See discussions, stats, and author profiles for this publication at: https://www.researchgate.

net/publication/348933570

QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY,

COLOUR SPECTROPHOTOMETER, TEXTURE ANALYSER AND
PHYSICAL IMAGE ANALYSIS

Article in Journal of Sustainability Science and Management · January 2020

DOI: 10.46754/jssm.2021.11.010

CITATIONS READS

6 2,393

3 authors, including:

Saliza Asman
Tun Hussein Onn University of Malaysia
53 PUBLICATIONS 562 CITATIONS

SEE PROFILE

All content following this page was uploaded by Saliza Asman on 13 February 2021.

The user has requested enhancement of the downloaded file.

Journal of Sustainability Science and Management eISSN: 2672-7226
Volume 16 Number 1, January 2021: 103-119 © Penerbit UMT

QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY, COLOUR

SPECTROPHOTOMETER, TEXTURE ANALYSER AND PHYSICAL IMAGE
ANALYSIS
AINUR NALISA ABD RASHID1, FARIDAH KORMIN1 AND SALIZA ASMAN*2,3
1
Department of Technology and Natural Resources, 2Department of Physics and Chemistry, 3Advanced Analytical and
Environmental Chemistry (AdEC), Faculty of Applied Sciences and Technology, Universiti Tun Hussein Onn Malaysia,
Education Hub Pagoh, 84600, Pagoh, Johor, Malaysia.

*Corresponding author: [email protected]

Submitted final draft: 6 June 2020 Accepted: 13 June 2020 http://doi.org/10.46754/jssm.2021.01.010

Abstract: Assessment methods of meat such as physicochemical analyses and microbial

techniques are laborious and time-consuming. A rapid and non-destructive quality analysis
method of meat is needed and important to satisfy consumer demand. This study aims to
implement FT-IR spectroscopy, colour spectrophotometer, texture analyser and physical
image analysis to analyse the quality of raw, boiling and roasting meat. The FT-IR analysis
revealed the functional group for proteins, triglycerides, fatty acids and carbohydrates with
different intensities mostly focused at 3300 cm-1, 2967 cm-1, 1639 cm-1, 1546 cm-1, 1453
cm-1. Colour parameters showed slight alterations and partial degradation of some proteins
in meat was observed. L*, a* and b* for raw meats decreased, L* and b* for boiled and
roasted meats increased, and a* decreased. The texture analysis shows significant different
tenderness of meats and even cooking methods. Tenderness of raw meats decreased while
the cooked meats increased from the first until the fifth day. The image analysis shows
no significant changes in the meat textural surface. The findings show that the quality of
cooked meats was better than raw meats. The assessment methods applied can evaluate
the quality of meats and provide additional information on the physical changes of meat
composition and structure.

Keywords: Beef, chicken, FTIR, colour spectrophotometer, texture analyser,

physical image analysis.

Introduction traditional quality assessment methods of

Meat quality has become more significant meat are always implied such as by sensory
in meat industries as the rapid growth of evaluation of meats and microbial techniques
pathogenic bacteria within meats may form (Zhou et al., 2010). The most common detection
surface slime, degradation of structural method on quality assessment of meat is by
components, cause off-odours, off-flavours and using physicochemical analyses and microbial
change in meat appearance (Chen et al., 2020). techniques (Herrero et al., 2017). Nevertheless,
Spoilage and contamination of vulnerable meats these methods have a major limitation such as
can subsequently have effects on both producers being very laborious and time-consuming with
and consumers. For instance, contamination high cost needed as in requiring a tremendous
from pathogenic bacteria as well as fungal may amount of samples. Therefore, it is required
cause foodborne illnesses among consumers. to introduce a fast, cost-effective, reagent-free
According to Mutawakil (2011), the quality of and non-destructive methods to detect meat
meats can reduce quickly due to contamination spoilage effectively. In the last year, alternative
that may be caused by oxidation and enzymatic approaches based on vibrational spectroscopy
autolysis. have been developed.

Analysis of meat is much needed to ensure In this regard, Fourier Transform Infrared
the compliance of the legal quality assurance Spectroscopy (FT-IR) is used as a quick and non-
standard. The previous study has shown that invasive method for detecting meat spoilage.
Ainur Nalisa Abd Rashid et al. 104

FT-IR spectroscopy has shown its potential also were chosen: the boiling process represents
to predict any functional group changes in moist heat treatment and the roasting process
meat substrates and might extract valuable represents dry heat treatment to identify the
data regarding the muscle decomposition effect of cooking and processing with freezer
and substance generation due to the onset of storage on the quality of the meat. This study
spoilage (Rahman et al., 2016). Hence, FT-IR aims to use FTIR, colour spectrophotometer,
spectroscopy is believed to be one of the most texture analyser and physical image analysis to
effective methods for meat characterisation. analyse the quality of raw meat and cooked meat
The previous study showed the FT-IR analysis (beef and chicken) by different cooking methods
reveals the presence of absorbance bands of i.e., boiling and roasting processes.
proteins, triglycerides, fatty acids, and others
with different intensities according to meat type
Materials and Methods
and processing (Dixit et al., 2017).
Samples Preparation
Apart from that, meat quality is closely
related to its colour and texture. Colour plays Two types of meat samples were used, are
a vital role in determining the quality of meat beef chops and chicken breast meat with three
products (Jackman et al., 2011). Accordingly, different analyses involving raw meats, boiled
the colour spectrophotometer can be used to meats and roasted meats. Beef chops (m.
examine the quality of meat which will give longissimus dorsi) and chicken breast meat (m.
wavelength spectra analysis of the transmitted pectoralis major) were freshly bought from
characteristics of the samples directly. It can the slaughtermen. The preparation method was
provide enough data on colour values for any inspired by Sinanoglou et al., (2018). For raw
colour differences under a different light source. meat analysis, the raw meat was packed and
Standard meat colour measurement performed stored at -18 ºC of frozen storage. The boiled
by colorimeter gives the direct benefit of meats were prepared by boiling in hot water
tristimulus data (L* for lightness, a* for redness (100 ºC) for 30 minutes (25±5) for beef chops
and b* for yellowness). and 15 minutes (10±5) for chicken breasts. At
the end of every five minutes the extractive
Besides, the texture analyser can evaluate
substances produced by meats were removed
and distinguish the texture and tenderness of
from boiling water (Oz et al., 2016). The
all types of meats according to processing
roasted meats were cooked by using a kitchen
types. Tenderness of meat also is one of the
type oven. The meat samples were cooked when
most essential quality parameters that must
the oven temperature reached 200 ºC for 15
be taken seriously as too tough and soft meats
minutes and 9 minutes respectively. All cooked
may cause lower quality. Texture analysis of
meat samples were processed until the internal
meats focused on evaluating the tenderness or
core temperature of beef and chicken reached 77
toughness differences of meats with different
ºC (well-done) and 70 ºC respectively using a
types. Meanwhile, the study on the physical
digital thermometer (Oz et al., 2016; Utama et
image analysis can differentiate the texture and
al., 2018). The meat samples were packed and
surface appearances of meat samples.
stored in a sealed vacuum-packed and moisture
This study implements FT-IR, colour impermeable polyethylene plastics and stored at
spectrophotometer, texture analyser, and -4 ºC in a freezer for a five-day period. The meat
physical image methods to analyse beef samples were analysed for five days in a row
(m.longissimus dorsi) chops and chicken using FT-IR, colour spectrophotometer, texture
(m.pectoralis major) breast and their shelf-life analyser, while the physical image analysis was
at freezing temperature storage (0 ) for five used to study raw meat samples.
days. Two examples of the cooking method

