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Antioxidant Activity of Keratin Hydrolysates Studied by DSC

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 20

Antioxidant Activity of Keratin Hydrolysates Studied by DSC

by
Ján Matyašovský,1 Ján Sedliačik,2* Peter Šimon,3 Igor Novák,4 Tomasz Krystofiak,5 Peter Jurkovič,1
Peter Duchovič,1 Mariana Sedliačiková,2 Zuzana Cibulková,3 Matej Mičušík4 and Angela Kleinová4
1
VIPO, a.s., Partizánske, Gen.,
Svobodu 1069/4, 958 01 Partizánske, Slovakia
2
Faculty of Wood Sciences and Technology, Technical University Zvolen,
Masaryka 24, 960 53 Zvolen, Slovakia
3
Faculty of Chemical and Food Technology, Slovak Technical University,
Radlinského 9, 812 37 Bratislava, Slovakia
4
Polymer Institute, Slovak Academy of Sciences,
Dúbravská cesta 9, SK-845 41 Bratislava, Slovakia
5
Faculty of Wood Technology, Poznań University of Life Sciences,
Wojska Polskiego 28, 60-637 Poznań, Poland

Abstract incinerators or wastewater and sludge. This waste, animal fat,

Due to the high content of thio-aminoacids, (i.e., methionine
and cysteine) and the structural intermolecular disulfide bonds,
this study has focused on new biopolymer keratin antioxidants.
The antioxidant activity of keratin hydrolysates in polyethylene
glycol (PEG) matrix has been studied using the differential
scanning calorimetry (DSC) under non-isothermal conditions.
The experimental results have been evaluated and kinetic
description of the oxidation induction periods have been carried
out using the Bethelot-Hood temperature function. The length
of induction periods has been assessed for all temperatures using
the kinetic results. In order to compare the stabilizing effect of
keratin hydrolysates, protection factors and antioxidant
effectiveness have been calculated. The results have shown that
the antioxidant activity of keratins strongly depends on the
hydrolysis process. The protection factors decreased with
increasing temperature and decreasing concentration of keratin.
Based on our previous experience, we propose that the qualitative
trend presented in this work can also be applied for other
matrices than PEG. Keratin hydrolysates and their modifications
with antioxidant properties significantly reduced formaldehyde
emissions from urea-formaldehyde adhesives.
Introduction
The last few years are characterized by the rapid development of
progressive technologies that focus on new applications of
biologically active natural substances with high added value.
Annually, large quantities of natural waste are produced that are
not adequately exploited and most often end up in landfills,
wool, hair, feathers, keratin hydrolysates, etc. that result from
meat and leather processing, contain a diverse mix of chemical
and biological substances. They can be inert, biodegradable and
dangerous. Thus, the great attention is mainly focused on the
possibilities of their further processing and use. In the recent
years, keratin research has increased and already led to the
development of many biomaterials for use in keratin biomedical
applications based on several key properties of keratin that
contribute to the overall physical, chemical and biological
behavior of these biomaterials.1,2
The use of new technologies has enabled researchers to develop
a wide range of tailored bio-materials and allowed considerable
progress in this area. Especially collagen, albumin, gelatin,
fibroin and keratin have been studied with regards to using of
natural materials for the biomaterials development. Among
these materials, keratin has been the most studied for
biomaterials development due to its natural biocompatibility,
biodegradability, mechanical stability, natural richness.
Moreover, common protein hydrolysis methods have been
ineffective for keratin.
The term “keratin” was originally related to a broad category of
insoluble proteins that are bounded with intermediate filaments
(IFs) and form the majority of cytoplasmic epithelium and
epidermal supplementary structures (hair, wool, horn, hooves
and nails). Further research of these structural proteins led to
the classification of mammalian keratin into two different
groups according to their structure and layout. “Hard” keratins
form regular IFs and they are inserted into the matrix of cysteine
rich proteins; thereby, they contribute to the rigid structure of

*Corresponding author e-mail: sedliacik@tuzvo.sk This Technical Paper, received and accepted June 22, 2018, was presented by the author at the
114th Annual Convention of the American Leather Chemists Association, June 19-22, 2018.

