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This study investigates the impact of gluten quality on the textural stability of cooked noodles, focusing on the glutenin-gliadin ratio and glutenin macropolymer (GMP) content. It was found that a suitable glutenin-gliadin ratio and high GMP content help preserve noodle texture during cooking and immersion. The research highlights the importance of gluten quality in maintaining the desirable textural properties of noodles, particularly in the context of the growing takeaway food industry.

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0% found this document useful (0 votes)
11 views10 pages

1 s2.0 S0268005X21002587 Main

This study investigates the impact of gluten quality on the textural stability of cooked noodles, focusing on the glutenin-gliadin ratio and glutenin macropolymer (GMP) content. It was found that a suitable glutenin-gliadin ratio and high GMP content help preserve noodle texture during cooking and immersion. The research highlights the importance of gluten quality in maintaining the desirable textural properties of noodles, particularly in the context of the growing takeaway food industry.

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Food Hydrocolloids 119 (2021) 106842

Contents lists available at ScienceDirect

Food Hydrocolloids
journal homepage: www.elsevier.com/locate/foodhyd

Impact of gluten quality on textural stability of cooked noodles and the


underlying mechanism
Zong-Bao Cao a, b, c, Chen Yu a, b, c, Zhen Yang a, b, c, Jun-Jie Xing a, b, c, Xiao-Na Guo a, b, c,
Ke-Xue Zhu a, b, c, *
a
State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu Province, People’s Republic of China
b
School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu Province, People’s Republic of China
c
Qingdao Special Food Research Institute, Qingdao, 266109, Shandong Province, People’s Republic of China

A R T I C L E I N F O A B S T R A C T

Keywords: The impact of gluten quality on the textural stability of the cooked noodles and its underlying mechanism were
Gluten quality investigated. Textural characterisation and cooking quality analysis were used to evaluate the quality of the
Cooked noodles noodles. The glutenin macropolymer (GMP) content, glutenin-gliadin ratio, dough rheological properties of the
Textural stability
reconstituted wheat flour, water mobility, microstructure, and intermolecular force of the cooked noodles were
Water mobility
also determined. When the immersion time was increased, the hardness, tensile distance, and hydrogen bonds in
Gluten network
the cooked noodles decreased, whereas the relaxation time (T22) increased, and the water penetrated gradually
into the cooked noodles. A suitable glutenin-gliadin ratio, a moderate dough stabilisation time, and high GMP
content contributed to the preservation of the texture of the cooked noodles. The confocal laser scanning mi­
croscopy (CLSM) images and network analysis confirmed that the properties of the cooked noodles made from
various reconstituted wheat flours were different.

1. Introduction the total protein in wheat flour (Morel, Redl, & Guilbert, 2002). It is
composed of polymeric glutenin and monomeric gliadin, which
As a traditional food, fresh wet noodles are popularly consumed in contribute to the elasticity and the viscosity of noodles, respectively
many Asian countries, due to their convenience, nutritional quality, and (Uthayakumaran, Gras, Stoddard, & Bekes, 1999). Both gluten quantity
palatability (Li et al., 2012). One way for fresh wet noodles to be pre­ and gluten quality have been demonstrated to influence the quality of
pared and consumed is as takeaway noodles, which are a new form of noodles (Hou, Saini, & Ng, 2013). Ross, Quail, and Crosble (1997) found
cooked noodle that possesses many advantages. Takeaway noodles are that the gluten quantity was positively correlated with the hardness of
defined as takeaway food that is ordered online and delivered from noodles. In addition to gluten quantity, the gluten quality, including
restaurants to consumers. With the rapid development of the takeaway dough rheological properties, sodium dodecyl sulfonate (SDS) sedi­
food industry in China, the market share of takeaway noodles is also mentation volume with constant gluten weight, and the score of
increasing. Unlike spaghetti, the gluten network of Chinese white salt HMW-GS, have significant correlations with the textural properties of
noodles is relatively loose (Cunin, Handschin, Walther, & Escher, 1995; the cooked noodles (Park, Hong, & Baik, 2003). The improvement of
Finnie & Atwell, 2016). They are more likely to become soft, resulting in gluten quality positively influences the palatability, elasticity, and
poor chewiness because of the excessive water absorption after cooking stickiness of noodles (Liu, He, Zhao, Peña, & Rajaram, 2003).
or during delivery (Horigane et al., 2006; Majzoobi, Ostovan, & Far­ Gluten quality is usually evaluated by the dough rheological prop­
ahnaky, 2011). Therefore, finding an effective way to slow down the erties, glutenin-gliadin ratio, glutenin macropolymer (GMP) content,
texture deterioration of the cooked noodles is of great interest in the and molecular force between gluten molecules. The dough rheological
foodservice industry. properties have also been shown to be related to the texture of cooked
Gluten is the main component of wheat flour, accounting for 85% of noodles. Crosbie, Ross, Moro, and Chiu (1999) found that the hardness

* Corresponding author. State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu Province, People’s
Republic of China.
E-mail address: [email protected] (K.-X. Zhu).

