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Foods 13 00391
Foods 13 00391
Article
Oxidative Modification, Structural Conformation, and Gel
Properties of Pork Paste Protein Mediated by Oxygen
Concentration in Modified Atmosphere Packaging
Rui Liu 1 , Wen Guan 1 , Wei Lv 1 , Zhuangli Kang 2 , Qingling Wang 1 , Duxin Jin 1 , Xinxin Zhao 1 , Qingfeng Ge 1 ,
Mangang Wu 1 and Hai Yu 1, *
1 College of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China;
[email protected] (R.L.); [email protected] (W.G.); [email protected] (W.L.);
[email protected] (Q.W.); [email protected] (D.J.); [email protected] (X.Z.);
[email protected] (Q.G.); [email protected] (M.W.)
2 School of Tourism and Cuisine, Engineering Technology Research Center of Yangzhou Prepared Cuisine,
Yangzhou University, Yangzhou 225127, China; [email protected]
* Correspondence: [email protected]
Abstract: The objective of this study was to investigate the effect of pork oxidation through modified
atmosphere packaging (MAP) on gel characteristics of myofibrillar proteins (MP) during the heat-
induced gelation process. The pork longissimus thoracis (LT) was treated by MAP at varying oxygen
concentrations (0, 20, 40, 60, and 80% O2 ) with a 5-day storage at 4 ◦ C for the detection of MP oxidation
and gel properties. The findings showed the rise of O2 concentration resulted in a significant increase
of carbonyl content, disulfide bond, and particle size, and a decrease of sulfhydryl content and
MP solubility (p < 0.05). The gel textural properties and water retention ability were significantly
improved in MAP treatments of 0–60% O2 (p < 0.05), but deteriorated at 80% O2 level. As the
concentration of O2 increased, there was a marked decrease in the α-helix content within the gel,
accompanied by a simultaneous increase in β-sheet content (p < 0.05). Additionally, a judicious
Citation: Liu, R.; Guan, W.; Lv, W.; oxidation treatment (60% O2 in MAP) proved beneficial for crafting dense and uniform gel networks.
Kang, Z.; Wang, Q.; Jin, D.; Zhao, X.; Our data suggest that the oxidation treatment of pork mediated by O2 concentration in MAP is capable
Ge, Q.; Wu, M.; Yu, H. Oxidative of reinforcing protein hydrophobic interaction and disulfide bond formation, thus contributing to the
Modification, Structural construction of superior gel structures and properties.
Conformation, and Gel Properties of
Pork Paste Protein Mediated by
Keywords: pork paste; modified atmosphere packaging; protein oxidation; textural properties; water
Oxygen Concentration in Modified
holding capacity
Atmosphere Packaging. Foods 2024,
13, 391. https://doi.org/10.3390/
foods13030391
attention [7,8]. High-oxygen MAP often consists of 70–80% O2 and 20–30% CO2 for main-
taining a vibrant red color in meat, but it also diminishes the edible quality of meat and af-
fects its tenderness and juiciness [9–12]. Clausen et al. [13] demonstrated how high-oxygen
MAP aggravated the oxidation of lipids and proteins and decreased protein degradation
and meat tenderness of beef. Bao et al. [14] observed that as the O2 concentration increased
(20–80%), protein oxidation levels elevated, subsequently leading to cross-link formation in
structural proteins. Those cross-links, in turn, increased mechanical strength, ultimately
resulting in tougher meat. Lund et al. [15] suggested that oxidation-induced myosin heavy
chain cross-linking through disulfide bonding represents another mechanism contributing
to the O2 -induced toughening of meat. Many studies have thus focused on the influence of
protein oxidation induced by O2 concentration in MAP on fresh meat quality. However, the
effect on meat processing characteristics, especially the gel properties of the myofibrillar
protein (MP), which are crucial functional attributes in the comminuted product matrix,
has received little attention.
The mechanism of thermogelation of MP gel properties of meat has been extensively
studied [16]. The MP undergoes denaturation and unfolding during heating, and the pro-
tein structure unfolds, exposing the functional groups that are originally in the protein [17].