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY, COLOUR SPECTROPHOTOMETER B

FTIR Characterisation Physical Image Analysis

All meat samples were cut into approximately Physical image analysis was determined by
0.001 g and were characterised by using UATR using a Canon digital camera by placing 3 cm ×
Two-FTIR spectrometer (Perkin Elmer) in the 2 cm (length × height) of raw meat samples (beef
absorbance mode of 4000 to 400 cm-1 at room and chicken meat) (Sinanoglou et al., 2018).
temperature (24 ºC). The spectra were triplicated
and recorded. Meat samples were analysed every
Results and Discussion
day in the five-day period. The characterisation
by FT-IR spectra was studied in two parts: (1) FTIR Characterization
differentiate types of meat samples based on All meat samples were analysed using FT-IR
main functional groups existence, (2) interpret spectroscopy in the mid-infrared region and
major and minor intensities of the obtained FT- wavelength of 4000 to 400 cm-1. Figures 1(a),
IR spectra based on increasing storage period 1(b) and 1(c) (in Appendix) show the FT-IR
(Sinanoglou et al., 2018). spectra of raw meats (beef and chicken), boiled
meats (beef and chicken) and roasted meats
Colour Measurement (beef and chicken), respectively. The purpose
All meat samples were weighed to is to determine the main functional groups that
approximately 5-10 g in individual sample existed and related to the compositional changes
cups. Meats were minced and compressed to of meats. Similar FTIR spectra showing a similar
obtain a smooth surface inside the cup and compositional of the nutritional content of meat
evaluated using a colour spectrophotometer samples was observed. The wide absorption
(Hunter Lab 4500L). Colour spectrophotometer band at the range of 3500 to 3000 cm-1 are is due
gave direct tristimulus of L* (lightness), a* to O-H and N-H symmetric stretching vibration
(redness) and b* (yellowness) values. L* of alcohols and amide or proteins, respectively.
signifies the lightness of the color, a* represents Besides, a strong band at 3300 cm-1 is referred
a measurement from red (+) to green (-) colour, to as amide A and amide B bands. The amide
and b* represents a measurement from yellow A band is contributed to the N-H vibration,
(+) to blue (-) colour. The obtained tristimulus and the amide B band is the first overtone of
data were triplicated and expressed in mean ± amide II vibration. The changes in this range of
standard deviation. wavelengths are related to changes in structural
secondary protein within meats. These findings
are similar to Sinanoglou et al. (2018), Petracci
Texture Analysis
& Berri (2017) and Barth (2007).
All meat samples were cut into small cubes with
measurement of 2 cm × 2 cm × 2 cm (height The weak absorptions bands at 2950 to
× width × length) and analysed using a texture 2850 cm-1 are related to methyl and methylene
analyser (Stable Micro System TA.XT Plus). groups’ asymmetric and symmetric stretching of
The texture analyser was calibrated first and the the carbonyl group of triglycerides’ ester bond.
meats were loaded in the T.A. System Software. These bands were the most significant in roasted
The meat samples were placed parallel to the meats and slightly intense in boiled meats. It
surface of the penetration point. The probe shows that higher heating treatment causes more
chosen was flat-faced cylindrical probe 5 mm, intense at 2950 to 2850 cm-1 as roasting used
with pre-test speed of 10 mm/sec, test speed of higher temperatures during the cooking process.
2 mm/sec and post-test speed of 10 mm/sec. The The strong and sharp absorption band at the
data of hardness or force required to compress range of 1640 to 1634 cm-1 can be described as
samples were triplicated (Peleg, 2019). The C=O stretching vibration of amides I. This peak
results of texture profile analysis (TPA) were is correlated with proteins adopting with β-sheets
triplicated and averaged with standard deviation. conformation and strong water absorption

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
Ainur Nalisa Abd Rashid et al. 106

which will significantly overlap the amide I groups (Herrero et al., 2017). Ammor et al.,
band (Herrero et al., 2017; Papadopoulou et al., (2009) found that the minor intensity peaks
2011). The strong water absorption indicates the observed at 1458 cm-1 are related to scissoring
high moisture content of meat that influences the of CH2 of fats. Moreira and co-workers (2018)
protein structure. The strong water absorptions proved that absorption bands at 1458 cm-1 are
will cause the meat to deuterate to prevent the due to C-H bending and stretching of methylene
protein structural changes. Despite the amide (CH2) and methyl (CH3) groups present in fats
I band, the amide II band can determine the within the meat. Minor peaks at 1398 cm-1
protein structural changes due to the intrusion and the peak at 1315 to 1303 cm-1 are related
of water bending at 1640 cm-1. The amide I to stretching of C-N and C-O, bending of N-H
absorption band which characterises the protein and O=C-N bending of amide III. The minor
secondary structure is located in the region of intensity peak observed at 1170 to 1154 cm -1 is
1648 to 1658 cm-1 and 1620 to 1640 cm-1 are attributed to the C-O stretching of proteins and
associated with the α-helix and the β-sheet triglycerides. The region can also be associated
protein structure, respectively (Yu., 2005). with C-O and C-C stretching vibrations due
Therefore, the major protein structure content to the presence of carbohydrates. At 1240
of both beef and chicken samples is β-sheet. and 1083 cm-1, there are P=O symmetric and
Another sharp absorption band can be identified asymmetric which contributed to phospholipids
in the range of 1546 to 1550 cm-1. This is the and nucleic acids. The absorption band at 1080
combined vibration of the amino group (N-H) cm-1 contributed as carbohydrate moieties and
bending with the C-N stretching of proteins. The in the case of meats, it can represent glycogen
peak at 1543 cm-1 represented C=O stretching (Sinanoglou et al., 2018). Table 1 tabulated the
band and the scissoring band of CH2 groups. summary of functional groups corresponding to
A similar result was observed by Herrero et al. the FTIR spectra for all meat samples.
(2017), where the strong absorption bands are Furthermore, the spectra of meat samples
affected by the amino group and the carbonyl showed the absorbance bands of higher
group of proteins. intensities at 3500 to 3000 cm-1, 2950 to 2920
The weak absorbance bands at 1453 to cm-1, 2852 and 1744 cm-1. It seems that beef
1399 cm-1 are related to the C-H bending of meat has a higher lipid content compared to
alkyl chain methylene of lipid moieties. It also chicken meat as the beef spectra show higher
corresponds to C-H asymmetric and symmetric intensities than chicken meat spectra. Moreover,
stretching vibrations of protein moieties, the band at 3500 to 3000 cm-1 is associated
respectively. Additionally, bands appearing in with the vibration of the olefin group, which is
1400 to 1200 cm-1 region can be attributed to characterised by the higher content of unsaturated
bending vibrations of CH2 and CH3 aliphatic fatty acids (Guntarti et al., 2015). Additionally,