https://doi.org/10.1016/j.foodhyd.2021.106842
Received 22 December 2020; Received in revised form 18 March 2021; Accepted 17 April 2021
Available online 19 April 2021
0268-005X/© 2021 Elsevier Ltd. All rights reserved.
Z.-B. Cao et al. Food Hydrocolloids 119 (2021) 106842

of the cooked noodles increased with the increase of the dough stabili­ β-mercaptoethanol, and trichloroacetic acid were all purchased from
sation time. A proper glutenin-gliadin ratio is critical for noodles quality Sinopharm (Shanghai, China) at analytical grade. The Fluorescein 5-iso­
(Bruneel, Pareyt, Brijs, & Delcour, 2010; Chaudhary, Dangi, & Khatkar, thiocyanate (FITC) and Rhodamin B were purchased from Sigma (St.
2016). On the one hand, a loose gluten network is formed when the Louis, Missouri, USA). Other reagents were at least of analytical grade in
glutenin-gliadin ratio is low, resulting in the quality of the noodles being the experiments.
low (Bruneel, Buggenhout, Lagrain, Brijs, & Delcour, 2016). On the
other hand, there is little gliadin to fill and adhere to the gluten network 2.2. Isolation of gluten and starch
when the glutenin-gliadin ratio is high, the gluten network will be weak
and easy for water molecules to invade. GMP is a kind of macromolec­ The gluten was extracted according to the method of AACC 38-10
ular polymer, and its content and structural characteristics greatly affect (AACC, 2009) with some modification. The wheat starch was extrac­
the quality of noodles (Ong, Ross, & Engle, 2010). The confocal laser ted according to the method described by Su et al. (2020) with some
scanning microscopy (CLSM), a new type of optical analysis method, modification. Wheat flour (1 kg) and deionized water (400 mL) were
could intuitively observe the gluten network structure formed in the mixed in a blender at 100 rpm for 5 min to form a dough, and then the
cooked noodles (Silva, Birkenhake, Scholten, Sagis, & van der Linden, dough was rested for 30 min at room temperature. To obtain pure
2013). In addition, the difference in the formation of the gluten network gluten, the dough was firstly washed by hand with excessive deionized
structure could be explained by measuring the molecular force between water and 10% sodium chloride solution, respectively, and then rinsed
gluten molecules. again with excessive deionized water. This procedure was repeated
There is a high number of articles published in the field of improving several times. Finally, the gluten was frozen in a − 80 ◦ C ultra-low
the quality of the cooked noodles (Lambrecht, Rombouts, Nivelle, & temperature refrigerator for 4 h, then freeze-dried, ground, and passed
Delcour, 2017a; Larrosa, Lorenzo, Zaritzky, & Califano, 2016; Li, et al., through 80-mesh sieves. Besides, the water collected from washing was
2020). However, to the best of our knowledge, little is known about the centrifuged at 3750 g for 10 min at room temperature. The upper layer
impact of gluten quality on the textural stability of the cooked noodles of sediments consisted of water-soluble components (pentosans, albu­
during immersion. Thus, the specific objectives of this study were 1) to mins, and globulins, etc.) was removed. Whereas the white bottom
illustrate the quality attenuation law of the cooked noodles during im­ layer, containing starch, was collected, and resuspended in deionized
mersion; 2) to point out the gluten quality that is suitable for the cooked water and passed through 200-mesh sieves to eliminate other impurities.
noodles; 3) to investigate the underlying mechanism of the impact of The suspension was centrifuged at 3750 g for 10 min at room temper­
gluten quality on the textural stability of the cooked noodles by per­ ature. This procedure was repeated three times, and a total volume of
forming reconstitution of wheat flours. 2.5 L deionized water was used for resuspension. After that, the sedi­
ment was then washed three times with a total volume of 2.5 L 70%
2. Materials and methods ethanol solution to remove the gliadin. Finally, the purified starch
sediment was frozen in a − 80 ◦ C ultra-low temperature refrigerator for
2.1. Materials 4 h, then freeze-dried, ground, and passed through 80-mesh sieves.
Furthermore, the freeze-drying conditions of gluten and wheat starch
Seven wheat flour samples were used in this study. The moisture, were set as follows: vacuum degree, 0.01 kPa; temperature, - 45 ◦ C;
protein, ash, and wet gluten contents are listed in Table 1. Wheat flour freeze-drying time, 72 h.
0–3 were provided by China Oil and Foodstuffs Corporation, Tianjin,
China. Wheat flour 4–6 were provided by Yihai Kerry Food Industry Co., 2.3. Analysis of the dough rheological properties
Ltd, Jiangsu, China. As shown in Table 1, the wet gluten content of the
seven wheat flour samples was 20.31%–38.81%, the moisture content Rheological properties of the dough made from the reconstituted
was 10.91%–14.25%, the protein content was 7.59%–12.41%, and the wheat flours were measured by Mixolab (Chopin Technologies, Paris,
ash content was 0.39%–0.49%. France) according to the method of ICC 173 (ICC, 2011). Each of the
Starch extracted from flour 0 was used as a base for the reconstitu­ reconstituted wheat flour samples (RWF-1 to RWF-6) was put into a
tion of gluten obtained from each of the other six flour samples (flour machine analyzer bowl at a certain amount calculated by the Mixolab
1–6), named as the reconstituted wheat flour samples RWF-1, RWF-2, analysis software on a 14%-moisture basis. Finally, the purified water
RWF-3, RWF-4, RWF-5, and RWF-6, respectively. Finally, the ratio of was added to reach the maximum torque of 1.1 ± 0.05 Nm. In this
starch to gluten in the reconstituted wheat flour was 84:16. Further­ experiment, the following results were obtained from the analysis: water
more, the reconstituted wheat flour should be homogenized at medium absorption (WA, %); dough development time (DDT, min), i.e., the time
speed for 12 h with a mixer machine to make it evenly mixed. Corre­ to reach the maximum torque at 30 ◦ C; dough stabilisation time (DST,
spondingly, the cooked noodles made from the reconstituted wheat flour min), i.e., the time until the loss of consistency is lower than 11% of the
samples RWF-1 to RWF-6 were named as samples CN-1 to CN-6, maximum consistency reached during the mixing; mechanical weak­
respectively. ening (Nm), i.e., the torque difference between the maximum torque at
The SDS, Tris (hydroxymethyl)aminomethane, urea, 30 ◦ C and the torque at the end of the holding time at 30 ◦ C.