The intermolecular interaction force is strengthened, the proteins aggregate with each other
to form larger polymers, and finally, the proteins are rearranged into a structurally stable,
viscoelastic three-dimensional gel network structure [18,19]. Disulfide bonds, in particular,
play a significant role in protein cross-linking, contributing to enhanced gel hardness and
water retention. Moderate oxidation-induced formation of disulfide bonds has been shown
to be crucial for improving gel quality [20]. Wang et al. [21] investigated the impact of O2
concentration (0, 20, 40, 60, and 80%) in MAP on beef MP gel properties during heating. It
was revealed that the 20% O2 treatment group produced a firmer and more elastic MP gel.
However, the internal mechanism underlying the linkage of protein oxidation induced by
MAP with gel properties warrants further investigation.
Up to the present, research concerning the oxidative modification of protein by O2
concentration in MAP have mostly emphasized clarification to the changes in raw meat
quality. However, there are few studies on the effect of O2 concentration in MAP on the
important functional properties of meat protein during the heat-induced gelation process.
Consequently, this study aims to explore the impact of pork oxidation levels in situ through
MAP with varying O2 concentrations (0, 20, 40, 60, and 80%) on gel characteristics of pork
paste during the heat-induced gelation process. This work will enrich and develop the
intrinsic relationship between the oxidative regulation of meat and protein gelation, thereby
providing a theoretical basis for improving the quality of gel products.
and contained 20% CO2 to inhibit microbial growth. Packaging was performed on a
packaging machine X-500D (Shanghai Tan Xin Packaging Technology Co., Ltd., Shanghai,
China) with a composite packaging bag (Dong Guang County Zhi Long Plastic Co., Ltd.,
Cangzhou, China) composed of polyamide/polypropylene. The O2 transmission rate was
12.707 cm3 /m2 /h/MPa. After the packaging was completed, the gas atmosphere (% O2 , %
N2 , and % CO2 ) in package was verified by a multi-in-one gas detector (GT-903, Shenzhen
Korno Electronic Technology Co., Ltd., Shenzhen, China), with no significant changes
observed. All packages were placed in a refrigerator (Qingdao Haier Co., Ltd., Qingdao,
China) for 5 days and the temperature was set to 4 ◦ C, which was confirmed by a portable
thermometer (ZG-8010, Ningbo Zhaoji Electrical Appliance Co., Ltd., Ningbo, China). After
5 days, the meat samples were ground and quick frozen with liquid nitrogen. Then, the
samples were stored at −80 ◦ C to enable further preparation of pork paste.
where L1 *, a1 * and b1 * are the values on day 0 sample and L2 *, a2 * and b2 * are the values on
MAP treatment samples.
W0 − W1
Cooking loss (%) = × 100% (3)
W0
W1 − W2
Centrifugation loss(%) = × 100% (4)
W1
A0 − A1
BPB (µg) = × 200 µg (5)
A0
Ca
Protein solubility = ×100% (6)
Cb
nmol
Free sulfhydryl content ( ) =73.53SA × D/C (7)
mg
nmol
Total sulfhydryl content ( ) =73.53SB × D/C (8)
mg
Foods 2024, 13, 391 5 of 19
nmol
S-S content ( ) =73.53SC × D/C − total sulfhydryl content (9)
mg
where D is the dilution coefficient and C (mg/mL) is the protein concentration in the
tested sample.
where A indicates the absorbance of the sample, b is the optical path (0.54 cm), C is the
protein concentration (mg/mL), and ε is the absorption coefficient 22,000 M−1 cm−1 .
2.3.7. SDS-PAGE
In order to observe the cross-linking of paste protein from pork through MAP treat-
ment, reducing and non-reducing gel electrophoresis were performed by referring to the
method of Grossi et al. [34] with slight adjustments. Protein samples (2 mg/mL) were
combined with an equivalent volume of loading buffer (100 mM Tris, 4% SDS, 20% Glycerol,
1% BPB), with or without 5% β-ME, and subsequently boiled for 5 min at 95 ◦ C. SDS–PAGE
was conducted using a 10% separating gel and a 4% acrylamide stacking gel. Standard pro-
tein (5 µL) was added to each gel as a reference marker, and 10 µg of protein samples were
loaded onto each well. The operating conditions were 90 V for the first 30 min and 120 V
for the latter 60 min. After the electrophoresis was completed, the gel was stained with
0.025% Coomassie brilliant blue G250 for 60 min, followed by destaining with a solution
composed of 10% methanol and 10% acetic acid. Protein profiles were scanned with a Geno
Sens 2100 Gel Imaging System (Qinxiang Scientific Instrument Co., Ltd., Shanghai, China).
collection, the curve underwent smoothing, and the multi-point baseline was calibrated
using the spectral processing software Labspec version 5.0. The Alix calculation method
was used to analyze the secondary structure of the protein.
