European Polymer Journal 136 (2020) 109945

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European Polymer Journal

journal homepage: www.elsevier.com/locate/europolj

Preparation, characterization of feather protein-g-poly(sodium allyl T

sulfonate) and its application as a low-temperature adhesive to cotton and
viscose fibers for warp sizing
Wei Li , Zhengyu Yu, Youkang Wu, Qian Liu
⁎

College of Textiles and Garments, Anhui Polytechnic University, Wuhu 241000, Anhui Province, China

ARTICLE INFO ABSTRACT

Keywords: Fulfilling high-valued utilization of feather wastes will favor overcoming environmental issues and promoting
Feather protein the poultry farmers’ income. This study developed a new bio-based protein sizing agent [feather protein-g-poly
Characterization (sodium allyl sulfonate) (FP-g-PSAS)] with high adhesion capacity to viscose and cotton fibers at low tem­
Graft copolymerization perature, through graft copolymerization of feather protein with SAS monomer by building an ammonium
Adhesion
persulfate (APS)/eSH groups (on the protein chains) redox system. Fourier transform infrared (FTIR) spectro­
scopy and energy dispersive x-ray spectrometer (EDS) demonstrated the successful preparation of FP-g-PSAS
samples. The samples were also characterized by scanning electron microscopy (SEM), thermogravimetric (TG)
and x-ray diffraction (XRD). Viscosity, water-solubility, light transmittance and adhesion of the samples were
investigated. The FP-g-PSAS exhibited high water-solubility and light transmittance. Compared with feather
protein, an increased viscosity and an improved adhesion to both fibers for FP-g-PSAS samples were exhibited at
60 °C. With the rises in grafting ratios, viscosity and adhesion strengths to both fibers gradually increased. The
FP-g-PSAS samples had the similar adhesion strengths in comparison with the modified starches investigated in
our previous works. These results indicated that FP-g-PSAS showed the potential in the application of viscose and
cotton warp sizing at a low temperature of 60 °C.

1. Introduction environmental issues produced by the landfill and incineration, and

According to the statistics of the Food and Agriculture Organization
of the United Nations in 2017, China shared the 88.8% of the combined
number of geese and guinea fowls in the world [1], implying that a
large number of feathers as a by-product of the poultry industry would
be produced in China. Feathers have some good characterizations such
as easy availability, renewability and biodegradability. However, most
of the feathers as a protein-rich resource are disposed as solid waste in
landfill and incineration [2], taking up precious land and causing a
waste of protein resources [3]. Moreover, more than 80% composition
in the feathers is protein, which cannot be degraded naturally in a short
period of time by the traditional landfill and incineration, resulting in a
great burden on the environment.
Fulfilling high-valued utilization of feather wastes by adopting them
to produce cheap and low-cost products, will favor overcoming
raising the poultry farmers’ income. Some works have referred to the
utilization of feather wastes as animal feed and reinforcement in com­
posite materials, etc. [4–6], but their utilization still be limited. To
widen the application range of feather-based materials in industry,
some works about preparing feather-based thermoplastics by physical
and/or chemical modifications [7–9], and extracting feather protein to
promote its thermoplastic application [10], have been performed in
recent years. Besides, the protein directly utilized as textile sizing agent
has also been attempted [11,12]. Nevertheless, an important limitation
of the raw feather protein used as textile sizing agent is its low water-
solubility. Although the addition of alkali substance can dissolve the
protein in water and solve the issue of low water-solubility, the alkali
can hydrolyze the protein and lower its cohesive strength, thereby
leading to a serious damage to the mechanical properties of some alkali-
sensitive fibers. At this situation, it will be considerably important to

Abbreviations: FP-g-PSAS, feather protein-g-poly(sodium allyl sulfonate); APS, ammonium persulfate; FTIR, Fourier transform infrared; EDS, energy dispersive x-ray
spectrometer; SEM, scanning electron microscopy; TG, thermogravimetric; XRD, X-ray diffraction; SAS, sodium allyl sulfonate; PSAS, poly(sodium allyl sulfonate);
GPC, gel permeation chromatography; RH, relative humanity
⁎
Corresponding author.
E-mail addresses: fangzhiliweiwu@sina.com, liw@ahpu.edu.cn (W. Li).