JALCA, VOL. 114, 2019

21 Antioxidant Activity of Keratin Hydrolysates
epidermal auxiliaries. “Soft” keratins preferentially form sparse
clusters of cytoplasmic IFs and add mechanical elasticity to the
epithelial cells.3-5
Although hard and soft keratins have a similar secondary
structure, the different amino acid sequence composition
contributes to their measurable differences. Mainly hair keratin
has a high content of cysteine residues in the non-helix domains
and therefore, forms more rigid and durable structures during
the formation of intermolecular disulfide bonds.4, 6-7 Hair fibers
are elongated keratinized structures, composed of strongly
cross-linked hard keratins. Oxygen-rich cysteine-based keratins
are physically cross-linked and give the hair strength and
flexibility.8
The biological properties of extracts have caused increased
interest in the use of keratins for medical applications. Keratin
powders for cosmetics, composites and drug coatings belong to
the first patents.9-11 The analyzes of oxidative and reductively
extracted keratins have been studied.12-13 Other studies have
focused on surface chemistry of wool, product processing, sheep
wool production, splicing, carbonization, surface treatment,
denaturation, chemica l modif ication, photochemica l
degradation and polymer application to wool. The most
commonly used technologies include hydrolysis by alkaline
solutions, acids, reduction and oxidization agents, and by
enzymes in recent years. The hydrolysates can be further
modified for applications in industry, cosmetics, medicine or
agriculture, etc.
Many diseases are the result of negative affect of free radicals in
living organisms that degrade important components
responsible for important functions. Therefore, research has
focused on the preparation and testing of new keratin
antioxidants. Free radicals are generally unstable, highly
reactive, short-lived, and capable of self-existence. Reactive
oxygen species or free radicals in the biological system can be
formed by pro-oxidative enzyme systems, lipid oxidation,
irradiation, inflammation in the body, smoking, air pollutants
and the glycoxidation process.14
Antioxidant is a substance capable of preventing oxidation of the
substrate by disposing the oxidant, the most common free
radical. Antioxidants prevent spontaneous oxidation of food,
polymers (plastics, rubber), motor oils, fuels, cosmetics; and
thus; they contribute to the preservation of their original
physical and chemical properties. Caesalpinia spinosa and
bucillamine were tested as potential antioxidants in a system
composed of Cu (II) and ascorbate, which induced degradation
of high molecular weight hyaluronan (HA). Changes in the
dynamic viscosity of HA solutions was measured by rotational
viscosity in relation to time and concentration.15-16
JALCA, VOL. 114, 2019
Other studies have focused on new keratin based antioxidants,
especially for the high content of thio-amino acids, e.g.
methionine and cysteine and the presence of the intermolecular
disulfide bonds. Keratin was tested as a relevant (endogenous)
substance with potential to scavenge reactive oxygen species
degrading HA by using rotational viscometry. The ABTS assay
was used to determine radical scavenging capacity of keratin
hydrolysates and their electron donor properties.2
The condensed phase processes often exhibit an induction
period (IP) with no chemical reaction. During IP, the technique
applied do not record any signal; however, the intermediates
necessary for the main stage progress are formed. Oxidation is
a  typical process exhibiting the induction period. It is an
exothermic process with the heat enabling to employ the
differential scanning calorimetry to detect the end of IP (or the
start of the main oxidation stage). IP is determined as a sudden
increase in the oxidation rate. At the end of IP, a sudden change
in material characteristics takes place (usually deterioration).
Thus, the length of induction period is often considered a relative
measure of material thermo-oxidative stability.17-18
In general, the accelerated oxidation tests are carried out in two
temperature regimes:
1. At the constant heating rate – in this case the oxidation onset
temperature (OOT) is determined,
2. At constant temperature – the oxidation induction time
(OIT) is measured.
The standard tests for IP determination are predominantly
carried out under isothermal conditions. During this process,
the peak is often flat and its onset, corresponding to the end of
induction period, cannot be determined unambiguously; hence,
the OIT values may carry great systematic errors.16 Studies of the
oxidation processes at various heating rates17-18 have shown that
the oxidation peak is distinct, and the onset temperature can be
measured accurately and unambiguously. A great advantage of
OIT is that it is much more illustrative than OOT. Hence, it
would be desirable to obtain the values of kinetic parameters