3. Results
3.1. Color, Texture and Water Holding Capacity
The properties of the gel from minced meat, including color, water holding capacity,
and texture are presented in Table 1. The color characteristics of meat products could affect
the satisfaction of consumers to a large extent, and the gel whiteness and ∆E values were
considered to be a useful indicator for the overall color evaluation [24,37]. As shown in
Table 1, with the increase of O2 concentration (0–80%) in MAP, ∆E, whiteness and L* values
of the gel slightly increased, but the difference was not significant (p > 0.05). The a* and b*
of gel decreased with O2 concentration from 0% to 20%, and then slightly increased in the
latter 40–80% O2 treatment. Lower a* values in MAP groups (0–80%) were observed when
compared to Day 0 samples. This may be due to the fact that the O2 concentration increases
meat oxidation, potentially leading to the unfolding of protein structure, which affects
the interaction between protein and water. The increased water absorption within the gel
network may contribute to a higher light reflection. That was evidenced by the detection
of water holding capacity, among which cooking loss and centrifugation loss of the gel
Foods 2024, 13, 391 7 of 19
Table 1. Color, texture, and water holding capacity (cooking loss and centrifugation loss) of pork
paste gels from minced meat before storage (Day 0) and after being placed in refrigerated storage for
5 days in MAP with different O2 concentrations.
concentration, especially under the condition of high H2O2 concentration. Moreover, the
Foods 2024, 13, 391 large aggregates were mainly cross-linked by myosin and proteins in MP through disul- 10 of 19
fide bonds.
Representative
Figure2.2.Representative
Figure SDS–PAGE
SDS–PAGE patterns
patterns of paste
of paste protein
protein in non-reduced
in non-reduced form ((a)form −β-ME)
((a)and
−β-ME)
and reduced
reduced form
form ((b) ((b) +β-ME)
+β-ME) from
from pork porkstorage
before before (Day
storage (Day
0) and 0) and
after after
being being
placed placed refrigerated
refrigerated stor-
age for 5 for
storage days in a modified
5 days atmosphere
in a modified with different
atmosphere O2 concentrations.
with different O2 concentrations.
3.3.Secondary
3.3. SecondaryStructure
Structure of of
thethe
GelGel
AsAsindicated
indicatedininthe the Raman
Raman spectra
spectra (Figure
(Figure 3a),3a), protein
protein secondary
secondary structures
structures of theofgel
the gel
were analyzed and the variations were found in groups of Day 0 samples and different O2 O2
were analyzed and the variations were found in groups of Day 0 samples and different
concentrationsin
concentrations inMAP.
MAP. Predominantly,
Predominantly, the the information
information on on protein
protein secondary
secondary structure
structure was
derived from the Amide I band (1600–1700 cm −1−1), primarily involving C-O stretching [53].
was derived from the Amide I band (1600–1700 cm ), primarily involving stretching
The The
bands from 1650–1658 cm −1−1 correspond to the α-helix, 1665–1680 cm −1 correspond
[53]. bands from 1650–1658 cm correspond to the α-helix, 1665–1680 cm−1 correspond
toβ-sheet, 1680–1690 −1 correspond to β-turn, and 1660–1665 cm−1 correspond
to β-sheet,1680–1690 cmcm−1 correspond to β-turn, and 1660–1665 cm−1 correspond to ran- to
random
dom coil coil [54,55].
[54,55]. WithWith the increase
the increase of O2ofconcentration
O2 concentration in MAP,
in MAP, the protein
the protein α-helix of gelof gel
α-helix
gradually
graduallydeclined
declined(p (p<<0.05),
0.05),while
whileβ-sheet
β-sheetincreased
increased(p(p<<0.05)
0.05)and
andminor
minorchanges
changesof ofβ-
β-turn
turn
and and random
random coil coil
were were observed
observed (Figure
(Figure 3b).3b). This
This suggests
suggests protein
protein structural
structural conver- of
conversions
sions of gel
gel from thefrom
α-helixthe to
α-helix
otherto other structures,
structures, which canwhich can possibly
possibly be attributed
be attributed to the Oto2 -induced
the
O 2-induced
protein proteinexpediting
oxidation oxidation expediting
the unfolding the unfolding of the
of the α-helix. α-helix.