https://doi.org/10.1016/j.eurpolymj.2020.109945
Received 23 June 2020; Received in revised form 27 July 2020; Accepted 3 August 2020
Available online 06 August 2020
0014-3057/ © 2020 Elsevier Ltd. All rights reserved.
W. Li, et al.
explore an efficient means of altering the structure of feather protein for
improving its water-solubility and exerting a strong adhesion for the
protein to fibers.
Graft copolymerization has been considered as an efficient chemical
modification to prepare the chemically modified polymers such as
grafted starches [13–15] and has a significant effect on improving the
properties of starch. One or more kinds of grafted branches can be in­
corporated onto polymer chains through the copolymerization [16].
Accordingly, grafting feather protein with hydrophilic monomer such
as sodium allyl sulfonate (SAS) for incorporating hydrophilic poly(so­
dium allyl sulfonate) (PSAS), will be a good choice to improve the
water-solubility of raw protein. Additionally, high adhesion to fibers
has been perceived to be an essential feature and extremely important
behavior for any kind of sizing agent [17]. This is because the sizing
agent with high adhesion not only can strengthen the strength of warps,
but also can diminish the hairs of warp yarns during warp sizing [18].
Therefore, the adhesion capability has been considered as an important
index for revealing the quality of a sizing agent.
Apparently, sizing temperature of the paste in size box depends on
the types of fibers and sizing agents. For staple fiber warps, their sizing
can be divided into high- and low-temperature sizing according to paste
temperature. When the temperature exceeds 95 °C, the sizing is known
as high-temperature sizing, while the temperature is lower than 80 °C, it
is named as low-temperature sizing [19]. Cotton and viscose fibers have
been widely applied in textile clothes. During the cotton warp sizing,
the paste in size box is usually maintained at 95–99 °C [20], which will
consume a large amount of steam energy for keeping the high tem­
perature during the whole sizing operation [21]. Undoubtedly, there is
an urgent demand to lower the temperature in cotton warp sizing for
saving energy. It has been speculated that one difficulty in decreasing
paste temperature during cotton warp sizing is the existence of non­
cellulosic wax [22,23] on the fiber surfaces. The melting point of the
wax is in the range of 70–80 °C [24], which can not be removed from
the surfaces of cotton fibers and dispersed in the paste at the tem­
perature of below the melting point. The wax imparts hydrophobic
nature on the fiber surface, impedes wetting and wicking [25,26] of the
paste, and subsequently retards the impregnation of paste into warp
yarns. Fortunately, our previous work pointed out a method that cotton
warp or roving was treated with 95 °C of distilled water for 10 min
before sizing [27]. In addition, viscose belongs to heat-sensitive fiber,
which is because the strength of viscose warp yarns will be greatly
decreased if they are subjected to high-temperature sizing process. As a
result, sized warp property, loom efficiency and fabric quality will be
seriously influenced during the process. To fulfill a good application in
the sizing of viscose and cotton warps, it will be of great significant to
obtain a strong adhesion for protein after graft copolymerization with
hydrophilic SAS to viscose and cotton fibers at low temperature.
Furthermore, some works have investigated the extraction of
feather protein with the hydrolysis method [28–30]. During the in­
itiation systems of oxidation, redox and radiation, redox system is
known as the most common method [9]. In this work, we attempt to
partially reduce the disulfide bonds of feather protein to eSH groups,
and then build a redox system consisting of ammonium persulfate (APS)
and eSH groups in the protein molecules to form the active sites on the
eSH groups for grafting hydrophilic PSAS branches. The hydrophilic
PSAS branches will be able to improve the water-solubility of feather
protein, and absorb water and store it within the protein adhesive
layers formed from protein solution. The water stored and steric hin­
drance of the grafted branches are probably to exert plasticization for
the layers, favoring adhesion. As a result, the hydrophilic SAS monomer
is selected for preparing the bio-based feather protein-g-PSAS (FP-g-
PSAS) by the APS/eSH groups redox system, as shown in Fig. 1.