from the OOT values and then to apply the values of kinetic
parameters to calculate the OIT values. They represent the
length of induction period at a chosen temperature.
Antioxidant activity of keratin hydrolysates was studied in the
polyethylene glycol matrix employing DSC under non/
isothermal conditions. The hydrolysates were prepared from
sheep wool by acidic, alkaline and oxidation hydrolysis. They
were analyzed and parametrized by X-Ray photoelectron
spectroscopy (XPS) and ATR-FTIR spectroscopy measurements.
Biologically active natural matters are possible to use for new
applications in the technology of polycondensation adhesives
 Antioxidant Activity of Keratin Hydrolysates 22
e.g.19-24 The addition of hydrolysates Keratin K, K-3 and  K-T
(described in the materials section) into urea-formaldehyde
adhesives (UF) was tested with the aim of lowering formaldehyde
emission.
Experimental
The raw material for the preparation of the keratin hydrolysate
was sorted, washed, defatted and dried sheep wool Merino.2
Materials and Chemicals
Three hydrolyzed dry powders of keratin were prepared from
the purified sheep wool:
1. Keratin K – prepared by alkaline hydrolysis
2. Keratin K-3 – prepared by acid hydrolysis
3. Keratin K-T – prepared by peroxide hydrolysis
The hydrolysis was carried out at 100°C.
Keratin K was prepared by alkaline hydrolysis. 1000 mL distilled
water, 10 g NaOH and 10 ml 30% H2O2 were added into 100 g of
sheep wool. The hydrolysis proceeded at the boiling point
in  closed glass vessel for 5 hours. Prepared hydrolysate was
filtered, neutralized, purified by dialysis against distilled water,
dried and milled to powder.
Keratin K-3 was prepared by acid hydrolysis. 900 mL distilled
water and 100 mL of concentrated HCl were added into 100 g of
sheep wool. The hydrolysis proceeded at the boiling point
in  closed glass vessel for 5 hours. Prepared hydrolysate was
filtered, neutralized, purified by dialysis against distilled water,
dried and milled to powder.
Keratin K-T was prepared by peroxide hydrolysis. 900 mL
distilled water and 100 mL 30% H2O2 were added into 100 g of
sheep wool. The hydrolysis proceeded at the boiling point in
closed glass vessel for 2 hours. Keratin was then liquefied by
alkaline treatment of pH, filtered, coagulated, washed, drained
by pressure filtration, dried, and powdered in a ball mill.
The antioxidant effect of keratin hydrolysates was determined in the
suspension with polyethylene glycol SLOVAPEG-600 (Slovchema,
Slovakia). The mixtures of PEG and keratin were ultrasonicated for
5 min. Keratin swelled in polyethylene glycol (PEG) forming a
suspension. Composition of the suspensions is shown in Table I.
The quantity X in Table I is the number of parts of keratin per
100 parts of PEG. It is an analogue of the quantity Parts per
Hundred Rubber (PHR) used in rubber compounds.
Methods of Testing
X-Ray photoelectron spectroscopy (XPS) signals were recorded
using a Thermo Scientific K-Alpha XPS system (Thermo Fisher
Scientific, UK) equipped with a micro-focused, monochromatic
Al Ka X-ray source (1486.6 eV). An X-ray beam of 400 mm size
was used at 6 mA x 12 kV. The spectra were acquired in the
constant analyzer energy mode with pass energy of 200 eV for
the survey. Narrow regions were collected using the snapshot
acquisition mode (150 eV pass energy), enabling rapid collection
of data (5 s per region). The Thermo Scientific Avantage software,
version 5.988 (Thermo Fisher Scientific), was used for digital
acquisition and data processing. Spectral calibration was
determined by using the automated calibration routine and the
internal Au, Ag and Cu standards supplied with the K-Alpha
system.
ATR-FTIR Spectroscopy Measurements
FTIR–ATR (Fourier transform infrared attenuated total
reflectance spectroscopy) was used to investigate the surface
chemical composition. Also, the KBr pellet technique was used
to expand the examined spectral region bellow 650 cm-1,
circumvent the optical material used in ATR measurements
(germanium crystal) limit. This process should allow detection
of the sulfidic vibrations, which occurs in region between 700
cm-1 – 500 cm-1.
DSC Calorimeter Shimadzu DSC-60
Thermo-oxidation tests were carried out employing the DSC
calorimeter Shimadzu DSC-60. The temperature calibration was
performed to the fusion temperature of In and Sn, the enthalpy
calibration to the melting enthalpy of In. The samples were
placed in open standard aluminum pans, the sample mass was
4-5  mg. Exothermic peaks on the DSC records are oriented
upwards. The purge gas, forming the reaction atmosphere, was
oxygen with the flow rate of 50 ml/min. The measurements were
carried out at the heat rates β = 1; 3; 5; 7 and 10°C min–1.
Table I
Mass of components of the suspensions
of PEG with keratin.
Parameter PEG + K PEG + K-3 PEG + K-T
m(keratin) [g] 0.09356 0.10034 0.09896
m(PEG) [g] 4.272 4.272 4.272
X 2.190 2.349 2.316
JALCA, VOL. 114, 2019
23 Antioxidant Activity of Keratin Hydrolysates