The The enhancement
enhancement of the β-sheet
of the β-sheet
indicates the indicates
formation theofformation of inter-molecular
inter-molecular hydrogen bondinghydrogenbetween
bondingpeptide
betweenchains
pep- and
tide chains and an ordered rearrangement of protein molecules
an ordered rearrangement of protein molecules [56]. In addition, a high ratio of [56]. In addition, a high
β-sheet
Foods 2024, 13, x FOR PEER REVIEW 11 of 19
ratio
was shown to facilitate the assembly of a dense gel network, resulting in improvedinwater
of β-sheet was shown to facilitate the assembly of a dense gel network, resulting
improved
retention water
capacity retention capacity
[57], which [57], which
is proven is proven
by the presentby the present study.
study.
Figure 3.
3. Raman
Ramanspectra
spectra(a)
(a)and
andsecondary
secondarystructures (b)(b)
structures of pork paste
of pork gelsgels
paste fromfrom
minced meatmeat
minced before
before
storage (Day 0) and after being placed in refrigerated storage for 5 days in a modified atmosphere
storage (Day 0) and after being placed in refrigerated storage for 5 days in a modified atmosphere
with different O2 concentrations. Note: different lowercase letters indicate significant differences
with different O2 concentrations. Note: different lowercase letters indicate significant differences
among treatment groups (p < 0.05).
among treatment groups (p < 0.05).
3.4. Chemical Forces in the Gel
As shown in Figure 4, the intermolecular chemical forces of the gel were determined
among treatment groups. It was found that hydrophobic interaction and disulfide bonds
occupied a higher proportion in gel compared to ionic and hydrogen bonds, suggesting
that hydrophobic interaction and disulfide bonds contributed significantly to the overall
chemical forces in all gels, highlighting their dominant role in stabilizing the gel structure.
Foods 2024, 13, 391 11 of 19
Chemicalforces
Figure4.4.Chemical
Figure forcesofofpork
porkpaste
pastegels
gelsfrom
frommeat
meatbefore
beforestorage
storage(Day(Day0)0)and
andafter
afterbeing
beingplaced
placed
ininrefrigerated
refrigeratedstorage
storageforfor5 5days
daysininaamodified
modifiedatmosphere
atmospherewithwithdifferent
differentOO2 2concentrations.
concentrations.Note:
Note:
the
thebar
barindicates
indicatesstandard
standarderror
errorofofmeans.
means.Different
Differentlowercase
lowercaseletters
lettersindicate
indicatesignificant
significantdifferences
differences
among
amongtreatment
treatmentgroups
groups(p(p<<0.05).
0.05).
3.5.Water
3.5. WaterDistribution
Distributionand
andMobility
Mobility
AsAsshown
shownininFigure
Figure5,5,the
theNMR
NMRcurves
curvesforforall
allgels
gelsexhibited
exhibitedthree
threedistinct peaks,TT2121
distinctpeaks,
(0–5ms),
(0–5 T22
ms),T22 (30–200
(30–200 ms),
ms), T23 T
andand 23 (700–2000
(700–2000 ms),ms),
which which signified
signified tightly
tightly bound bound
water,water,
im-
immobilized water, and free water, respectively [61]. In particular, a shorter
mobilized water, and free water, respectively [61]. In particular, a shorter relaxation time relaxation time
(T ) implies reduced water mobility and intensified interaction between
(T2) implies reduced water mobility and intensified interaction between water molecules
2 water molecules
andproteins
and proteinswithin
within the
the gel
gel structure
structure [62].