Currently, no attempt at preparing the bio-based FP-g-PSAS by
building an APS/eSH groups redox system and further applying it as an
adhesive to bond viscose and cotton fibers for revealing its potential in
the application of viscose and cotton warp sizing at low temperature.
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European Polymer Journal 136 (2020) 109945
Therefore, the important objectives of this work are to reveal if the FP-
g-PSAS has higher adhesion to both fibers than raw feather protein at
low temperature, and to determine if the FP-g-PSAS exhibits higher
adhesion to both fibers at low temperature in comparison with modified
starches for confirming its potential in the low-temperature sizing of
cotton and viscose warps. The obtained FP-g-PSAS samples were char­
acterized by Fourier transform infrared (FTIR) spectroscopy, scanning
electron microscopy (SEM), energy dispersive x-ray spectrometer
(EDS), thermogravimetric (TG) and x-ray diffraction (XRD). Besides,
the measurements on grafting ratios were performed, and the influences
of the PSAS branches introduced on apparent viscosities, light trans­
mittances, water-solubility and low-temperature adhesion to viscose
and cotton fibers were evaluated.
2. Materials and methods
2.1. Materials
Feathers were kindly offered by Guqi Feather & Down Co., Ltd.
(Wuhu, China). SAS was purchased from Aladdin Industrial
Corporation (Shanghai, China). The other analytically pure chemicals
such as ethanol, hydrochloric acid, sodium bisulfite, urea, sodium hy­
droxide, sodium dodecyl sulfate, ammonium persulfate, were obtained
from Shanghai Maclean Biochemical Technology Co., Ltd. (Shanghai,
China) and used directly. The pure cotton roving (372 tex) and viscose
one (590 tex), adopted for adhesion measurement, were obtained from
Anhui Huamao Group Co., Ltd. (Anhui, China) and Tianyi Textile Co.,
Ltd. (Jiangsu, China), respectively.
2.2. Graft copolymerization of feather protein extracted
The feathers were firstly treated for obtaining feather protein ac­
cording to the work [31]. Mw of the feather protein extracted was
analyzed by gel permeation chromatography (GPC, PL-GPC220, Eng­
land), and the result was 9.5 × 104.
Subsequently, the protein extracted was pre-treated with NaHSO3
for increasing the content of eSH groups in the protein molecules, and
then applied for performing the graft polymerization with SAS by an
APS/eSH groups (on the protein chains) redox system. Briefly, dried
feather protein (100 g) and NaHSO3 (20 g) were dispersed in 8 M urea
aqueous solution (300 mL). The mixture was transferred into a 1000 mL
four-necked flask, heated to 70 °C and maintained at this temperature
for 1 h under mechanical agitation. Then, the pre-treated protein was
precipitated, washed and freeze-dried in vacuum. Subsequently, the
pre-treated protein was dissolved in 8 M urea aqueous solution
(300 mL). After having been degassed with N2 for 30 min, APS solution
(40 wt%) and a certain amount (indicated in Fig. 5) of SAS were
dropped into the pre-treated protein solution over a 30–40 min period.
The reaction was maintained for 3 h at 70 °C under N2 atmosphere.
Then, 2% paradioxybenzene solution (1 mL) was added to terminate
the copolymerization. Finally, the product was precipitated by ad­
justing the pH to approximately 4, washed thoroughly with ethanol and
distilled water for removing the residual SAS, chemicals and PSAS
homopolymer formed, and then the resulting product was freeze-dried
in vacuum for obtaining the FP-g-PSAS samples. The chemical structure
of the FP-g-PSAS is presented in Fig. 1.
2.3. Characterizations of the FP-g-PSAS samples
Before characterization, to avoid the possible residual of the PSAS
homopolymer in the FP-g-PSAS sample, FP-g-PSAS sample was further
purified with methanol for 24 h using Soxhlet’s extractor [32].
Before the determination of grafting ratio, acidification of purified
FP-g-PSAS sample was carried out according to our previous work [33].
Subsequently, back titration with HCl [34,35] was used to determine
the percentage content (S, %) of PSAS branches in the FP-g-PSAS.
W. Li, et al.
Fig. 1. Graft copolymerization of feather protein with SAS by building an APS/eSH groups redox system.
Grafting ratio (GR, %) was calculated using Eq. (1).
S
GR = × 100%
100 S (1)
Scanning electron microscope (Hitachi S-4800, Tokyo, Japan)
technique was applied for analyzing the surface morphologies of