Table 1: Summary of functional groups in meat samples

Wavenumber (cm-1) Functional groups

3500-3000 O-H, N-H symmetric stretching vibration of alcohols & amide of proteins, strong
water absorption, O-H
3300 Amide A and amide B
2950-2850 Methyl & methylene of C=O of triglycerides
1634-1640 C=O stretching vibration of amides
1546-1550 C=O stretching & scissoring band of CH
2

1240 P=O symmetric & asymmetric of phospholipids & nucleic acids

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY, COLOUR SPECTROPHOTOMETER B

beef meat has higher protein content than other intensities peak at 1550-1540 cm-1 is
chickens, as the spectra of beef showed higher probably due to the presence of partial protein
intensities at 1450, 1395, and 1170 to 1154 cm-1 rupture representing the stretching vibration of
than the ones of the chicken meat samples. In C=O and bending vibration of N-H (Yu, 2005).
this sense, the adsorption bands at 1627 and The decreasing of minor intensities peaks
1541 cm-1, which are characteristics of the between 1450-1440 cm-1 and 1399-1395 cm-1
protein exhibited a higher signal in the spectra within five days corresponds to the reducing
of beef meat than in those of the chicken ones. A of C-H bending of alkyl chain methylene
similar observation was found by Sinanoglou et of lipid moieties and C-H asymmetric and
al (2018) who studied on turkey and pork hams. symmetric stretching vibrations of protein
The spectra of the chicken obtained significantly moieties respectively. Meanwhile, the reducing
higher intensities at 1040 to 1020 cm -1 than the intensities at 1245 to 1240 cm-1 marginally
beef, which is indicative of higher carbohydrate throughout freezing storage indicates that P=O
content. absorption of nucleic acids reluctantly decreased
due to freezing storage (Rahman et al., 2018)
Effect of Frozen Storage Towards Meat Quality and followed with slightly reducing intensities
by FT-IR Interpretation peak at 1174 to 1165 cm-1 and 1082 to 1075 cm-1
as an increasing storage period. The intensity of
To monitor the quality of all meat in frozen
1174 to 1165 cm-1 decreased from day 1 to day
storage, a comparative analysis was carried out
2 but remained constant in the next remaining
where the meat samples were analysed every
three days. The intensities are associated with
day in a five-day period. The analysis comprises
C=O and C-O stretching of carbonyl and ether
of the selected range of wavelengths consisting
bonds of triglycerides and the decrease probably
of significant intensity peaks for all types of
means lessening of the triglyceride content in
different samples that were used.
meat samples (Sinanoglou et al., 2018).
Based on Figures 2(a) and 2(b) (Appendix),
Figures 2(c) and 2(d) (Appendix) show the
it can be observed that the FTIR spectra of
difference of FTIR spectra interpretation for
raw meat samples (beef and chicken) showed
boiled meats. It shows that as days of frozen
a significant decrease at 3500-3000 cm-1. The
storage increased, boiled meat samples did
bands are correlated with olefin group vibration
not experience any significant changes in their
which indicates unsaturated fatty acid contents
chemical properties. Most of the intensity peaks
(Sinanoglou et al., (2018). The decrease in those
from 3500 to 3000 cm-1, 1634 to 1630 cm-1
absorbance bands confirmed that there is a partial
and 1550 to 1540 cm-1 in both meat samples
reduction of unsaturated fatty acids within meat
showed stagnant in those five days of storage
samples. The slightly increased intensities at
where all of the chosen intensity peak range did
2990-2880 cm-1 from Day 1 to Day 5 in raw meat
not show any extreme differences or changes
samples correspond to methyl and methylene
in those five days. This can also be seen in the
groups’ asymmetric and symmetric stretching
FTIR spectra interpretation of roasted meats
of fatty acids. These changes may suggest that
in Figures 2(e) and 2(f) (Appendix) where it
there is a degradation of triglycerides and an
exhibited a stationary intensity peak within five
increase in the hydrolysis process resulting in
days of frozen storage. However, at 2990-2880
the accumulation of free fatty acids. The freezing
cm-1, roasted meats exhibit a higher absorbance
storage may suppress triglycerol acyl hydrolases
than in the boiled meats. In this case, there was
that activate lipid hydrolysis, arising to free fatty
a higher chance for a high amount of carbonyl
acids, dimonoglycerides and monoglycerides
group methyl and methylene stretching in
(Liu & Kokare, 2016).
roasted meats. There were no previous findings
Moreover, the decrease at the intensity for this comparative analysis of boiled meat
peaks of 1634-1630 cm-1 followed with the and roasted meat in frozen storage. However, it