2.4. Preparation of the cooked noodles


Table 1
The wet gluten, moisture, protein, and ash contents of the wheat flour samples.
Each of the reconstituted wheat flour (100 g) was homogenized using
Flour samples ID Wet gluten (%) Moisture (%) Protein (%) Ash (%)
a mixer machine (JHMZ-200, Beijing Dongfu Jiuheng Instrument
flour 0 38.81 ± 0.08a 14.25 ± 0.21a 12.41 ± 0.04a 0.49 ± 0.03a Technology Co., Ltd., Beijing China) for 5 min. Then, the deionized
flour 1 21.31 ± 1.25d 11.22 ± 0.24cd 10.08 ± 0.23d 0.40 ± 0.04cd
water (34 g) was added and mixed for 5 min to form a dough, and then
flour 2 20.86 ± 0.67d 11.25 ± 0.36cd 8.89 ± 0.07e 0.44 ± 0.01bc
flour 3 31.85 ± 1.39b 10.91 ± 0.27d 11.83 ± 0.11b 0.40 ± 0.02cd rested in a sealed plastic bag at 25 ◦ C for 30 min. Finally, the dough was
flour 4 30.72 ± 0.98b 12.35 ± 0.43b 12.02 ± 0.09b 0.48 ± 0.01ab sheeted through a semiautomatic noodle machine (JMTD-168/140,
flour 5 27.20 ± 0.65c 11.03 ± 0.25cd 10.56 ± 0.27c 0.45 ± 0.03ab Beijing, Dongfu Jiuheng Instrument Technology Co., Ltd., Beijing,
flour 6 20.31 ± 0.21d 11.51 ± 0.20c 7.59 ± 0.21f 0.39 ± 0.01d China) at the roll gap of 2.0, 1.8, 1.6, 1.4, 1.2, 1.0 mm for 3 times,
Means with different small letter superscripts within the same column are sig­ respectively. During this step, the first two times were double-layered
nificantly different at p < 0.05. rolling and the last time was single-layered rolling. Finally, the sheet
was cut into noodles with a dimension of length at 20 cm, width at 0.2

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Z.-B. Cao et al. Food Hydrocolloids 119 (2021) 106842

cm, and height at 0.1 cm. moisture.


Thirty noodle strands were boiled in 500 mL boiling deionized water For NMR experiments, a Carr-Purcell-Meiboom-Gill (CPMG) pulse
for 2.5 min. Then the cooked noodles were immersed in bath water at sequence was selected to acquire the transverse relaxation curves. The
80 ◦ C for 0, 5, 10, 15, 20, 25, 30 min, respectively. parameters were set as follows: scanning frequency (SF) = 21 kHz, the
number of sampling points (TD) = 120,014, the interval time of sam­
2.5. Analysis of cooking property pling (TW) = 1500 ms, number of slice (NS) = 2, echo time (TE) = 0.300
ms and NECH = 4000.
The cooking properties of noodles include cooking loss and water For MRI experiments, a standard SPIN-ECHO (SE) sequence and a
absorption, which were measured according to AACC method 66–50 radiofrequency (SF) coil (15 mm) were selected to produce images. For
(AACC, 2010) with some modification. Approximately 10 g of noodles the measurements, the settings were as follows: Average = 4, TR = 500
were cooked in 500 mL boiling deionized water for 2.5 min. After that, ms, TE = 20 ms, RG = 20 dB.
the water was then collected and diluted to 500 mL with deionized
water, and 100 mL of which was transferred into a pre-dried beaker to 2.8. Analysis of glutenin-gliadin ratio
evaporate most of the water and dried in an oven (105 ◦ C) till a constant
mass. Determination of glutenin-gliadin ratio was conducted according to
Cooking loss was expressed as the loss rate of dry matter during the method described by Song and Zheng (2008) with some modifica­
cooking: tions. Gluten powder (1 g) prepared in Section 2.2 was dispersed in 5 mL
of 70% aqueous ethanol using a laboratory mixer (Dragon Laboratory
M3
Cooking ⋅ loss ⋅ (%) ⋅ = ⋅ × 100% (1) Instruments Limited, Beijing, China) at medium speed for 1 min. The
M1 × (1 − m)
suspension was then placed on the magnetic stirring hot plate at 37 ◦ C
overnight. The mixture was then centrifuged at 1160 g for 10 min at
where M3 was the weight of total dry residue in the cooking water, M1
room temperature. The sediment was further washed with 70% aqueous
was the weight of the uncooked noodles, m was the moisture of the
ethanol three times. After that, the supernatant was collected and
uncooked noodles.
diluted to 25 mL by 70% aqueous ethanol. The total protein content of
Water absorption was used to evaluate the degree of water absorp­
gluten and the protein content of the supernatant was measured by the
tion of the noodles, which was calculated as the ratio of weight before
means of Kjeldahl determination (AACC, 2009). The gliadin content was
and after cooking:
considered as the protein content of the supernatant, and the glutenin
(M2 − M1 ) content was calculated as the total protein content of gluten minus the
Water ⋅ absorption ⋅ (%) ⋅ = ⋅ × 100% (2)
M1 gliadin content.