feather protein and FP-g-PSAS samples after having been covered by a
conducting gold layer.
To demonstrate the successful incorporation of PSAS branches in the
protein molecules, the chemical compositions of the protein samples
before and after graft copolymerization were characterized by the SEM
equipped with an energy dispersive x-ray spectrometer.
To evaluate the difference in the thermal stability, feather protein
and FP-g-PSAS were underwent the TG analysis on a DTG-60H
((Shimadzu Co. Ltd., Kyoto, Japan) from 25 °C to 600 °C at 20 °C/min
and N2 atmosphere with a flow rate of 200 mL/min.
The XRD patterns of feather protein and FP-g-PSAS were collected
by a XRD-6000 x-ray diffractometer (Shimadzu Co., Japan) using a
wavelength of 0.154 nm Cu Ka radiation at 30 mA and 40 kV range. The
scattering angle (2θ) was in the range of 10-50° in a step width of 0.02°.
2.4. Determinations of viscosity and water-solubility
The apparent viscosities of protein sample aqueous solutions were
measured using a NDJ-79 rotary viscometer (Electrical and Mechanical
Plant, Shanghai, China) according to the literature [36]. Briefly, protein
sample was dissolved in distilled water at 60 °C and maintained at this
temperature for 1 h under mechanical stirring with a speed of 120 r/
min to form a protein aqueous solution (6%, w/w). Viscosity of the
protein solution was measured in duplicate by the viscometer with a
shear rate of 3550 s−1 (viscosity < 10 mPa·s) at 60 °C, and the average
was reported.
Protein sample and distilled water were added into a test tube, and
heated up to 60 °C in an oscillating water bath for 1 h to form a protein
aqueous solution (1%, w/w). Then, the tube was placed vertically at
room temperature for 6 h, and its digital photograph was taken for
evaluating the water-solubility of protein sample.
2.5. Determination of adhesion to fibers
The adhesion of feather protein and FP-g-PSAS to cotton and viscose
fibers was determined according to a legal standard method (FZ/T
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European Polymer Journal 136 (2020) 109945
15001-2008) in China. The determination method of the adhesion in­
cludes three steps: formation of protein aqueous solution, immersing
roving and drying in air, and drawing test of dried roving. Briefly,
protein sample was dissolved in distilled water in a water bath at 60 °C
to form a 1% (w/w) sample aqueous solution. Then, the rectangular
steel frames, onto which cotton and viscose roving had been carefully
wound, respectively, were immersed into the solution (60 °C) for 5 min,
and subsequently the immersed roving were dried in air. Then, the
dried roving were equilibrated at 65% relative humanity (RH) and
20 °C for 24 h, and their adhesion strengths were determined with a
YG026D Electronic Strength Tester (Ningbo Textile Instrument Factory,
Zhejiang, China) according to the literature [37]. In each case, the data
reported was expressed as the average and standard deviation of 20
successful tests.
2.6. Determination of light transmittance
Light transmittance of protein sample aqueous solution (1 wt%) was
measured by the Craig’s method [38]. Briefly, dried protein sample
(1 g) was completely dissolved in distilled water (99 mL) in a water
bath at 60 °C under consistent agitation. Then, percent transmittance
was determined in duplicate using an UV9600 spectrophotometer (Ruili
Analytical Instrument Co., Ltd., Beijing, China) against distilled water
blank, and the mean value was reported.
2.7. Statistical analysis
Statistical significance was estimated with one-way analysis of
variance using Origin 6.0 software (OriginLab Inc., USA). The data
obtained were considered significantly different at p < 0.05. In
Figs. 12 and 13, data points with the different small letter were sta­
tistically significantly different from each other.
3. Results and discussions
3.1. Extraction of feather protein and its graft copolymerization
The extraction process and graft copolymerization of feather protein
are represented in Fig. 2 and Fig. 1, respectively, which mainly involve
the following steps. Feathers were cleaned by washing and drying, and
the dried feathers are shown in Fig. 3(a) (I). A pre-treatment of the
dried feathers with ethanol and HCl was performed for removing the
W. Li, et al.
Fig. 2. Extraction process of feather protein and its graft copolymerization.
organic substances and destroying the hydrogen bonds and ionic ones
