195
0.466
b0.050
0.815

0.02 0.002
0.26 0.029
0.07 0.008

0.04 0.005
0.68 0.066
0.05 0.005

b0.001
b0.0001
b0.05

The lipid oxidation was similar (TBARS value of approximately 1.75 mg

MDA/kg of meat) for both treatments. Although the amount of free carbonyls
(mM) was greater (P b 0.0001) in the frozen/thawed samples as well as the
amount of protein (mg) (P b 0.001), the fresh samples showed greater (P b
0.05) protein oxidation.
4. Discussion
There were clear quality differences between the fresh and frozen/ thawed
meat samples. However at this point it is essential to note that time (1-month
separation between analysis of fresh and fro-zen/thawed samples) was an
unavoidable confounding factor. Loss of fluid as exudate is the major quality
concern within the meat pro-cessing industry and it was seen that ostrich is
also plagued by this problem with the frozen/thawed samples losing 7.3%
fluid combined for thaw loss and drip loss. This is the direct result of the loss
in water holding capacity (WHC, Table 1) due to the formation of ice crystals
during freezing that penetrate the cell membranes puncturing the cell
membranes with subsequent leakage of moisture from the intra-cellular space
to the extracellular space (Leygonie, Britz, & Hoffman, 2012; Ngapo et al.,
1999). The increase in solute concentration during freezing and frozen storage
also leads to the denaturing of proteins, which influence the WHC (Wagner &
An, 1985). These all (pre-dominantly ice crystal formation but also protein
denaturation Leygonie et al., 2012; Estvez, 2011) contribute to the loss in
ability of the meat to take up fluid during thawing and retain fluid during
display post-thawing (Leygonie et al., 2011a). The rate of freezing in-fluences
the amount of moisture loss (thaw and drip losses) as it in-fluences the
location and size of the ice crystals. An and Calvelo (1980) found that in
beef frozen at a characteristic freezing time of 17 min, the drip loss was at its
greatest, after which it decreased to reach a linear plateau. In this
investigation, the fastest freezing sec-tion (surface) was already slower than
the 17 min barrier therefore it can be deduced that the entire meat sample
(muscle) lost the same amount of fluid at each rate interval in the temperature
gradi-ent that formed in the muscle during freezing and thus did not influ-ence
the moisture loss.

The slight decrease in pH due to freezing and thawing most likely arose
from the loss of minerals and small protein compounds as exu-dates, thereby
changing the ionic balance in the meat, which resulted in a decreased pH. The
increased amount of free amino acids and free carbonyls caused by the
denaturation of the protein may also have changed the iso-electrical point of
the proteins resulting in decreased water binding capacity (see review of
Estvez, 2011). The cooking loss was not affected by the freezing/thawing
treatment, as the water expelled during cooking originates mostly from
chemically bound water (10% of total fluid) and from the fat that melts,
which is not affected by freezing and thawing (Vieira et al., 2009). However,
if the total water lost is compared between the fresh (41%) and
frozen/thawed (46%) it is clear that the latter lost more waterthis is most
likely attributed to structural damage as dis-cussed previously and reviewed
by Leygonie et al. (2012).
As water leaches out of the meat during thawing the muscles fi-bres
become less hydrated, the meat thus increases in toughness due the shrinkage
of the fibres, which in turn increases the density of fibres per surface area
increasing the force necessary to shear through the fibres. According to
sensory research, a Warner-Bratzler shear force value b42.87 N and >52.68 N
is the classification for ten-der and tough meat respectively (McMillin, 2008).
This places the fresh meat in the grey area between tough and tender and the
fro-zen/thawed meat well above the threshold for toughness, which could
significantly influence the consumer's sensory experience. This result
contradicts that of Muela, Saudo, Campo, Medel, and Beltrn (2012) who

sensory panel and

between fresh versus

could not find any differences between a trained

consumer evaluations
frozen lamb.