where M2 was the weight of the cooked noodles, M1 was the weight of 2.9. Analysis of the GMP content
the uncooked noodles.
Determination of the GMP content was done according to the method
2.6. Analysis of texture properties described by Weegels, Pijpekamp, Graveland, Hamer, and Schofield
(1996) with some modification. In brief, 50 mg of the reconstituted
The texture properties of the cooked noodles were analyzed ac­ wheat flour was dispersed in 1 mL of 1.5% SDS solution and then
cording to the method described by Luo, Guo, and Zhu (2015) with some centrifuged at 15,500 g at 20 ◦ C for 30 min. The supernatant was
modifications. The cooked noodles, which were immersed individually removed carefully and the sediment was dissolved using 4 mL Biuret
in a water bath (80 ◦ C) for 0, 5, 10, 15, 20, 25, 30 min, respectively, after regent. The absorbance of these samples was measured at 540 nm with a
which their texture properties were measured by a TA-XT2i Texture spectrophotometer (TU-1810, Beijing, China) using Biuret regent as the
Analyzer (Stable Micro Systems, London, England). Briefly, three blank (Gornall, Bardawill, & David, 1949). Finally, the GMP content
strands of the cooked noodles were placed on the texture analyzer (mg/g) was expressed as the protein content of the sediment.
platform and compressed by a P36/R probe. The testing parameters
were given as follows: pre-test, 1.0 mm/s; test speed, 1.0 mm/s; post-test 2.10. CLSM analysis
speed, 1.0 mm/s; strain, 75%; trigger force, 5.0 g. Tensile strength
analysis was used to examine the tensile distance of the cooked noodles. The microstructure of the gluten network was measured by CLSM
One strand of the cooked noodles was fixed on an A/SPR probe and (Model LSM 710, Leica, Germany) according to the method described by
increase the tensile load until breakage. The parameters were set at: Silva et al. (2013) with some modifications. About 1 cm of the cooked
pre-test speed, 1.0 mm/s; test speed, 2.0 mm/s; post-test speed, 10.0 noodles was wrapped in Leica glue and cut into 20 μm slices with a
mm/s; distance, 150 mm; trigger force, 5.0 g. Both two measurements freezing microtome (PM2245, Leica). Then the slice was placed on the
were conducted 10 times. glass slides and stained with 0.2% (w/w) FITC solution and 0.025%
The texture decay rate equation of the cooked noodles was obtained (w/w) Rhodamin B solution for 1 min. After dyeing, the sample was then
by nonlinear curve fitting with drawing analysis software Origin 9.5 rinsed with a small amount of deionized water and wiped with filter
(OriginLab Corp., Northampton, MA, USA). The fitting equation was paper. CLSM images, acquired in 1024 × 1024 resolution, were analyzed
expressed as y=y0 + Ae-x/t, and the fitting coefficient was greater than by a vascular network analysis software (Angio Tool) to determine the
0.96. property of the gluten network. The excitation wavelengths for FITC and
Rhodamine B were at 488 nm and 561 nm respectively.
2.7. Analysis of water distribution and migration
2.11. Analysis of molecular force between gluten molecules
Water distribution and migration of the cooked noodles were
determined by NMR and MRI according to the method described by The molecular force between gluten molecules was evaluated by the
Horigane et al. (2006) with some modification. The cooked noodles, solubility of the protein in different denaturation solvents using the
which were immersed individually in a water bath (80 ◦ C) for 0, 10, 20, method described by Roussel and Cheftel (1990) with some modifica­
30 min, were analyzed using a MesoMR23-060V–I Series NMR Analyzer tion. The solvents included 30 mM Tris-HCL buffer (B1); 30 mM
(Shanghai Niumag Co., Ltd, Shanghai, China). Samples were put into the Tris-HCL buffer containing 1% SDS (B2); 30 mM Tris-HCL buffer con­
test tube and sealed with Teflon tape to avoid the interference of air and taining 6M urea (B3); 30 mM Tris-HCL buffer containing 2%