on the protein chains, respectively (II). A further pre-treatment with
NaHSO3 was carried out for increasing the content of the eSH groups
on the protein chains which favored the extraction of the protein in the
next step (III). The protein pre-treated with NaHSO3 was extracted with
urea and sodium hydroxide at the protection of sodium dodecyl sulfate
(IV). The protein extracted was precipitated, washed with ethanol
several times, and freeze-dried in vacuum to obtain the raw feather
protein, as presented in Fig. 3(b) (V). After the reduction of eSeSe to
eSH in the protein molecules with NaHSO3, the APS was selected to
build a redox system with the eSH groups for performing the graft
copolymerization of the reduced protein with SAS monomer in an 8 M
urea aqueous medium (VI). The grafted protein (FP-g-PSAS) could be
observed in Fig. 3(c).
3.2. Chemical mechanism of the graft copolymerization of feather protein
The chemical mechanism of synthetizing the FP-g-PSAS samples
through graft copolymerization of feather protein with SAS by building
the eSH groups/APS redox system is illustrated in Fig. 4. To build the
redox system that is composed of APS and eSH groups on the protein
chains, the reduction of NaHSO3 to the disulfide bonds on the protein
chains (a) is firstly performed for raising the number of eSH groups on
the protein chains. And then the eSH groups are used to combine with
APS in an 8 M urea aqueous solution to form a redox-initiated copo­
lymerization system. The eSH groups can induce APS to decompose
and form sulfate radicals (b) while the hydrogen atoms of eSH groups
are transferred to sulfate radicals, thereby producing a lot of thiyl ra­
dicals on the protein chains and leading to the generation of protein
macro-radicals (c). The protein macro-radical is added to a double bond
of SAS monomer for forming the initiated protein SAS radical chain on
the feather protein (d). Then, the addition of SAS monomer to the in­
itiated chain propagates the growing chain grafted onto the feather
protein chains (e). Finally, the growing chain (grafted PSAS branch) can
be terminated via the reaction (g) to (j) with paradioxybenzene [39], or
through combination, coupling and disproportionation [40].
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European Polymer Journal 136 (2020) 109945
3.3. Determination of grafting ratio
Grating ratio denotes the percentage content of grafted branches on
protein sample. Grafting ratios of the FP-g-PSAS samples were de­
termined by an back titration method, and the results are depicted in
Fig. 5. It could be found that grafting ratios of the FP-g-PSAS samples
increased from 0% to 28.2%, as the amounts of SAS monomer to feather
protein raised from 0 g to 40 g. This indicated that FP-g-PSAS samples
with the grafting ratios of 0% to 28.2% could be obtained by the graft
copolymerization of feather protein with SAS monomer using a eSH
groups/APS redox system in an 8 M urea aqueous medium at 70 °C.
3.4. SEM analysis
Fig. 6 shows the surface morphologies of feather protein before and
after graft copolymerization collected by SEM analysis. It could be seen
from Fig. 6(a-b) that the feather protein extracted showed the surface
morphology of spherical and big aggregates. Compared with the ag­
gregates of feather protein, FP-g-PSAS had a lower aggregation and
exhibited the surface morphology of small and scattered fragments
(Fig. 6(c-d)). The variation in the morphology of the protein after graft
copolymerization is probably attributed that the formation of hydro­
philic PSAS branches and the reduction of the disulfide bonds in the
protein molecules obviously improve the dispersibility of feather pro­
tein in ethanol and distilled water during washing.
3.5. FTIR analysis
Fig. 7 depicts FTIR spectra of feather protein and FP-g-PSAS samples
for proving the successful introduction of PSAS branches on the protein
chains. The peaks appeared in the region: 3000–2800 cm−1 corre­
sponded to the characteristic absorption peaks of eCH2 and eCH3 [41].
The peaks at 1655 cm−1 and 1543 cm−1 corresponded to the amide I
and II, and the ones at 1234 cm−1 (feather protein) and 1230 cm−1
(FP-g-PSAS) corresponded to the amide III [41]. In addition, a new peak
appeared at 1041 cm−1 in the spectra of FP-g-PSAS, which belonged to
the symmetric stretching vibration of sulfonic ions [42,43], and there
W. Li, et al. European Polymer Journal 136 (2020) 109945