Formaldehyde Emissions
Test method JIS A 1460 (2001). Building boards. Determination
of formaldehyde emission. Desiccator method.
The volume of desiccator: 9-11 dm3
Loading coefficient: 1800 cm2
Temperature: 20 ± 0.5°C
Test duration: 24 h
The ana ly tica l met hod: acet ylacetone met hod w it h
spectrophotometric evaluation.
Preparation of birch (Betula) veneer panels: Five layers plywood
were prepared to determine the formaldehyde emission under
the following conditions: pressure of 1.8 MPa, temperature of
105°C, pressing time 6 min. Samples were kept at the temperature
of 20 ± 2°C and relative humidity of 65 ± 5°C for 7 days.
Figure 1. XPS survey of K hydrolysate, K-3, and K-T.

Results and Discussion

The antioxidant activity of keratin hydrolysates in polyethylene

glycol (PEG) matrix was studied using the differential scanning
calorimetry (DSC) under non-isothermal conditions.

Testing of Keratin Parameters

X-Ray photoelectron spectroscopy (XPS) was used for
qualitative and quantitative determination of basic elements:
overall carbon (C1s signal at ~ 285 eV), oxygen (O1s signal at ~
532 eV), nitrogen (N1s signal at ~ 400 eV), natrium (Na1s signal
at ~ 1072 eV), chlorine (Cl2p signal at ~ 198 eV), and sulfur as
C–S (S2p signal at ~ 163 eV) and SO3 (S2p signal at ~ 168 eV),
(Table II, Figures 1 and 2).

Figure 2. XPS S2p region of K hydrolysate, K-3, and K-T.

Table II
Apparent surface chemical composition of K, K-3, K-T as determined by XPS.

Sample Surface chemical composition [at%]

S2p
C1s O1s N1s Cl2p Na1s
sulfide(C-S)/SO3
1.9
K 57.2 21.4 12.0 0.9 6.6
44.4/55.6
3.0
K-3 65.8 15.8 13.5 1.3 0.6
89.2/10.8
0.2
K-T 89.5 7.4 2.5
23.9/76.1

JALCA, VOL. 114, 2019

 Antioxidant Activity of Keratin Hydrolysates 24

Changes in the spectra of keratin hydrolysates are mainly shown

in the content of sulfur, in proportion between the reduced C-S
form (S2p signal at ~163 eV) and SO3 (S2p signal at ~ 168 eV)
oxidized form.

In the Keratin K-T sample prepared by oxidative hydrolysis, a

significant decrease of oxygen (O1s signal at ~ 532 eV), nitrogen
(N1s signal at ~ 400 eV), sulfur (to 0.2%) and its reduced form
(S2p signal at ~163 eV) was observed. At the same time, a
significant increase of overall carbon (C1s signal at ~ 285 eV)
was found. Keratin K-3 has the highest sulfur content that leads
Figure 3. FT-IR spectra analysis of Keratin K hydrolysate.
to reduction of the sulfide bonds.

Infrared FTIR–ATR Spectroscopy

The spectra of three keratins K, K-3 and K-T are shown in
Figures 3, 4 and 5. The main peaks typical for the protein-type
materials are observed in all three materials. In the spectra of
keratin hydrolysate samples, a broad band between 3600 cm-1-
2200 cm-1 appears with various maxima. These maxima can be
assigned to the valency vibrations of the –OH, –NH and –CH
functional groups. In the area of deformation vibrations, the
bands were observed that are characteristic for the amide
structure (the band with the maximum at 1660 cm-1 can be
Figure 4. FT-IR spectra analysis of keratin K-3 hydrolysate.

Table III
Dependence of the oxidation onset temperature (OOT) on the heating rate (β).
OOT (°C)
β (°C/min)
PEG pure PEG + K PEG + K-3 PEG + K-T

1 121.82 127.39 158.12 129.46

3 131.88 138.81 169.21 144.78

5 138.73 143.18 172.17 151.20

7 144.51 145.12 177.62 153.55

10 150.95 152.01 181.84 157.42

Table IV
Kinetic parameters describing the induction period of the samples.
ln (A/min) ± SD D (K–1) ± SD