3
Z.-B. Cao et al. Food Hydrocolloids 119 (2021) 106842

β-mercaptoethanol (B4); 30 mM Tris-HCL buffer containing 2% β-mer­ conducive to the preservation of the texture of the cooked noodles. It can
captoethanol and 1% SDS (B5); 30 mM Tris-HCL buffer containing 6 M be seen from Table 2 that the degree of softening was inversely pro­
urea and 1% SDS (B6). portional to the DST. Liu et al. (2003) found that the degree of softening
The freeze-drying procedure of the cooked noodles was the same as of dough was negatively associated with all the quality of the cooked
mentioned in Section 2.2. Lyophilized noodle powder (0.3 g) was noodles. However, this study did not investigate the effect of the im­
dispersed in 5 mL of each of the above buffer solution (B1–B6) and then mersion process on the quality of cooked noodles. Our research found
centrifuged at 13,600 g for 10 min at room temperature. The superna­ that the DDT was the main factor affecting the textural stability of the
tant was collected, and 2 mL of which was mixed with an equal amount cooked noodles. The reason for this difference may be due to the
of 20% trichloroacetic acid, oscillated for 30 min, and then centrifuged different states of the cooked noodles.
at 10,000 g for 10 min at room temperature. Finally, the sediment was
collected and then dissolved in 5 mL of 0.5 M NaOH. The protein con­ 3.2. Effect of gluten quality on the cooking properties of noodles
centration determination method was the same as described in method
2.9. The cooking properties of the noodles are presented in Table 3.
Gluten quality had a significant influence on the water absorption of the
2.12. Statistical analysis cooked noodles (p < 0.05). After cooking, CN-3 and CN-4 had higher
water absorption than the other four samples, which might be attributed
All the analyses in this study were performed at least in triplicate. to high water absorption in the gluten of CN-3 and CN-4. Noodles with a
One-way analysis of variance (ANOVA) followed by Duncan’s test was high cooking yield are desirable (Zhou et al., 2013). However, excessive
conducted to verify significant differences (p < 0.05) using the software water was absorbed during the immersion process of the cooked noo­
SPSS 16.0 for windows (SPSS Inc., Chicago, IL, USA). dles, leading to excessive hydration, and swelling of the starch amor­
phous regions (Biliaderis, Maurice, & Vose, 1980), which thus lowered
the noodles’ eating quality. Low values of water absorption in CN-1 and
3. Results and discussion
CN-2 were observed when the immersion time reached 30 min, which
might have been due to the compact gluten network making it hard for
3.1. Effect of gluten quality on the dough rheological properties of the
the water to penetrate (Pu et al., 2017). Also, the water absorption of the
reconstituted wheat flour
cooked noodles increased with the increase of immersion time. Irie,
Kawahara, Hirauchi, Horigane, and Yoshida (2017) also found that the
Rheological properties of the dough made from reconstituted wheat
water absorption of spaghetti increased with the increase of cooking
flours (RWF-1 to RWF-6) are listed in Table 2. The WA values of RWF-1
time.
and RWF-2 were lower than these of RWF-3 to RWF-6, which may be
Compared with other groups, lower values of cooking loss of CN-1
attributed to the number of hydrophilic residues of gluten (Sun, Yan,
and CN-2 were observed. This may have been due to the dense gluten
Jiang, Li, & MacRitchie, 2010). The DST values of RWF-3 and RWF-5
network adhering tightly to the starch granule, which could have pre­
were relatively longer than the other samples. The DST of RWF-6,
vented the starch from leaking out during cooking (Baiano, Conte, & Del
which was like that of RWF-4, was the shortest, and these values were
Nobile, 2006). Marti et al. (2013) reported that the addition of egg could
moderate for RWF-1 and RWF-2. That is to say, the gluten networks
promote the density of the protein network, thereby preventing the
strength of RWF-3 and RWF-5 were strong, while the gluten networks
leaking of solids.
strength of RWF-4 and RWF-6 were weak, and the gluten networks
strength of RWF-1 and RWF-2 were moderate. Crosbie et al. (1999)
3.3. Effect of gluten quality on texture properties of the cooked noodles
found that the hardness of the cooked noodles increased with the in­
crease of the DST. Whereas, we found that the hardness of the cooked
The texture properties of the cooked noodles are among the primary
noodles was not completely proportional to the DST. For example,
concerns of consumers (Ajila, Aalami, Leelavathi, & Rao, 2010). Palat­
RWF-5 had the longest DST, but its initial hardness was the lowest than
ability and toughness are two important indexes in the sensory evalua­
other groups. The difference might be due to the different influencing
tion of noodles (Sozer, Dalgıç, & Kaya, 2007); thus, hardness and tensile
factors. In the present study, the amount of gluten in the flour was the
distance are selected to evaluate the eating quality of the cooked
same, so the gluten quality was the only factor that affected the DST.
noodles.
However, in Crosbie’s research, both the gluten quantity and gluten
With the prolongation of immersion time, the hardness and tensile
quality affected the DST. Although the gluten networks strength of
distance decreased sharply (Fig. 1). The curves of hardness and tensile
RWF-1 and RWF-2 were moderate, their DDT values were lower than the
distance fitted well with the exponential equation (y=y0 + Ae-x/t). The
other four samples, indicating the quick formation of the gluten network
fitting coefficient was greater than 0.96, indicating that the immersion
in the dough. This could be ascribed to the fast formation of covalent
time was a crucial factor for the hardness and tensile distance of the
bonds and non-covalent bonds in gluten (Pu et al., 2017), which is
cooked noodles. A similar trend was reported by Yao, Li, Dhital, Tian,
and Guo (2020), who also found that the hardness of the noodles
Table 2
decreased with the extension of over-cooking time. Clearly, the textural
Effect of gluten quality on the dough rheological properties of the reconstituted
quality and textural deterioration of the cooked noodles made from
wheat flour.
different reconstituted wheat flour were different (Fig. 1). After 30 min
Samples ID WA (%) DDT (min) DST (min) Degree of softening (Nm)
of immersion, the values of the hardness of CN-1 and CN-2 were 21.48 N
RWF-1 62.2 ± 0.1d 6.7 ± 0.3c 14.8 ± 0.3c 0.03 ± 0.00c and 23.14 N, respectively, which were higher than these of CN-3 (20.31
RWF-2 62.7 ± 0.0c 6.3 ± 0.6c 14.0 ± 0.0c 0.04 ± 0.00b N), CN-4 (19.19 N), CN-5 (17.25 N), and CN-6 (17.71 N). Although the
RWF-3 64.8 ± 0.1a 8.3 ± 0.3a 17.2 ± 1.3b 0.01 ± 0.00d
RWF-4 64.9 ± 0.3a 8.2 ± 0.8a 10.8 ± 0.8d 0.06 ± 0.00a
final hardness of CN-2 was higher than that of CN-1, the rate of textural
RWF-5 63.1 ± 0.2b 7.8 ± 0.6ab 19.2 ± 0.3a 0.01 ± 0.00d deterioration (data not shown) was lower for CN-1. Similarly, the final
RWF-6 62.9 ± 0.1bc 7.0 ± 0.5bc 10.5 ± 0.5d 0.05 ± 0.00b values of the tensile distance of CN-1 and CN-2 were higher than those of
Means with different small letter superscripts within the same column are sig­
the other four cooked noodles. Additionally, the declining rate of the
nificantly different at p < 0.05. WA, DDT, and DST are water absorption, dough tensile distance of CN-1 was slower than that of CN-2.
development time and dough stabilisation time, respectively. RWF represents Liu, Guo, and Zhu (2019) found that the hardness and tensile force of
the reconstituted wheat flour. frozen cooked noodles reduced during frozen storage, due to the
reduction of integrity and compactness of the gluten network. Unlike

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Z.-B. Cao et al. Food Hydrocolloids 119 (2021) 106842

Table 3
Effect of gluten quality on the cooking properties of noodles.
Samples ID Water absorption (%) Cooking loss (%)

0 min 10 min 20 min 30 min

CN-1 46.6 ± 0.6b 101.6 ± 3.7b 134.4 ± 0.3b 157.8 ± 5.6b 4.8 ± 0.0b
CN-2 47.9 ± 0.8b 102.0 ± 3.7b 136.3 ± 10.4b 161.2 ± 1.3b 4.8 ± 0.1b
CN-3 53.1 ± 1.7a 111.5 ± 1.7a 156.7 ± 5.1a 174.9 ± 1.0a 5.1 ± 0.1a
CN-4 52.4 ± 3.4a 110.4 ± 3.3a 150.9 ± 2.6a 173.1 ± 0.1a 5.1 ± 0.2a
CN-5 48.5 ± 1.3b 106.1 ± 2.4ab 136.7 ± 8.4b 172.5 ± 2.1a 5.2 ± 0.2a
CN-6 49.3 ± 0.0b 106.0 ± 4.1ab 139.5 ± 3.7b 170.4 ± 2.9a 5.2 ± 0.1a