chemical compositions of polymer materials [44]. The chemical com­

positions of feather protein and FP-g-PSAS samples were tested by this
technique, as shown in Fig. 8(a) and (b), respectively. As found, ele­
mental compositions of the feather protein (Fig. 8(a)) mainly contained
C, O, N and S. As seen from Fig. 8(b), besides the four elements, the FP-
g-PSAS also included Na element, which existed in the SAS units of the
PSAS branches. The existence of Na element confirmed the successful
introduction of PSAS branches on the backbones of protein.

3.7. TG analysis

Thermal degradation behavior of feather protein before and after

grafting was evaluated by TG analysis and their TG curves are shown in
Fig. 9(a) and (b), respectively. TG results showed that FP-g-PSAS had a
similar initial thermal degradation temperature with feather protein,
and showed an approximately 6% of weight loss due to the removal of
bound and absorbed water. As the temperature exceeded the initial
degradation temperature, hydrogen bonds and disulfide bonds in the
protein molecules would be broken. As seen, when the temperature
exceeded 250 °C, weight loss of FP-g-PSAS was more than that of
feather protein, and the FP-g-PSAS was completely degraded at the
temperature of 590 °C, whereas the feather protein had a 4.4% of re­
sidual weight at 600 °C. This observation indicated that the introduc­
tion of the PSAS branches slightly reduced the thermal stability of
feather protein.

3.8. XRD analysis

XRD patterns of feather protein and FP-g-PSAS were collected, as

illustrated in Fig. 10. It could be found in the Fig. 10(a) that feather
protein displayed crystallinity from the peaks at approximately 17.8°
and 19°, which corresponded to the diffraction pattern of the α-helix
and typical of the β-sheet structure, respectively [45,46]. As observed
from Fig. 10(b), the FP-g-PSAS had a different XRD pattern, there was
no strong crystallinity peak at about 19° whereas there just displayed a
broad peak at about 19°, which indicated that the introduction of the
PSAS branches destroyed the crystalline structure of the protein, re­
sulted in the transformation of the protein from crystalline to amor­
phous state, and implied a remarked decrease in the β-sheet structure at
approximately 19°.

3.9. Influence of graft copolymerization

3.9.1. Influence on viscosity and water-solubility

Fig. 3. Digital photographs of feathers (a), feather protein (b) and FP-g-PSAS
(c).
was no sign of this peak in the spectra of feather protein, indicating the
successful introduction of PSAS branches on the protein chains.
3.6. EDS analysis
EDS technique has become an important method of determining the
Water-solubility and viscosity of FP-g-PSAS samples were estimated
and illustrated in Fig. 11(a) and (b), respectively. It could be observed
from Fig. 11(a) that the FP-g-PSAS samples could be completely dis­
solved in water, indicating that the introduction of the PSAS branches
obviously enhanced the water-solubility of feather protein. In addition,
as seen from Fig. 11(b), the viscosity of feather protein paste after graft
copolymerization increased, and the viscosity of FP-g-PSAS depended
on grafting ratio. The viscosity gradually increased as the ratio raised.
Apparently, the increased viscosity is mainly due to the hydrophilic
feature of the PSAS branches introduced. The hydrophilic branches
impart a hydrophilic feature to FP-g-PSAS, thereby obviously improving
the water-solubility of feather protein. In addition, the hydrophilicity
can increase the intermolecular interaction between protein and water,
thereby promoting the relaxation and extension of macromolecular
coils of the protein, and causing an increased friction resistance to the
flow of protein paste. As a result, the viscosity of FP-g-PSAS paste is
observed to increase compared with that of the raw protein one. The
more the PSAS branches, the stronger the relaxation and extension,
which result in a gradually increased viscosity as the ratio increases.