[62]. As
As presented
presentedininTable
Table2,2,with
withthe O2Oconcentration
the 2 concentra-
from 0% to 60%, T and
tion from 0% to 60%,21T21 and 22 T of gel decreased, from 1.18 ms to 0.79
T22 of gel decreased, from 1.18 ms to 0.79 ms, fromms, from79.25
79.25msms
to 73.07 ms, respectively. Nevertheless, when O concentration reached
to 73.07 ms, respectively. Nevertheless, when O2 2concentration reached 80%, an increase 80%, an increase
T21
ininT21 and
and T22Twas
22 was observed,
observed, suggesting
suggesting the water
the water fluidity
fluidity was raised
was raised and flowed
and flowed out
out more
easily during processing. Moreover, the proportions of peak areas corresponding to the
three states of water were shown as P21, P22, and P23. The immobilized water (P22) occupied
the major constituent in the gel (91–95%), which was followed by free water and bound
water. The P22 significantly increased from 92.50% to 94.82%, with an increase in O2 con-
centration (0–60%). Concurrently, P23 experienced a notable drop from 6.10% to 3.44%.
Foods 2024, 13, 391 12 of 19
more easily during processing. Moreover, the proportions of peak areas corresponding
to the three states of water were shown as P21 , P22 , and P23 . The immobilized water (P22 )
occupied the major constituent in the gel (91–95%), which was followed by free water and
bound water. The P22 significantly increased from 92.50% to 94.82%, with an increase in
O2 concentration (0–60%). Concurrently, P23 experienced a notable drop from 6.10% to
3.44%. This observation suggests that protein oxidation not only hinders water fluidity in
the gel but also promotes the transformation of free water into immobile water, indicating
Foods 2024, 13, x FOR PEER REVIEW increased water entrapment within the protein structure, leading to immobilization. These
13 of 19
were also in accordance with the detection of water holding capacity. According to chemical
forces in the gel, changes in inter- and intramolecular bonds within proteins, induced by
oxidation, influenced proton accessibility, thereby causing alterations in the relaxation
velocity of water in close proximity to protein molecules and its retention ability.
Figure 5. Water distribution of pork paste gels from minced meat before storage (Day 0) and
Figureafter bring distribution
5. Water placed in refrigerated storage
of pork paste for from
gels 5 days in a modified
minced atmosphere
meat before with
storage different
(Day 0) andOafter
2
bring concentrations.
placed in refrigerated storage for 5 days in a modified atmosphere with different O2 concen-
trations.
Table 2. Corresponding relaxation time (T2 ) and peak area proportion (P) of pork paste gels from
Tableminced meat before relaxation
2. Corresponding storage (Day 0) and
time (T2)after
andbeing
peak placed in refrigerated
area proportion (P) storage
of porkfor 5 days
paste gelsinfrom
a
modified
minced atmosphere
meat before with
storage different
(Day O2 after
0) and concentrations.
being placed in refrigerated storage for 5 days in a
modified atmosphere with different O2 concentrations.
Parameter Day 0 0% 20% 40% 60% 80% p Value
ParameterT21 (ms)Day 01.18 ± 0.03 b 0%1.30 ± 0.01 a 20% 1.07 ± 0.02 c 40%
0.88 ± 0.01 d 60%
0.79 ± 0.01 e 80%
1.19 ± 0.00 b p<0.001
Value
b b ± c ± c d ± a
T (ms) 79.25 ± 0.40
T21 (ms) 22 1.18 ± 0.03 b 78.23 ± 0.14
1.30 ± 0.01 a 75.76
1.07 ± 0.02 c 0.32 74.61
0.88 ± 0.01 0.75
d 0.7973.07 ± 0.67 1.19 ± 0.00
± 0.01 e 81.38 0.40
b <0.001
<0.001
a a
T23 (ms) 1256b ± 30.5 b 1275 ± 23.2 b 1312 ± c41.4 b 1438 ± 30.9 1420 ± 34.5 1217 ± 24.1a b 0.001
T22 (ms) 79.25 ± 0.40 78.23 ± 0.14 b 75.76 ± 0.32 74.61 ± 0.75 a73.07 ± 0.67 a 81.38 ± 0.40 b
c d <0.001
P21 (%) 1.52 ± 0.02 b 1.29 ± 0.06 c 1.55 ± 0.05 b 1.76 ± 0.04 1.88 ± 0.05 1.43 ± 0.02 <0.001
T23 (ms) P221256
(%) ± 30.5
b 1275
91.30 ± 0.25 d ± 23.2 b 1312
92.50 ± 0.45 c ±93.57
41.4±b0.191438
b ± 30.9
94.15 ± 0.08 ab1420
a ± 34.5
94.82 ± 0.15 a 1217
a ± 24.1
93.50
b
± 0.46 b 0.001
<0.001
a ab c cd d b
P21 (%) P23 1.52
(%) ± 0.02 b 1.29 ± 0.06
6.84 ± 0.33 6.10 ± 0.391.55 ±4.55
c 0.05± 0.24 1.764.29
b ± 0.04
± 0.15 1.883.44
a ± 0.05
± 0.23 1.43
a ±±
5.58 0.02
0.50b <0.001
<0.001
P22 (%) 91.30 ± 0.25 d 92.50 Note:
± 0.45Mean 93.57
c values ±± 0.19
standard 94.15
b ± 0.08 lowercase
error. Different ab 94.82 letters
± 0.15( ) in93.50
a
a–e
± 0.46
the same line indicate <0.001
b significant
differences between treatmentc groups at p < 0.05. cd
P23 (%) 6.84 ± 0.33 a 6.10 ± 0.39 ab 4.55 ± 0.24 4.29 ± 0.15 3.44 ± 0.23 d 5.58 ± 0.50 b <0.001
Note: 3.6.