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
Ainur Nalisa Abd Rashid et al. 108

can be concluded that frozen storage of cooked from Day 1 where 6.82 ± 0.015 (raw beef) and
meat does not give any effects to its chemical 14.90 ± 0.021 (raw chicken) until Day 5 where
properties. The cooking of meats would retain the 4.08 ± 0.046 (raw beef) and 11.56 ± 0.090 (raw
quality of meats by un-disturbing the chemical chicken), respectively.
composition of meats thus maintaining the shelf Besides that, the L* values of boiled meat
life of meats compared to the unprocessed meats. showed an increase from Day 1 to Day 5. The L*
Table 2 tabulated the summarisation of intensity values of boiled meats are 43.98 ± 0.030 (boiled
peak changes towards the frozen storage effect. beef) and 72.41 ± 0.040 (boiled chicken) in Day
1 and increased to 44.83 ± 0.020 (boiled beef)
Colour Measurement and 74.64 ± 0.040 (boiled chicken) in the Day
The colour measurement of meat samples was 5. The increase was also shown in b* value of
analysed using a colour spectrophotometer. both boiled meat samples, where 10.30 ± 0.300
Table 3 shows the values of the tristimulus of (boiled beef) and 15.95 ± 0.040 (boiled chicken)
L* (lightness), a* (redness) and b* (yellowness) in Day 1 to 10.66 ± 0.010 (beef boiled) and 16.47
of meat samples within a five-day period frozen ± 0.290 (chicken boiled) in Day 5, respectively.
storage. It shows that the values of L* in all raw However, a* values for boiled meats decreased
meat samples were significantly higher in Day 1 from Day 1, with values of 6.96 ± 0.006 (boiled
compared to Day 5. The L* values in Day 1 of beef) and 2.35 ± 0.010 (boiled chicken) to
raw beef and chicken meats are 38.63 ± 0.230 5.84 ± 0.010 (boiled beef) and 1.63 ± 0.020
and 63.35 ± 0.044, respectively. Eventually, both (boiled chicken) at Day 5. The roasted meats
samples exhibit a slight decrease in L* values also showed an increase of colour parameters
until Day 5 of frozen storage, where the L* L* with 40.74 ± 0.060 (roasted beef) and 70.32
values are decreased to 34.79 ± 0.089 (raw beef) ± 0.090 (roasted chicken) in Day 1 to 42.30 ±
and 58.99 ± 0.116 (raw chicken), respectively. A 0.040 (roasted beef) and 71.12 ± 0.040 (roasted
decrease of a* values of meat samples was from chicken) in Day 5. There are decreases in a*
Day 1 which exhibited 11.71 ± 0.026 (raw beef) values from Day 1 to Day 5 with values of 0.35
and 8.91 ± 0.021 (raw chicken), and on the 5th ± 0.010 to 0.022 ± 0.010 for roasted beef, and
day exhibited 10.36 ± 0.120 (raw beef) and 7.3 1.54 ± 0.020 to 1.10 ± 0.050 for roasted chicken,
± 0.050 (raw chicken). Likewise, the b* values respectively. While b* values of roasted meats
showed a similar trend with a slight reduction showed a slight increase from Day 1 to Day 5
Table 2: Changes in intensity peak in a five-day storage

Wavenumber (cm-1) Functional groups Interpretation

3500-3000 O-H, N-H Decrease in unsaturated fatty acid contents;
partial reduction of unsaturated fatty acids within meat
samples
2990-2880 Methyl & Increase in the?? represents fatty acids
methylene of C=O Degradation of triglycerides & increase of hydrolysis
process resulting in the accumulation of free fatty acids
1634-1630 C=O Represent partial protein rupture
1550-1540 C=O Represent partial protein rupture
1450-1400 C-H Decrease in lipid moieties
1399-1395 C-H Decrease in protein moieties
1245-1240 P=O Decrease of nucleic acids
1174-1165 C=O Decrease of triglycerides
1082-1075 C-O Decrease of triglycerides

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY, COLOUR SPECTROPHOTOMETER B

with 10.93 ± 0.050 (roasted beef) and 13.12 ± resulting in lower surface light reflectivity
0.090 (roasted chicken) to 11.73 ± 0.007 (roasted (Hughes et al., 2014).
beef) and 13.72 ± 0.030 (roasted chicken). It The colour of meat samples can be also
can be simplified that the L*, a* and b* values affected by the cooking method. The boiling
of raw meats decreased from Day 1 until Day method is one of many cooking methods
5. The boiled and roasted meats exhibited an preferred by meat consumers. The colour of
increase in L* and b*values but a decrease in the boiled sample did not show any significant
a* values within five days of storage. It can be difference within five days of storage. However,
revealed that the L* and b* values of raw meats it can be seen that the L* and b* parameters
are lower than boiled and roasted meats, while for boiled and roasted meats are higher than
a* values of raw meats were significantly higher the raw meats (Table 3), while a* values of
than the boiled and roasted meats. The results boiled and roasted meats are lower than the raw
and findings for cooked meat correspond to the meats. During the time of cooking the meat, the
findings of Oz, et al. (2016). globin gives the colour to fresh meat denatured
The reduction L*, a* and b* values of raw forming haemoglobin (Aberle et al., 2001).
meats from Day 1 until Day 5 are correlated This leads to subsequent decrease in a* values.
with myoglobin content in meat muscle. Meat Besides, a lower average of L* values in roasted
colour in both white meat and red meat is meat was correlated with dry heat treatment
mostly determined by the amount of myoglobin, applied while a higher average of L* values
haemoglobin and cytochrome C catalase in in boiled meat represents moist heat treatment
skeletal muscle (Nathan et al., 2016; Yu et al., (Oz and Zikirov, 2015; Utama et al., 2018). The
2017). However, 80 to 90 % of meat colour decrease in a* value of roasted and boiled meat
depends on myoglobin content. Frozen storage indicates the denaturation of myoglobin content
and increasing shelf life of meat samples may as it is usually correlated with the amount of
give an impact on the stability of myoglobin oxymyoglobin. Therefore, a decrease in a* value
content. It can also be described that after also indicates the denaturation the myoglobin
freezing storage meat for a long time, a high pigments. Similar findings were obtained by
concentration of metmyoglobin gives the meat Sanzhez del Pulgar et al. (2012) as their research
an undesirable brown colour and lessens the red also obtained a decrease in a* values of beef.
colour of meat. This is the cause of changes of Choi et al., (2016) also obtained similar results
both a* and b* values of meat samples. Similar for boiled chicken breast meats. The increased
results have been found with frozen storage of b* values of boiled and roasted meats are noted
fresh beef (Pietrasik & Janz, 2009), poultry meat more than raw meat samples and this indicates
(Leygonie et al., 2012) and fresh lamb (Belles yellow colour intensity. The yellow colour on
et al., 2018). The colour changes that occur meat is still unexplained. However, findings
are caused by the deterioration of the globin by Wei et al., (2017) also have shown similar
moiety of myoglobin during storage. Myoglobin results, where the b* value increased and was
will be more susceptible to autoxidation when correlated with increased lipid oxidation.
deterioration occurs, leading to a subsequent
Based on the findings, it shows that the
amount of discoloration within the meat. The
value of L*, a* and b* of raw meat samples
accumulation of metmyoglobin within meat
decreased from Day 1 of frozen storage until
during storage can explain the reduction of a*
Day 5 These changes were caused by the effect
value of meat samples (Bekhit et al., 2007).
of frozen storage on the raw meat samples. The
Changes in b* values are mostly caused by
L*, a* and b* values of boiled meat samples
the metmyoglobin content as well and lipid
during the five days of storage did not give
oxidation (Xiong, 2000), while the decreasing
any significant difference. This shows that the
L* value is caused by decreased water retention,
colour measurement of boiled and roasted meat