5
W. Li, et al.
Fig. 4. Chemical mechanism of graft copolymerization of feather protein with SAS using an APS/eSH groups redox system.
3.9.2. Influence on the adhesion of feather protein to viscose and cotton
fibers
The influence of graft copolymerization on the adhesion of feather
protein to viscose and cotton fibers is depicted in Figs. 12 and 13, re­
spectively. As seen, adhesion strengths (grafting ratio = 0%) of feather
protein to viscose and cotton fibers were 15.3 cN/tex and 14.6 cN/tex
at 60 °C, respectively. FP-g-PSAS samples were superior to feather
protein in the adhesion strengths to both fibers at 60 °C, implying that
the PSAS branches incorporated were able to improve the adhesion of
feather protein to both fibers at low temperature. The strengths of FP-g-
PSAS samples to both fibers depended upon the grafting ratios of SAS
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European Polymer Journal 136 (2020) 109945
monomer. As the ratios raised from 0 to 28.2%, the strengths gradually
increased from 15.3 to 17.5 cN/tex for viscose fibers while from 14.6 to
17.2 cN/tex for cotton ones. When the ratios were in the range of
22.1–28.2%, the strengths of FP-g-PSAS samples to both fibers were
significant differences with those of feather protein (p < 0.05). In
addition, we had ascertained that sulfosuccinylated starch
(DS = 0.0036) had a good low-temperature adhesion to viscose fibers
[47] while quaternized-sulfosuccinylated starch (DS = 0.0443) had a
good low-temperature adhesion to cotton fibers [27]. Therefore, to
reveal if the FP-g-PSAS had the potential in the low-temperature sizing
of viscose and cotton warps, we measured the strengths (17.0 cN/tex) of
W. Li, et al.
Fig. 5. Grafting ratios of FP-g-SAS samples prepared.
the sulfosuccinylated starch (DS = 0.0036) to viscose fibers and (16.8
cN/tex) of the quaternized-sulfosuccinylated starch (DS = 0.0443) to
cotton fibers at the temperature of 60 °C. By the comparison, it could be
seen that the strengths of FP-g-PSAS with a grafting ratio of 28.2% to
both fibers were higher than those of the modified starches, which in­
dicated that the FP-g-PSAS could be expected as a sizing agent in the
application of viscose and cotton warp sizing at low temperature.
Moreover, before being applied for low-temperature sizing, the starches
must be paste at 95 °C for 1 h and then reduced to a required low-
temperature for sizing. Undoubtedly, it will consume a lot of steam
energy for pasting the starch at 95 °C. However, the FP-g-PSAS can be
dissolved in water at 60 °C and used directly, inevitably reducing the
energy consumption. It is well known that starch paste trends to occur
Fig. 6. SEM micrographs of feather protein (a and b), and FP-g-PSAS (c and d).
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European Polymer Journal 136 (2020) 109945
Fig. 7. FTIR spectra of feather protein and FP-g-PSAS samples.
retrogradation at low temperature, which provides an obvious adverse
influence for low-temperature sizing [47]. In contrast, FP-g-PSAS paste
does not occur the retrogradation. Therefore, the FP-g-PSAS will show a
better application value in the low-temperature sizing of viscose and
cotton warps.
Obviously, there are a great number of disulfide bonds on the
feather protein chains, which seriously restrain the water-solubility of
feather protein. Therefore, raw feather protein extracted has a bad
water-solubility, and it needs to be dissolved in water with alkaline
substance [11]. However, although the alkaline substance can dissolve
the protein in water, it also can cause severe hydrolysis of the protein
chains [12] to polypeptide or even small peptide, thereby leading to an
obvious decreased cohesive strength of feather protein. The decreased
strength can make the reduction of interfacial interactions at the in­
terfaces between protein adhesive layers (formed from the protein
W. Li, et al.
Fig. 8. EDS images of feather protein (a) and FP-g-PSAS (b).
Fig. 9. TG curves of feather protein and FP-g-PSAS.
Fig. 10. XRD of feather protein (a) and FP-g-PSAS (b).
aqueous solution) and fibers. Consequently, it will be easy to involve
cohesive and interfacial failures which are described as the main frac­
ture forms of an adhesive joint according to the fracture location [48],
displaying a poor adhesion capacity to fibers.
The grafted feather protein samples prepared could be completely
dissolved in water at 60 °C under neutral condition, as shown in
Fig. 11(a). This observation proved that the FP-g-PSAS samples pre­
pared had high water-solubility. The reason for the high solubility is
that the PSAS branches introduced by the copolymerization have a
large number of sulfonates. The polar sulfonates have strong hydro­
philicity, thereby obviously improving the water-solubility of feather
protein without the addition of alkaline substance. As a result, hydro­
lysis of the protein macromolecule chains arisen from the addition of
alkaline substance will be obviously weakened, thereby alleviating the
reduction of cohesive strength. Additionally, steric hindrance of the
PSAS branches and absorbed water arisen from the hydrophilicity of the
8
European Polymer Journal 136 (2020) 109945
grafted branches, can provide the plasticization for protein adhesive