Mean values ± standard
Ultrastructure of Gel error. Different lowercase letters ( ) in the same line indicate signif-
a–e
uniform pores and filamentous structure. However, in the 80% O2 treatment group, the
gel structure was tight and irregular, and large aggregates and pore sizes appeared in the
microstructure. Nyaisaba et al. [63] stated that the microstructure of heat-induced protein
gel was closely associated with the relative velocity of protein unfolding and aggregation.
The oxidation of protein, induced by different O2 concentrations in MAP can affect its gel
Foods 2024, 13, x FOR PEER REVIEW 14 of 19
properties via structural and conformational changes to the ultrastructural formation of gel
during heating.
Figure6.6.Microstructure
Figure Microstructureof of pork
pork paste
paste gelsgels
fromfrom minced
minced meatmeat before
before storage
storage (Day(Day
0) and0)after
and being
after being
placed in refrigerated storage for 5 days in a modified atmosphere with different O2 concentrations.
placed in refrigerated storage for 5 days in a modified atmosphere with different O2 concentrations.
3.7.
3.7.SDS-PAGE
SDS-PAGEof of
GelGel
The
Thenon-participating
non-participating proteins
proteinsin the gelgel
in the formation
formationare presented in Figure
are presented 7. It was
in Figure 7. It was
observed that the thick bands were low molecular weight proteins (<36 kDa).
observed that the thick bands were low molecular weight proteins (<36 kDa). A previous A previous
study
studydemonstrated
demonstrated thatthat
tropomyosin
tropomyosin (a doublet in 34–36
(a doublet in kDa)
34–36 and troponin
kDa) (about 20 (about
and troponin kDa) 20
had a marginal role in gel formation [64]. Consistent with the report
kDa) had a marginal role in gel formation [64]. Consistent with the report of Gao of Gao et al. [65],et al.
myosin heavy chain (MHC) and actin nearly vanished in all gels with reduced form and
[65], myosin heavy chain (MHC) and actin nearly vanished in all gels with reduced form
non-reduced forms, providing additional confirmation of their predominant role in the
and non-reduced forms, providing additional confirmation of their predominant role in
gelation process. With the increase in O2 concentration, the intensity of the bands 2, 3, and
the gelation process. With the increase in O2 concentration, the intensity of the bands 2, 3,
3′ was gradually weakened, but the intensity of the bands 4 and 4′ was strengthened in the
and 3′ was
respective gradually weakened,
non-reduced butand
gel (Figure 7a) the reduced
intensitygel
of (Figure
the bands7b).4In
and 4′ was itstrengthened
addition, should
in the respective non-reduced gel (Figure 7a)′ and reduced
′ gel
be noted that in reduced gels, a tenuous band 1 and 2 vanished with the increase (Figure 7b). In addition,
in O2 it
should be noted
concentration. The that in reduced
findings suggestedgels, a tenuous
that band 1′could
MAP treatment and 2′ vanishedpromote
effectively with the increase
more
in O2 concentration.