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
Ainur Nalisa Abd Rashid et al. 110

Table 3: Colour measurement values (L*, a*, b*) of raw, boiled and roasted beef and chicken meats

Raw Beef
Time (day) L* a* b*
1 38.63 ± 0.230 11.71 ± 0.026 6.82 ± 0.015
2 37.79 ± 0.220 11.37 ± 0.015 5.03 ± 0.017
3 37.18 ± 0.046 11.24 ± 0.034 4.91 ± 0.023
4 36.79 ± 0.075 10.87 ± 0.110 4.72 ± 0.026
5 34.79 ± 0.089 10.36 ± 0.120 4.08 ± 0.046
Raw Chicken
Time (day) L* a* b*
1 63.35 ± 0.044 8.91 ± 0.021 14.90 ± 0.021
2 62.53 ± 0.100 7.72 ± 0.050 12.88 ± 0.040
3 61.56 ± 0.030 7.66 ± 0.005 12.64 ± 0.010
4 59.03 ± 0.006 7.45 ± 0.04 11.82 ± 0.060
5 58.99 ± 0.116 7.30 ± 0.05 11.56 ± 0.090
Boiled Beef
Time (day) L* a* b*
1 43.98 ± 0.030 6.96 ± 0.006 10.30 ± 0.300
2 44.00 ± 0.140 6.79 ± 0.006 10.66 ± 0.010
3 44.47 ± 0.050 6.68 ± 0.050 11.01 ± 0.150
4 44.71 ± 0.020 6.49 ± 0.020 11.12 ± 0.040
5 44.83 ± 0.020 5.84 ± 0.010 11.66 ± 0.010
Boiled Chicken
Time (day) L* a* b*
1 72.41 ± 0.040 2.35 ± 0.010 15.95 ± 0.040
2 72.47 ± 0.120 2.24 ± 0.050 16.12 ± 0.030
3 72.94 ± 0.050 2.06 ± 0.030 16.44 ± 0.006
4 73.88 ± 0.020 1.66 ± 0.006 16.46 ± 0.020
5 74.64 ± 0.040 1.63 ± 0.020 16.47 ± 0.290
Roasted Beef
Time (day) L* a* b*
1 40.74 ± 0.060 0.350 ± 0.010 10.93 ± 0.050
2 41.77 ± 0.050 0.032 ± 0.010 10.87 ± 0.010
3 41.81 ± 0.010 0.029 ± 0.030 11.38 ± 0.030
4 41.80 ± 0.030 0.025 ± 0.010 11.69 ± 0.040
5 42.30 ± 0.040 0.022 ± 0.010 11.73 ± 0.070
Roasted Chicken
Time (day) L* a* b*
1 70.32 ± 0.090 1.54 ± 0.020 13.12 ± 0.090
2 70.51 ± 0.070 1.49 ± 0.010 13.57 ± 0.010
3 70.75 ± 0.020 1.35 ± 0.010 13.62 ± 0.030
4 70.87 ± 0.050 1.27 ± 0.030 13.67 ± 0.010
5 71.12 ± 0.040 1.10 ± 0.050 13.72 ± 0.030

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY, COLOUR SPECTROPHOTOMETER B

samples was not affected by frozen storage but crystals will attract water from intracellular to
mostly by the cooking method treatment. The intercellular spaces leading to an excessive loss
reasons are probably due to the denaturation of moisture during the thawing process. The
of myoglobin during cooking resulting in no damaged muscle fibres do not reabsorb water
further changes exhibited during the frozen upon thawing, thus a further loss of moisture
storage of cooked meats. The slight changes are to occurs. Wang et al (2020) stated that the
increased in L* and b* and decreased in a* in tenderness of meats is affected mostly by the
both boiled and roasted meat samples, perhaps formation of ice crystals similar to this finding.
as a result of freeze burn exhibit by meats. This As a consequence, the texture of meat may
finding supported FTIR analysis. To summarise, deteriorate due to an increase in the affluence
the raw meats indicate the colour changes of water-soluble nutritional components and
which represent the differences in meat quality also decrease the water holding capacity (WHC)
freshness. The colour of raw meats decreased of meat (Cho et al., 2014; Lagerstedt et al.,
and this shows the reduction of raw meats 2008). In conformance with Huff-Lonergan
quality compared to the cooked meats. & Lonergan (2005), as stated that water loss
is directly proportional to the WHC of muscle
Texture Profile Analysis meat.
The mechanical and geometrical texture For boiled and roasted meat samples, with
attributes of meats were evaluated using a increasing frozen storage, the force needed was
texture analyser. The TPA was carried out to increased. Boiled meats exhibited an increase in
analyse the tenderness of meat samples. The tenderness from Day 1 until Day 5 with 9.56 ±
results of the meat samples are shown in Table 0.001 N (boiled beef) to 10.12 ± 0.08 N (boiled
4. Force needed to compress raw meat samples beef) and 9.45 ± 0.030 N (boiled beef) to 9.96
in Day 1 is higher than the raw meat samples ± 0.020 N (boiled chicken). Similarly, roasted
in Day 5, recorded with 8.25 ± 0.030 N (raw meats also display similar findings with an
beef) to 7.89 ± 0.050 N (raw beef) and 7.45 ± increase in tenderness from Day 1 until Day 5.
0.010 N (raw chicken) to 6.74 ± 0.012 N (raw Roasted beef showed a total of 10.26 ± 0.020 N
chicken), respectively. This indicates that as and the roasted chicken exhibited the total force
the storage period increased, the force needed of 10.21 ± 0.030 N on Day 1. Both exhibited an
for the compression of all raw meat samples increase in tenderness on the last day with 11.35
decreased. The decline in force required was ± 0.050 N for roasted beef and 10.61 ± 0.060 N
due to an increase in deterioration in the protein for roasted chicken, respectively. These findings
structure of raw meats. were comparable to findings of Choi et al.
(2016), in that increased tenderness is obtained
As reported by Rhee et al. (2004), tenderness
for dry heat than moist heat treatment of meats.
of meat may result from the degradation of
structural proteins or protein patterns during The results of tenderness for cooked meats
freezing storage. Myosin degradation within are higher than raw meats due to the toughening
meat muscle proteins is the main factor that of muscle fibres and tenderness of connective
may affect meat tenderness. Frozen storage tissue. Changes can occur in actin and myosin
also caused ice crystal formation within meat muscle fibre protein when heating. The peptide
muscles, thus affecting meat tenderness. When chains of amino acids undergo deformation and
the ice crystal formed within meat muscles, then reformed or coagulate back. This results in
desiccation of the protein cell membrane will moisture loss and toughening of muscle fibres.
occur (Kang et al., 2014). The ice crystals may However, it has been shown that moist heat
destroy the structure of meat as the water was gave a tenderising effect on connective tissue as
frozen leading to a high concentration of solutes a result of the alteration of collagen to gelatine.
within the protein structure of meats. The ice When heat is applied, collagen converted into