layers, which favors reducing the probability of the failures and ame­
liorating the adhesion. Besides, there are a lot of polar hydroxyls on the
viscose and cotton fibers, which have the chemical similarity with the
polar sulfonate groups in the PSAS branches. Based on “similar dissolve
mutually” theory, the existence of the polar sulfonate groups favors
increase in the van der Waals force at the interfaces between protein
adhesive layers and both fibers, and subsequently improving the ad­
hesion. As grafting ratio increases, the amount of polar sulfonate groups
introduced will also increase gradually, producing an increased force at
the interfaces and providing an increase in the adhesion.
In addition of these reasons that generate an gradually increased
adhesion as the grafting ratio raises, enhancement in the water-dis­
persibility of protein after the copolymerization may also be an im­
portant factor. The water-dispersibility can be evaluated by measuring
the light transmittance of FP-g-PSAS aqueous solution. We found that
the FP-g-PSAS samples with the ratios of 14.8–28.2% corresponded to
the transmittances of 29.4–40.1%, suggesting that the transmittances of
FP-g-PSAS aqueous solutions gradually increased with the rises in the
ratios. Generally, the lower the transmittance, the worse the water-
dispersibility [18]. It has been confirmed that the worse water-dis­
persibility easily induces incomplete wetting and outspreading [43],
leading to interfacial failure and exerting an adverse effect on adhesion.
Accordingly, as the ratios raise, a continuously increased water-dis­
persibility is displayed, which will reduce the probability of interfacial
failure and produce a gradually improved adhesion.
4. Conclusion
In this study, feather protein was extracted from feather wastes, and
its graft copolymerization with SAS monomer was performed for pre­
paring FP-g-PSAS samples with an APS/eSH groups (on the protein
chains) redox system in a 8 M urea aqueous solution. FTIR and EDS
techniques proved the successful introduction of PSAS branches in the
protein molecules. The thermal stability of FP-g-PSAS was lower than
raw feather protein extracted, but the difference in the stability was not
obvious in the temperature range of 25–600 °C. The introduction of the
PSAS branches made feather protein transform from crystalline (raw
feather protein) to amorphous state (FP-g-PSAS), as indicated by the
XRD analysis. FP-g-PSAS samples were superior to feather protein in the
adhesion strengths to both fibers at 60 °C, and when grafting ratios
were in the range of 22.1–28.2%, the strengths of FP-g-PSAS samples to
both fibers were significant differences with those of feather protein
(p < 0.05). Adhesion strengths of FP-g-PSAS samples were correlated
with grafting ratios, and the strengths gradually increased from 16.4 to
17.5 cN/tex for viscose fibers and 15.9–17.2 cN/tex for cotton fibers,
with raising the ratios from 14.8% to 28.2%. In addition, the strengths
of the sulfosuccinylated starch (DS = 0.0036) to viscose fibers and the
quaternized-sulfosuccinylated starch (DS = 0.0443) to cotton fibers
were determined at the temperature of 60 °C, and the results were 17.0
cN/tex and 16.8 cN/tex, respectively. As seen, the strengths of FP-g-
PSAS with a grafting ratio of 28.2% to both fibers were higher than
those of the two modified starches, indicating that the FP-g-PSAS could
W. Li, et al.
Fig. 11. Digital photographs (a) of the FP-g-PSAS solutions for evaluating the water-solubility. (A) grafting ratio = 14.8%, (B) 22.1%, (C) 28.2%, and viscosities (b)
of the solutions.
Fig. 12. Influence of graft copolymerization on the adhesion of feather protein
to viscose fibers at 60 °C.
be expected as a sizing agent in the application of viscose and cotton
warp sizing at low temperature. The finding of our work would provide
useful information for preparing the grafted polymer with high adhe­
sion strength by building an APS/eSH groups (in the protein molecules)
redox system, and providing a new protein-based grafted copolymer as
sizing agent for viscose and cotton warp sizing at low temperature.
CRediT authorship contribution statement
Wei Li: Conceptualization, Writing - original draft, Writing - review
& editing, Methodology, Resources, Funding acquisition. Zhengyu Yu:
Investigation. Youkang Wu: Validation. Qian Liu: Investigation.
9
European Polymer Journal 136 (2020) 109945
Fig. 13. Influence of graft copolymerization on the adhesion of feather protein
to cotton fibers at 60 °C.
Declaration of competing interest
The authors declare that they have no known competing financial
interests or personal relationships that could have appeared to influ­
ence the work reported in this paper.
Acknowledgments
This work was financially supported by the Natural Science
Foundation of Anhui Province (No. 1908085ME124), Key Research and
Development Program of Anhui Province (No. 201904a06020001),
Science and Technology Planning Project of Wuhu City (No. 2018pt04),
China.
W. Li, et al.
Data availability statement
The raw/processed data required to reproduce these findings cannot
be shared at this time as the data also forms part of an ongoing study.
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