C. Leygonie et al. / Meat Science 91 (2012) 364368

367

The visual sensory experience is also significantly influenced by freezing

and thawing, as a significant decrease in the CIE L*, a* and Chroma values
(Table 1) occurred in the frozen/thawed samples. This translates into a
product that is browner and duller in appear-ance, overall less attractive to the
consumer. This is due to the culmi-nating effect of the denaturing of the
globin moiety of the myoglobin molecule during freezing, frozen storage and
thawing (An & Calvelo, 1980); the loss in activity of the metmyoglobin
reducing en-zyme system that continually reduces metmyoglobin back to
deoxy-myoglobin and then to oxymyoglobin (Livingston & Brown, 1981) and
the increase in free radicals (and pro-oxidants) due to lipid and protein
oxidation (Farouk & Swan, 1998). These factors all contribute to accelerated
oxidation of myoglobin post freezing/thawing and the consequent brown, dull
colour of the meat.

related to an increase in protein (and other solutes) concentration due to the

moisture loss.

During frozen storage (20 C) a portion of the water, termed unfrozen

water, does not freeze and is available for chemical reac-tions. The increase in
solute concentration due to the freezing out of the water fraction also
increases the chemical reactivity (Petrovi, 1982), thereby creating a
favourable environment for lipid and pro-tein oxidation reactions. Generally
lipid oxidation increases rapidly post-thawing as peroxidation (primary lipid
oxidation) occurs during frozen storage giving rise to rapid and severe
secondary lipid oxida-tion (thiolbarbituric acid forming) resulting in increased
TBARS (Owen & Lawrie, 1975). In this study, however there was no significant difference between the fresh and frozen/thawed samples as per-taining to
the measured TBARS measured immediately after thawing, most likely due to
the low lipid content naturally present in ostrich meat. However, in previous
studies (Leygonie, Britz, & Hoffman, 2011b; Leygonie et al., 2011a), the rate
of TBARS formation was accel-erated under a 10-day chilled shelf life study
in frozen/thawed ostrich meat compared to fresh meat packaged under
different modified at-mospheric conditions. Muela, Saudo, Campo, Medel
and Beltrn (2010) also noted an increase in the rate of TBARS formation as
the duration of freezing increased (in lamb).

Acknowledgements

Protein oxidation showed a very interesting phenomenon, the amount of

carbonyls detected increased significantly from the fresh to the frozen/thawed
samples but the amount of protein also increased significantly thus resulting in
the overall mM carbonyls/ mg protein to be less (P b 0.05) in the
frozen/thawed samples. The increase in carbonyls was expected (Leygonie et
al., 2011a) as the freezing and thawing treatments lead to structural changes in
the proteins through oxidative modification of the amino acid side chains,
presumably initiated by the peroxidation of the polyunsatu-rated fatty acids
(Estvez, 2011; Xiong, 2000). The oxidation of the proteins (mainly cysteine
and methionine as well as the basic amino acids such as lysine and arginine)
leads to the polymerisation of protein as well as peptide scission, which
destabilise the protein matrix leading to increased toughness, loss of water
binding capac-ity and loss in protein solubility (Estvez, 2011; Xiong, 2000).
The interaction between lipid and protein oxidation presumably leads to a
lower TBARS value as malondiadehyde (MDA) acts as a sub-strate in one of
the pathways of protein oxidation (Xiong, 2000). Thereby decreasing the level
of MDA in the meat, which could ex-plain the lack of a significant difference
in TBARS, an argument sup-ported by the higher carbonyl level. The only
unexplained result is the higher protein content in the frozen/thawed samples
during the analysis for protein oxidation. A possible explanation is that the
freezethaw cycles caused the protein structure to open more and thus allow
for better access of the cupric ions, from the copper sulphate in the BCA kit,
to bind at the existing peptide bonds. As the cupric ion reacts with four to six
peptide bonds to produce the col-our reaction (Voet & Voet, 2004). Therefore,
as more peptide bonds are exposed due to the loss in tertiary structure it
results in more cupric ions binding, thus producing a more intense colour
reaction that leads to a higher protein content estimation using the BCA kit.
Alternatively, the higher protein levels measured could be

5. Conclusion
The quality of ostrich meat is negatively affected by the freezing and
thawing regimes tested and currently used in the industry. The most
significant changes include the increase in toughness, loss of colour, increased
protein oxidation and moisture loss after freezing and thawing. These changes
may affect the consumer's repurchase behaviour. Further research is
imperative to establish if improved methods of freezing and thawing will
decrease the deterioration brought on by these processes.

The authors acknowledge Klein Karoo Ostrich Abattoir for donat-ing the
ostrich muscles. The Food Security program of the University of Stellenbosch
and FoodBev Seta are thanked for financial support. All the help from staff
and post graduate students from the Depart-ment of Animal Sciences and
Food Science at the University of Stellenbosch.

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