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
Ainur Nalisa Abd Rashid et al. 112

Table 4: Texture profile analysis (TPA) of raw, boiled and roasted beef and chicken meats

Time of Force (N)

Frozen
Storage Raw Raw Boiled Boiled Roasted Roasted
(Day) beef chicken beef chicken beef chicken
1 8.25 ± 0.030 7.45 ± 9.56 ± 9.45 ± 10.26 ± 0.020 10.21 ± 0.030
0.010 0.001 0.030
2 8.21 ± 0.040 7.40 ± 9.67 ± 9.53± 0.090 10.59 ± 0.010 10.32 ± 0.010
0.012 0.020
3 8.15 ± 0.070 7.29 ± 9.85 ± 9.78 ± 10.65 ± 0.040 10.46 ± 0.050
0.012 0.060 0.010
4 8.12 ± 0.010 6.89 ± 9.96 ± 9.83 ± 10.87 ± 0.030 10.53 ± 0.010
0.012 0.010 0.030
5 7.89 ± 0.050 6.74 ± 10.12 ± 9.96 ± 11.35 ± 0.050 10.61 ± 0.060
0.012 0.08 0.020

water-soluble gel and muscle softens. A high Physical Image Analysis

softened connective tissue can be obtained by Figures 3(a) and 3(b) (Appendix) show the
using moist heat treatment. Besides that, the images of raw beef and chicken meat surfaces
harder texture of dry heated meat represents in Day 1 and Day 5. The images were taken
the denaturation of intramuscular collagen or to analyse any significant changes in the meat
changes in myofibrillar structure. muscles. There was no significant difference
In conformance with that, Kaur et al. (2020) in meat muscles on the first day and the fifth
stated that denaturation of myofibrillar protein day due to the low magnification of the digital
leads to meat toughening while tenderisation camera used. However, according to Kim et al.
is caused by the solubilisation of connective (2015), the analysis of a meat structure using
tissue. This explained the higher average force the hyperspectral image can show a significant
in roasted meats than boiled meats. Freezing or change occurring during frozen storage. This
frozen storage may also affect the tenderness of might be due to frozen storage during those five
cooked meat. However, it is not as obvious as days, indicating that ice crystal formation affects
raw meat samples. Cooked meat has achieved the muscle fibres in beef and chicken meat. As
its best tenderness resulting from the cooking reported by Hong et al., (2005), frozen storage
method. Frozen-thawed cooked meats would can result in the destruction of muscle fibres due
not impact meat tenderness (Liu et al., 2020). to the formation of ice crystals of various sizes
The slight changes in the tenderness of meat according to the freezing rate. A faster freezing
in Table 4 probably indicate the ice crystal rate results in smaller ice crystals while slower
formation during frozen storage. It shows freezing rate leads to a bigger size of ice crystal
different tenderness of raw and cooked meats formation. The larger the size of ice crystal,
which is decreases and increases respectively the more damage it can do to the meat muscle
due to the treatment process. In conclusion, this fibres. A smaller ice crystal formation will cause
texture analysis is correlated with FTIR and less physical damage to meat components while
colour measurement analysis. It inferred that larger ones interrupt the muscle cells and cause
the freshness of meat quality could be easily exudation. Other than freezing, thawing has
analysed. been proven to give effects on muscle fibres of
meats. According to Taher and Farid (2001),
minimum thawing can reduce degradation in
quality of meats.

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY, COLOUR SPECTROPHOTOMETER B

Conclusion Barth, A. (2007). Infrared Spectroscopy of

This study was successfully implemented using Proteins. Biochimica et Biophysica Acta
the rapid and ease analysis methods, FT-IR (BBA) - Bioenergetics, 1767(9), 1073-
spectroscopy, color spectrophotometer, texture 1101. doi:https://doi.org/10.1016/j.bbabio.
analyser and physical image analysis for raw 2007.06.004
and cooked meats via boiling and roasting Bekhit, A. E. D., Cassidy, L., Hurst, R. D.,
cooking methods throughout the five days of & Farouk, M. M. (2007). Post-Mortem
frozen storage. The FTIR analysis shows that Metmyoglobin Reduction in Fresh Venison.
there are significant changes in the composition Meat Science, 75(1), 53-60. doi:https://doi.
of raw meat samples compared to cooked meat org/10.1016/j.meatsci.2006.06.015
samples. The color measurement showed such Bellés, M., Leal, L. N., Díaz, V., Alonso, V.,
substantial changes in meat samples within five
Roncalés, P., & Beltrán, J. A. (2018). Effect
days, where the freezing storage caused slight
of Dietary Vitamin E on Physicochemical
alterations for the colour parameters and partial
and Fatty Acid Stability of Fresh and
degradation of some proteins in meat. The
Thawed Lamb. Food Chemistry, 239, 1-
texture analysis shows significant difference
8. doi:https://doi.org/10.1016/j.
in tenderness with different types of meat and
foodchem.2017.06.076
cooking methods. However, the image analysis
shows no significant changes in the textural Cheah, J. C. (2016). Protein Thaw Loss in Meat
surface of meat due to the conventional image Systems: Biochemical Influence Towards
analysis. It can be summarised that those Meat Authentication of Fresh Versus
methods applied were able to evaluate the Thawed.
differences in the quality of raw and cooked Chen, S. H., Fegan, N., Kocharunchitt, C.,
meats instead by of using laborious, costly and Bowman, J. P., & Duffy, L. L. (2020).
time-consuming analysis methods. Changes of the Bacterial Community
Diversity on Chicken Carcasses Through an
Acknowledgements Australian Poultry Processing Line. Food
Microbiology, 86, 103350. doi:https://doi.
The authors would like to thank the Faculty of org/10.1016/j.fm.2019.103350
Applied Sciences and Technology, Universiti
Tun Hussein Onn Malaysia for providing the Cho, S., Kang, G., Seong, P., Park, K., Kim,
facilities. Y., Park, B., & Kang, S. M. (2014). Effect
of Thawing Method on Water-soluble
Nutritional Components and Quality
References Properties of Hanwoo Beef.
Aberle, E. D., Forrest, J. C., Gerrard, D. E. & Choi, Y.-S., Hwang, K.-E., Jeong, T.-J., Kim, Y.-
Mills, E.W. (2001). Principles of Meat Sci- B., Jeon, K.-H., Kim, E.-M., Sung J-M., Kim
ence. 4th edition. Kendall/Hunt Publishing H-W., & Kim, C.-J. (2016). Comparative
Corporation. Dubuque, Iowa. Study on the Effects of Boiling, Steaming,
Ammor, M. S., Argyri, A., & Nychas, G.-J. E. Grilling, Microwaving and Superheated
(2009). Rapid Monitoring of The Spoilage of Steaming on Quality Characteristics of
Minced Beef Stored Under Conventionally Marinated Chicken Steak. Korean Journal
and Active Packaging Conditions Using for Food Science of Animal Resources,
Fourier Transform Infrared Spectroscopy 36(1), 1-7. doi:10.5851/kosfa.2016.36.1.1
in Tandem With Chemometrics. Meat Dixit, Y., Casado-Gavalda, M. P., Cama-
Science, 81(3), 507-514. doi:https://doi. Moncunill, R., Cama-Moncunill, X.,
org/10.1016/j.meatsci.2008.10.015 Markiewicz-Keszycka, M., Cullen, P. J.,