Means with different small letter superscripts within the same column are significantly different at p < 0.05. CN represents the
cooked noodles made from reconstituted wheat flour.

frozen cooked noodles, the textural attenuation of the cooked noodles gluten network, thus causing the hardness and tensile distance of the
might be caused by excessive water absorption and continuous input of cooked noodles to decline.
waste heat. In this process, starch granules expanded or even dis­
integrated, which may destroy the integrity of starch granules (Yao
et al., 2020). Furthermore, heat input weakened the strength of the 3.4. Effect of gluten quality on water distribution and migration in the
cooked noodles

3.4.1. Effect of gluten quality on water distribution in the cooked noodles


Two peaks were detected in the cooked noodles (Fig. 2(A)), one at
relatively short times (0.1–10 ms) and the other at relatively long times
(10–100 ms). This indicated that multiple water domains existed in the
cooked noodles, which was consistent with the results reported by
Kontogiorgos, Goff, and Kasapis (2008). Concerning the peak between
0.1 and 10 ms, a right-shift trend was observed in the cooked noodles.
Another peak (10–100 ms) showed the same right-shift trend. This
suggested that the interaction between water and other components in
the cooked noodles was weakened with the prolongation of immersion
time. An obvious increased relaxation peak area was observed with the
prolongation of immersion time between 10 and 100 ms, indicating that
more free water existed as a result of the excessive water absorption (Li
et al., 2012).
The results of the transverse relaxation time (T22) of the cooked
noodles are shown in Table 4. The relaxation times (T22) of the cooked
noodles increased in all the samples with the prolongation of immersion
time. However, after 10 min of immersion, the relaxation times (T21)
(data are not shown) and the relaxation peak area (0.1–10 ms) of the
cooked noodles barely changed. The results indicated that weakly bound
water was more susceptible to the immersion process than strong bound
water. In other words, the water absorbed by the cooked noodles in the
immersion process was mainly converted into weakly bound water.
Moreover, after 30 min of immersion, the relaxation times (T22) of CN-1,
CN-2, and CN-3 were shorter than those of the other three samples. As to
CN-1 and CN-2, the short T22 was mainly due to low water absorption
and a dense gluten network (Li et al., 2012). Concerning CN-3, the short
T22 may be related to a dense gluten network.

3.4.2. Effect of gluten quality on water migration in the cooked noodles


MRI was considered an effective tool for tracking water migration
during processing (Liu et al., 2013). In this study, MRI was used to
evaluate the water migration of the cooked noodles during immersion.
MRI pseudo-colour images for each of the immersion times are shown in
Fig. 2(B).
After cooking, the surface of the cooked noodles was surrounded by
red areas with high water content, while the inner part was blue, indi­
cating low water content. With the prolongation of immersion time, the
water penetrated gradually from the surface to the interior of the cooked
noodles. Similarly, Horigane et al. (2006) studied the effect of cooking
time on water distribution in cooked spaghetti. It was also found that the
Fig. 1. Effect of gluten quality on texture properties of the cooked noodles with water penetrated from the surface to the interior of the cooked spaghetti
different immersion time; A) the fitting curve for hardness reduction; B) the when the cooking time was prolonged. Unlike CN-1 and CN-2, the
fitting curve for tensile distance reduction. CN represents the cooked noodles pseudo-colour diagram of CN-3 to CN-6 showed a large red area with
made from reconstituted wheat flour. high water content after they were immersed for 30 min. The results

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Z.-B. Cao et al. Food Hydrocolloids 119 (2021) 106842

Table 4
Effect of gluten quality on water distribution of the cooked noodles with
different immersion time.
Samples ID Relaxation times (T22, ms)

0 min 10 min 20 min 30 min

CN-1 30.6 ± 2.3b 37.7 ± 0.0c 43.3 ± 0.0b 43.3 ± 0.0b


CN-2 28.5 ± 0.0c 37.7 ± 0.0c 43.3 ± 0.0b 43.3 ± 0.0b
CN-3 28.5 ± 0.0c 32.8 ± 0.0d 38.6 ± 2.3c 43.3 ± 0.0b
CN-4 37.7 ± 0.0a 43.3 ± 0.0a 49.8 ± 0.0a 49.8 ± 0.0a
CN-5 28.5 ± 0.0c 39.5 ± 2.9b 48.7 ± 2.7a 49.8 ± 0.0a
CN-6 27.2 ± 1.9c 37.7 ± 0.0c 43.3 ± 0.0b 49.8 ± 0.0a

Means with different small letter superscripts within the same column are sig­
nificantly different at p < 0.05. CN represents the cooked noodles made from
reconstituted wheat flour.