proteins to become involvedThe findings suggestedofthat
in the construction gel MAP
network treatment
structure.could effectively pro-
mote more proteins to become involved in the construction of gel network structure.
the gelation process. With the increase in O2 concentration, the intensity of the bands
and 3′ was gradually weakened, but the intensity of the bands 4 and 4′ was strength
in the respective non-reduced gel (Figure 7a) and reduced gel (Figure 7b). In additio
should be noted that in reduced gels, a tenuous band 1′ and 2′ vanished with the incr
Foods 2024, 13, 391 in O2 concentration. The findings suggested that MAP treatment could 14 of effectively
19
mote more proteins to become involved in the construction of gel network structure
Figure 7. Representative
Figure 7.SDS–PAGE patterns
Representative of non-participating
SDS–PAGE proteins of porkproteins
patterns of non-participating paste gels frompaste gels
of pork
minced meat before storage
minced meat(Day 0)storage
before and after being
(Day placed
0) and afterin refrigerated
being placed instorage for 5 storage
refrigerated days in for 5 day
a modified atmosphere with different O2 concentrations. Samples were prepared in the absence
((a) −β-ME) or presence ((b) +β-ME) of 5% β-ME.
before storage (Day 0) and after being placed in refrigerated storage for 5 days in a modified atmos-
phere with different O2 concentrations.
Figure 9. The mechanism diagram of pork paste gels from minced meat before storage (Day 0) and
Figure 9. The mechanism diagram of pork paste gels from minced meat before storage (Day 0) and
after being placed in refrigerated storage for 5 days in a modified atmosphere with different O2
after being placed in refrigerated storage for 5 days in a modified atmosphere with different O2
concentrations.
concentrations.
4. Conclusions
The primary outcome of this study was that moderate oxidation in MAP (~60% O2)
markedly improved the gelling performance of paste protein during thermally-induced
gelation, as corroborated by the enhanced gel texture and water retention capacity. More-
Foods 2024, 13, 391 16 of 19
4. Conclusions
The primary outcome of this study was that moderate oxidation in MAP (~60% O2 )
markedly improved the gelling performance of paste protein during thermally-induced
gelation, as corroborated by the enhanced gel texture and water retention capacity. More-
over, T2 relaxation analysis demonstrated that moderate oxidation can decrease the water
fluidity during the gelation of paste protein and prompted the transformation of free water
into immobilized water. The oxidation enhanced protein-protein interactions and triggered
a more compact and homogenous gel network. Gel properties, chemical forces, and the
ultrastructure of gels were shown to differ significantly between packaging with different
O2 concentrations. In the case of 60% O2 in MAP, the gel had greater textural properties,
stronger elasticity, and a denser structure. Collectively, the present study would be benefi-
cial for the application of MAP as a potential tool to regulate meat proteins with improved
gel performance via oxidative modification.
Supplementary Materials: The following supporting information can be downloaded at: https:
//www.mdpi.com/article/10.3390/foods13030391/s1, Table S1: The average particle size of pork
paste gels from minced meat before storage (Day 0) and after being place in refrigerated storage for
5 days in a modified atmosphere with different O2 concentrations.
Author Contributions: Conceptualization, R.L.; methodology, R.L., W.G. and W.L.; resources, R.L.,
Z.K., Q.W., D.J., X.Z., Q.G., M.W. and H.Y.; data curation, W.G.; writing—original draft preparation,
W.G.; writing—review and editing, R.L. and W.G.; visualization, W.G. and W.L.; funding acquisition,
R.L. and H.Y. All authors have read and agreed to the published version of the manuscript.
Funding: This research was funded by the Outstanding Youth Science Fund Project of Natural Science
Foundation of Jiangsu Province (BK20230070), China; Qing Lan Project of Yangzhou University,
China; High-Level Talent Support Program of Yangzhou University, China. National Natural Science
Foundation of China (No. 32172276; No. 32101859), China; Jiangsu Provincial Key Research and
Development Program (BE2022333), China.
Institutional Review Board Statement: Not applicable.
Informed Consent Statement: Not applicable.
Data Availability Statement: Data is contained within the article.
Acknowledgments: The technical was supported by Bingbing Shen from Guoke Testing Technology
Co., Ltd., Hefei, China.
Conflicts of Interest: The authors declare no conflict of interest.
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