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
Ainur Nalisa Abd Rashid et al. 114

& Sullivan, C. (2017). Developments and the Activities of Antioxidant Enzyme and
Challenges in Online NIR Spectroscopy for Lysosomal Enzymes of the Longissimus
Meat Processing. Comprehensive Reviews dorsi Muscle from Hanwoo (Korean
in Food Science and Food Safety, 16(6), Cattle) in Various Freezing Conditions.
1172-1187. doi:10.1111/1541-4337.12295 Korean Journal for Food Science of Animal
Guntarti, A., Martono, S., Yuswanto, A., & Resources, 34(6), 742-748. doi:10.5851/
Rohman, A. (2015). FTIR Spectroscopy kosfa.2014.34.6.742
in Combination with Chemometrics for Kaur, L., Hui, S. X., & Boland, M. (2020).
Analysis of Wild Boar Meat in Meatball Changes in Cathepsin Activity during
Formulation. Asian Journal of Biochemistry, Low-Temperature Storage and Sous Vide
10, 165-172. doi:10.3923/ajb.2015.165.172 Processing of Beef Brisket. Food science
Herrero, A. M., Carmona, P., Jiménez- of animal resources, 40(3), 415-425.
Colmenero, F. and Ruíz-Capillas, C. (2010). doi:10.5851/kosfa.2020.e21
Applications of Vibrational Spectroscopy Lagerstedt, Å., Enfält, L., Johansson, L., &
to Study Protein Structural Changes in Lundström, K. (2008). Effect of Freezing
Muscle and Meat Batter Systems. In on Sensory Quality, Shear Force and Water
Handbook of Vibrational Spectroscopy Loss in Beef M. longissimus dorsi. Meat
(eds J.M. Chalmers and P.R. Griffiths). Science, 80(2), 457-461. doi:https://doi.
doi:10.1002/0470027320.s8949 org/10.1016/j.meatsci.2008.01.009
Hong, G. P., Park, S. H., Kim, J. Y., Lee, S. Leygonie, C., Britz, T. J., & Hoffman, L. C.
K., & Min, S.-G. (2005). Effects of Time- (2012). Meat Quality Comparison Between
Dependent High Pressure Treatment on Fresh and Frozen/Thawed Ostrich M.
Physico-Chemical Properties of Pork. Food iliofibularis. Meat Science, 91(3), 364-
science and biotechnology, 14, 808-812. 368. doi:https://doi.org/10.1016/j.meatsci.
Huff-Lonergan, E., & Lonergan, S. M. (2005). 2012.02.020
Mechanisms of Water-Holding Capacity Liu, J., Ellies-Oury, M.-P., Chriki, S., Legrand,
of Meat: The Role of Postmortem I., Pogorzelski, G., Wierzbicki, J., Farmer,
Biochemical and Structural Changes. Meat L., Troy, D., Polkinghorne, R., & Hocquette,
Science, 71(1), 194-204. doi:https://doi. J.-F. (2020). Contributions of Tenderness,
org/10.1016/j.meatsci.2005.04.022 Juiciness and Flavor Liking to Overall
Hughes, J. M., Oiseth, S. K., Purslow, P. P., Liking of Beef in Europe. Meat Science,
& Warner, R. D. (2014). A Structural 168, 108190. doi:https://doi.org/10.1016/j.
Approach to Understanding the Interactions meatsci.2020.108190
between Colour, Water-Holding Capacity Liu, X., & Kokare, C.R. (2016). Chapter 11
and Tenderness. Meat Science, 98(3), 520- Microbial Enzymes of Use in Industry.
532. doi:https://doi.org/10.1016/j. Mancini, R. A., Kropf, D. H., Hunt, M. C., &
meatsci.2014.05.022 Johnson, D. E. (2005). Effects of Endpoint
Jackman, P., Sun, D.-W., & Allen, P. (2011). Temperature, pH, and Storage Time on
Recent Advances in the Use of Computer Cooked Internal Color Reversion of Pork
Vision Technology in The Quality Longissimus Chops. Journal of Muscle
Assessment of Fresh Meats. Trends in Foods, 16(1), 16-26. doi:10.1111/j.1745-
Food Science & Technology, 22(4), 185- 4573.2004.07103.x
197. doi:https://doi.org/10.1016/j.tifs.2011. Mi, Y., Bo, S., Il, K., Min, S.-G., SangYoon, L.,
01.008 Ji, J., & Jung, C. (2015). Effects of Various
Kang, S. M., Kang, G., Seong, P.-N., Park, B., Freezing and Thawing Techniques on Pork
Kim, D., & Cho, S. (2014). Evaluation of Quality in Ready-To-Eat Meals. African

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY, COLOUR SPECTROPHOTOMETER B