Table 5
The glutenin-gliadin ratio and GMP content of the reconstituted wheat flour.
Samples Glutenin Gliadin glutenin- GMP content
ID content (%) content (%) gliadin ratio (mg/g)

RWF-1 47.3 ± 0.6b 52.7 ± 0.6b 0.9 ± 0.0b 21.7 ± 0.7a


RWF-2 46.8 ± 0.1b 53.2 ± 0.1b 0.9 ± 0.0b 21.5 ± 0.1a
RWF-3 44.6 ± 1.0c 55.4 ± 1.0a 0.8 ± 0.0c 21.4 ± 0.1a
RWF-4 44.7 ± 0.4c 55.3 ± 0.4a 0.8 ± 0.0c 19.0 ± 0.2b
RWF-5 45.3 ± 0.4c 54.8 ± 0.4a 0.8 ± 0.0c 16.4 ± 0.1c
RWF-6 49.4 ± 0.2a 50.6 ± 0.2c 1.0 ± 0.0a 16.1 ± 0.1c

Means with different small letter superscripts within the same column are sig­
nificantly different at p < 0.05. RWF represents the reconstituted wheat flour.

noodles during immersion. The possible reasons are as follows: 1) when


the glutenin-gliadin ratio was high, there were not enough gliadin to fill
and adhere the gluten network, thus enabling the easy penetration of
water molecules; 2) when the glutenin-gliadin ratio was low, there was a
lack of glutenin needed to form a tight gluten network, which made it
difficult to hinder the penetration of water (Bruneel et al., 2016). Similar
results were also found by Li, et al., 2020, who reported that the texture
properties of noodles could be improved by optimising the
glutenin-gliadin ratio.
Since the small molecule glutenin does not participate in the for­
mation of the network skeleton of the gluten (Wang et al., 2017), the
GMP content was further determined in the present study. As shown in
Table 5, RWF-1, RWF-2, and RWF-3 had a high GMP content, while
RWF-5 and RWF-6 had a low GMP content. Usually, a high GMP content
can lead to a more condensed gluten network (Gupta, Khan, &
Macritchie, 1993).

3.6. Effect of gluten quality on the microstructure of gluten network in


cooked noodles
Fig. 2. Effect of gluten quality on water distribution and migration of the
cooked noodles with different immersion time: A) changes of water distribu­ The results of the CLSM of the gluten network in the cooked noodles
tion; B) MRI images. CN represents the cooked noodles made from reconstituted are shown in Fig. 3(A). CN-1, CN-2, and CN-3 possessed a relatively
wheat flour. compact and continuous gluten network. A dense gluten network
structure of noodles could restrain the intrusion of water and reduce the
were in line with the increase of water absorption of the cooked noodles, cooking loss rate, and could better maintain the hardness and elasticity
where the water absorption increased with the prolongation of immer­ of the cooked noodles during immersion. However, clear differences
sion time. were noticed in CN-4, CN-5, and CN-6, which had loose gluten networks
with lots of small fragments. This may have been caused by the low
aggregation of gluten due to the weak molecular force (Lambrecht,
3.5. Glutenin-gliadin ratio and GMP content of the reconstituted wheat Rombouts, Nivelle, & Delcour, 2017b). Loose gluten networks are not
flour conducive to maintaining the textural quality of the cooked noodles
during immersion, which may be improved by adding additives. For
Table 5 showed that RWF-6 had the highest glutenin-gliadin ratio, instance, Jia et al. (2019) found that a strengthened entanglement was
RWF-1 and RWF-2 possessed medium glutenin-gliadin ratios. However, formed in the clustered network of noodles, especially at the low levels
the values were low in RWF-3, RWF-4, and RWF-5. Considering the of alkali addition. Wee and Henry (2019) also claimed that trans­
results of the texture (Fig. 1), this may indicate that a proper glutenin- glutaminase could promote protein cross-linking to form a dense gluten
gliadin ratio was beneficial to the textural stability of the cooked network structure.

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Z.-B. Cao et al. Food Hydrocolloids 119 (2021) 106842

Fig. 3. Effect of gluten quality on the microstructure of gluten network: A) CLSM micrographs of gluten network and its fitting diagram; B) the analysis results of the
CLSM micrographs: (a) proteins area (%); (b) the total number of junctions; (c) total chain length; (d) lacunarity. CN represents the cooked noodles made from
reconstituted wheat flour.

Furthermore, the differences in the gluten network were quantified high. Zou, Yang, Gu, and Wang (2019) also quantitatively analyzed the
by protein area, the total number of junctions, total chain length, and network structure features of gluten. They found that frozen gluten had
lacunarity (Fig. 3(B)). The protein percentage areas of CN-1, CN-2, and larger mesh pores and a smaller protein area compared with the fresh
CN-3 were higher than CN-4, CN-5, and CN-6, which was consistent with gluten during heating, which was also due to the restriction aggregation
their GMP content. Similarly, as to the total number of junctions and of gluten. The high protein area indicated that a dense gluten network
total chain length, the values of CN-1, CN-2, and CN-3 were higher than was formed in the cooked noodles, which indirectly resulted in low
CN-4, CN-5, and CN-6. Conversely, a low lacunarity in CN-1, CN-2, and lacunarity. Furthermore, the total number of junctions may be related to
CN-3 was observed, while the lacunarity of CN-4, CN-5, and CN-6 was the degree of protein cross-linking, which could affect its total chain

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Z.-B. Cao et al. Food Hydrocolloids 119 (2021) 106842

Fig. 3. (continued).

Table 6
Effect of gluten quality on the molecular force between gluten molecules in the cooked noodles.
Samples ID Immersion time (min) Extractable proteins (mg/mL)