Journal of Food Science, 9, 525-533. Analysis for Predicting Poultry Meat

doi:10.5897/AJFS2015.1358 Spoilage. PeerJ, 6, e5376.
Mutwakil, M. (2011). Meat Spoilage Mechanisms Rahman, U. u., Shahzad, T., Sahar, A., Ishaq,
and Preservation Techniques: A Critical A., Khan, M. I., Zahoor, T., & Aslam, S.
Review. American Journal of Agricultural and (2016). Recapitulating the Competence
Biological Sciences, 6, 486-510. doi:10.3844/ of Novel & Rapid Monitoring Tools for
ajabssp.2011.486.510 Microbial Documentation in Food Systems.
Oz, F., & Zikirov, E. (2015). The Effects of Sous- LWT - Food Science and Technology,
Vide Cooking Method on the Formation 67, 62-66. doi:https://doi.org/10.1016/j.
of Heterocyclic Aromatic Amines in lwt.2015.11.041
Beef Chops. LWT - Food Science and Rhee, M. S., Wheeler, T. L., Shackelford, S.
Technology, 64(1), 120-125. doi:https://doi. D., & Koohmaraie, M. (2004). Variation
org/10.1016/j.lwt.2015.05.050 in Palatability and Biochemical Traits
Oz, F., Aksu, M. I., & Turan, M. (2017). The Within and Among Eleven Beef Muscles.
Effects of Different Cooking Methods Journal of Animal Science, 82(2), 534-550.
on Some Quality Criteria and Mineral doi:10.2527/2004.822534x
Composition of Beef Steaks. Journal of Rohman, A., Sismindari, Erwanto, Y., & Che
Food Processing and Preservation, 41(4), Man, Y. B. (2011). Analysis of Pork
e13008. doi:10.1111/jfpp.13008 Adulteration in Beef Meatball using Fourier
Papadopoulou, O., Panagou, E. Z., Tassou, C. Transform Infrared (FTIR) Spectroscopy.
C., & Nychas, G. J. E. (2011). Contribution Meat Science, 88(1), 91-95. doi:https://doi.
of Fourier Transform Infrared (FTIR) org/10.1016/j.meatsci.2010.12.007
Spectroscopy Data on the Quantitative Sánchez del Pulgar, J., Gázquez, A., & Ruiz-
Determination of Minced Pork Meat Carrascal, J. (2012). Physico-Chemical,
Spoilage. Food Research International, Textural and Structural Characteristics of
44(10), 3264-3271. doi:https://doi. Sous-Vide Cooked Pork Cheeks as Affected
org/10.1016/j.foodres.2011.09.012 by Vacuum, Cooking Temperature, and
Peleg, M. (2019). The Instrumental Texture Cooking Time. Meat Science, 90(3), 828-
Profile Analysis Revisited. Journal 835. doi:https://doi.org/10.1016/j.meatsci.
of Texture Studies, 50(5), 362-368. 2011.11.024
doi:10.1111/jtxs.12392 Sinanoglou, V. J., Cavouras, D.,
Petracci, M., & Berri, C. (2017). Poultry Xenogiannopoulos, D., Proestos, C.,
Quality Evaluation Quality Attributes and & Zoumpoulakis, P. (2018). Quality
Consumer Values. Assessment of Pork and Turkey Hams
Using FT-IR Spectroscopy, Colorimetric,
Pietrasik, Z., & Janz, J. A. M. (2009). Influence and Image Analysis. Foods (Basel,
of Freezing and Thawing on the Hydration Switzerland), 7(9), 152. doi:10.3390/
Characteristics, Quality, and Consumer foods7090152
Acceptance of Whole Muscle Beef Injected
with Solutions of Salt and Phosphate. Meat Taher, B. J., & Farid, M. (2001). Cyclic
Science, 81(3), 523-532. doi:https://doi. Microwave Thawing of Frozen Meat:
org/10.1016/j.meatsci.2008.10.006 Experimental and Theoretical Investigation.
Chemical Engineering and Processing:
Rahman, U. u., Sahar, A., Pasha, I., Rahman, Process Intensification, 40, 379-389.
S. u., & Ishaq, A. (2018). Assessing the doi:10.1016/S0255-2701(01)00118-0
Capability of Fourier Transform Infrared
Spectroscopy in Tandem with Chemometric

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
Ainur Nalisa Abd Rashid et al. 116

Utama, D. T., Baek, K. H., Jeong, H. S., Yoon, Xiong, Y. L. (2000). Protein Oxidation and
S. K., Joo, S.-T., & Lee, S. K. (2018). Implications for Muscle Food Quality (pp.
Effects of Cooking Method and Final 85-111). New York: John Wiley and Sons.
Core-Temperature on Cooking Loss, Lipid Yu, P. (2007). Protein Secondary Structures (α-
Oxidation, Nucleotide-Related Compounds helix and β-sheet) at a Cellular Level and
and Aroma Volatiles of Hanwoo Brisket. Protein Fractions in Relation to Rumen
Asian-Australasian journal of animal Degradation Behaviours of Protein: A New
sciences, 31(2), 293-300. doi:10.5713/ Approach. British Journal of Nutrition,
ajas.17.0217 94(5), 655-665. doi:10.1079/BJN20051532
Wang, Y., Liang, H., Xu, R., Lu, B., Song, X., Yu Q. P., Feng D. Y., Xiao J., Wu F., He X. J.,
& Liu, B. (2020). Effects of Temperature Xia M. H., Dong T., Liu Y.H., Tan Z.E.,
Fluctuations on The Meat quality and Zou S.G., Zheng T., Ou X.H. & Zuo J. J.
Muscle Microstructure of Frozen Beef. (2017). Studies on Meat Color, Myoglobin
International Journal of Refrigeration, Content, Enzyme Activities, and Genes
116, 1-8. doi:https://doi.org/10.1016/j. Associated with Oxidative Potential of Pigs
ijrefrig.2019.12.025 Slaughtered at Different Growth Stages.
Wei, R., Wang, P., Han, M., Chen, T., Xu, X., Asian-Australasian journal of animal
& Zhou, G. (2017). Effect of Freezing on sciences, 30(12), 1739-1750. doi:10.5713/
Electrical Properties and Quality of Thawed ajas.17.0005
Chicken Breast Meat. Asian-Australasian Zhou, G. H., Xu, X. L., & Liu, Y. (2010).
journal of animal sciences, 30(4), 569-575. Preservation Technologies for Fresh Meat
doi:10.5713/ajas.16.0435 – A review. Meat Science, 86(1), 119-
128. doi:https://doi.org/10.1016/j.meatsci.
2010.04.033

Appendix

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY, COLOUR SPECTROPHOTOMETER B

Figure 1: FT-IR spectra of (a) raw beef and chicken, (b) boiled beef and chicken and (c) roasted beef and
chicken meats

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
Ainur Nalisa Abd Rashid et al. 118

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119
 QUALITY ANALYSIS OF MEATS USING FTIR SPECTROSCOPY, COLOUR SPECTROPHOTOMETER B

Figure 2: The FT-IR spectra interpretation of (a) raw beef; (b) raw chicken; (c) boiled beef; (d) boiled
chicken; (e) roasted beef; (f) roasted chicken within five days storage

(a) (b)
Figure 3: Image of (a) raw chicken and (b) raw beef in day 1 (above) and day 5 (below)

Journal of Sustainability Science and Management Volume 16 Number 1, January 2021: 103-119

View publication stats