B1 B2 B3 B4 B5 B6

CN-1 0 0.24 ± 0.01a 0.94 ± 0.02ab 0.70 ± 0.03a 0.32 ± 0.03a 2.11 ± 0.03d 1.59 ± 0.06a
10 0.24 ± 0.02a 0.93 ± 0.01ab 0.68 ± 0.01a 0.33 ± 0.01a 2.28 ± 0.01c 1.55 ± 0.16ab
20 0.23 ± 0.02a 0.89 ± 0.01b 0.66 ± 0.05a 0.33 ± 0.05a 2.33 ± 0.02b 1.51 ± 0.02ab
30 0.22 ± 0.01a 0.95 ± 0.04a 0.64 ± 0.01a 0.32 ± 0.01a 2.40 ± 0.02a 1.40 ± 0.07b
CN-2 0 0.13 ± 0.01a 0.90 ± 0.05a 0.53 ± 0.01a 0.16 ± 0.01a 2.25 ± 0.02a 1.54 ± 0.02a
10 0.14 ± 0.03a 0.87 ± 0.07a 0.43 ± 0.01b 0.17 ± 0.01a 2.19 ± 0.04bc 1.41 ± 0.08b
20 0.13 ± 0.02a 0.82 ± 0.03a 0.41 ± 0.04b 0.19 ± 0.04a 2.16 ± 0.02c 1.40 ± 0.02b
30 0.12 ± 0.01a 0.88 ± 0.03a 0.36 ± 0.03c 0.18 ± 0.03a 2.21 ± 0.01ab 1.35 ± 0.03b
CN-3 0 0.14 ± 0.01ab 0.85 ± 0.01a 0.65 ± 0.03a 0.20 ± 0.03a 1.99 ± 0.02b 1.63 ± 0.04a
10 0.16 ± 0.01a 0.86 ± 0.00a 0.58 ± 0.02b 0.19 ± 0.02a 2.07 ± 0.07ab 1.61 ± 0.10a
20 0.13 ± 0.01ab 0.74 ± 0.01b 0.56 ± 0.01bc 0.19 ± 0.01a 2.13 ± 0.05a 1.54 ± 0.06a
30 0.12 ± 0.02b 0.73 ± 0.01b 0.51 ± 0.01c 0.19 ± 0.01a 2.05 ± 0.01ab 1.25 ± 0.06b
CN-4 0 0.18 ± 0.02a 0.88 ± 0.02a 0.59 ± 0.01a 0.22 ± 0.01a 1.95 ± 0.07b 1.53 ± 0.10a
10 0.15 ± 0.01a 0.84 ± 0.02b 0.48 ± 0.02b 0.21 ± 0.02a 2.07 ± 0.06ab 1.36 ± 0.10b
20 0.16 ± 0.02a 0.84 ± 0.01b 0.48 ± 0.01b 0.20 ± 0.01a 2.14 ± 0.07a 1.35 ± 0.05b
30 0.16 ± 0.01a 0.83 ± 0.01b 0.47 ± 0.01b 0.21 ± 0.01a 2.11 ± 0.09a 1.31 ± 0.04b
CN-5 0 0.23 ± 0.02a 0.91 ± 0.03b 0.73 ± 0.01a 0.36 ± 0.01a 1.99 ± 0.10b 1.69 ± 0.18a
10 0.22 ± 0.03a 1.01 ± 0.09a 0.66 ± 0.04b 0.36 ± 0.04a 2.14 ± 0.07a 1.64 ± 0.17a
20 0.21 ± 0.01a 0.93 ± 0.02ab 0.65 ± 0.00b 0.30 ± 0.00b 2.12 ± 0.01a 1.60 ± 0.18a
30 0.21 ± 0.01a 0.89 ± 0.01b 0.58 ± 0.02c 0.30 ± 0.02b 1.95 ± 0.01b 1.40 ± 0.14a
CN-6 0 0.13 ± 0.01a 0.64 ± 0.01b 0.42 ± 0.02a 0.18 ± 0.02a 1.92 ± 0.06c 1.18 ± 0.06a
10 0.11 ± 0.02a 0.65 ± 0.01b 0.40 ± 0.01ab 0.18 ± 0.01a 2.01 ± 0.03b 1.15 ± 0.01a
20 0.13 ± 0.01a 0.66 ± 0.02b 0.39 ± 0.01ab 0.17 ± 0.02a 2.05 ± 0.03b 1.14 ± 0.01a
30 0.13 ± 0.02a 0.68 ± 0.01a 0.38 ± 0.01b 0.16 ± 0.01a 2.18 ± 0.05a 1.13 ± 0.02a

Means with different small letter superscripts within the same column are significantly different at p < 0.05. B1: 30 mM Tris-HCL buffer; B2: 30 mM Tris-HCL buffer
containing 1% SDS; B3: 30 mM Tris-HCL buffer containing 6M urea; B4: 30 mM Tris-HCL buffer containing 2% β-mercaptoethanol; B5: 30 mM Tris-HCL buffer
containing 2% β-mercaptoethanol and 1% SDS; B6: 30 mM Tris-HCL buffer containing 6 M urea and 1% SDS. CN represents the cooked noodles made from recon­
stituted wheat flour.

8
Z.-B. Cao et al. Food Hydrocolloids 119 (2021) 106842

length. Author statement

3.7. Effect of gluten quality on the molecular force between gluten Zong-Bao Cao: Conceptualization, Methodology, analysis and inter­
molecules in the cooked noodles pretation of the data, Writing - original draft. Chen Yu: Data curation,
Writing - reviewing and editing. Zhen Yang: Writing - reviewing and
To elucidate the difference in the integrity of the gluten network, the editing. Jun-Jie Xing: Writing - reviewing and editing. Xiao-Na Guo:
molecular force between gluten molecules in different cooked noodles Supervision, Funding acquisition, Writing - reviewing and editing. Ke-
was measured. The molecular force between gluten molecules was Xue Zhu: Supervision, Funding acquisition, Writing - reviewing and
described with the solubility of proteins in different reducing solvents. editing.
SDS was reported to disrupt hydrogen bonds and hydrophobic in­
teractions, urea to disrupt hydrogen bonds, and β-mercaptoethanol to
cleave S–S to SH-free (Liao, Liu, Zhao, Zhao, & Cui, 2011). As is shown in Declaration of competing interest
Table 6, the solubility of proteins in the reducing solvents is listed as
follows: SDS and β-mercaptoethanol (B5) > SDS and urea (B6) > SDS The authors have declared no conflicts of interest.
(B2) > urea (B3) > β-mercaptoethanol (B4) > the control (B1).
Furthermore, hydrogen bonds and hydrophobic interactions have strong References
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