PEG pure 34.2 ± 3.0 0.0804 ± 0.0076

PEG + K 42.0 ± 3.1 0.0991 ± 0.0077

PEG + K-3 45.2 ± 2.9 0.0995 ± 0.0067

PEG + K-T 35.6 ± 1.9 0.0820 ± 0.0047

JALCA, VOL. 114, 2019

25 Antioxidant Activity of Keratin Hydrolysates

attributed to the (C=O)stretch vibration - Amide I). The bands
attributed to Amide II (1500-1400 cm-1, NH bending and CH
stretching) are also present in the spectra, as well as the band at
the maximum of 1224 cm-1 - Amide III (combination of (CN)
stretch
and (NH in plane)bend along with the contribution of (C–C)
stretch
and (C=O)bend vibrations). Apart from the amide bands, the
band at 1722 cm-1, originated from the hydrolysis of the carbonyl
(C=O) group from –COOH group, also appears in the spectra of
samples of hydrolyzed keratin. The main differences between
the IR spectra of keratin samples were found in the area of
valency vibrations associated with the sulfur compounds.
In the Keratin K-3 sample, a band at 2600 cm-1 (a shoulder) as
part of a broad band between 3800-2200 cm-1 in the valency
vibration region is present. This band is most likely associated
with S–H binding. The band with a maximum at 2600 cm-1 is
related to (SH)stretch vibration originated from cysteine.
In all keratin hydrolysate samples (Keratin K, K-3, and KT) a
band of varying intensity, which is characteristic for sulfur
oxides - (SO2)stretch resulting from hydrolysis of keratin, can be
observed at 1040 cm-1.
In the spectra of Keratin K and K-3 samples, a band that can be
assigned to the alkyl- and di-alkyl sulfide vibrations (C-S)stretch,
appeared in the spectral range of 500-700 cm-1.
The stabilizing effect of antioxidants depends on the matrix
where they are dispersed. The keratin samples are aimed as the
stabilizers of aqueous gels of hyaluronic acid. Since the peak of
water evaporation would overlap the oxidation peak of
hyaluronic acid, we applied the water-free PEG matrix.
The values of OOT as a function of heating rate are summarized
in Table III. An example of the DSC record of PEG with keratin
K-3 for the heating rate 1 K/min is illustrated in Figure 6.
Previous studies 25-27 show that the Arrhenius temperature
function overestimates the evaluation of the lengths of induction
period for the edible oil oxidation. Two other non-arrhenian
temperature functions provide thermos-oxidation stabilities. In

Figure 5. FT-IR spectra analysis of keratin KT hydrolysate. Figure 6. DSC record of PEG with keratin K-3 for the heating rate 1 K/min.

Table V
Test results – formaldehyde emission by the desiccator method.
Sample Emission [mg/l] Decrease emissions [%]

0 – UF resin + 20% filler + 5% hardener – standard 0.362 100.0

2 – UF resin + 20% filler + 5% hardener + 2% K 0.318 12.2

3 – UF resin + 20% filler + 5% hardener + 5% K 0.293 19.1

5 – UF resin + 20% filler + 5% hardener + 2% K- 3 0.258 28.7

6 – UF resin + 20% filler + 5% hardener + 5% K- 3 0.223 38.4

8 – UF resin + 20% filler + 5% hardener + 2% K-T 0.326 10.0

9 – UF resin + 20% filler + 5% hardener + 5% K-T 0.297 18.0

JALCA, VOL. 114, 2019

 Antioxidant Activity of Keratin Hydrolysates 26
our study, the Berthelot-Hood temperature function was applied
which provides the most reasonable estimates of the stability for
edible oils.25 For this function, the dependence of OOT (OOT is
marked as Ti) can be expressed by the relationship
1 ti (PEG pure)
Ti = ln(ADβ +1) (1)
D
The kinetic parameters A and D in Eq. (1) have been obtained
from the data of Table III by the non-linear least squares method
using the program ORIGIN. Their values with standard
deviations (SD) are listed in Table IV.
As shown in Figure 7, agreement between the experimental and
calculated values of OOT is very good, demonstrating that the
theory correctly describes the experimental findings. Figure 7.
Agreement between the experimental and calculated values of
OOT for individual samples.
The A and D kinetic parameters enable to assess the length of IP
for any temperature regime. For a constant temperature, the
length of induction period (i.e., OIT marked here as ti) can be
calculated as 25, 28
ti = Aexp ⎡⎣−DT ⎤⎦ (2)
The values of OIT have been calculated for the temperature (25–
125) °C. They are shown in Figure 8.
From Figure 8 can be seen that OIT decreases exponentially with
increasing temperature. The highest estimations of OIT exhibits
PEG stabilized with keratin K-3. For 25°C, the OIT value is about
90000 hours, i.e. about 10 years. Stabilizing effect of the other
keratin samples is much lower. The stabilizing effect of the
Figure 7. Agreement between the experimental and calculated values of
OOT for individual samples.
antioxidant is more seen from the value of the protection factor
(PF), which is defined28 as the ratio of OITs for the stabilized and
unstabilized samples:
PF =
(
ti PEG+keratin ) (3)
The values of PF for individual samples are shown in Figure 9.
From Figure 9 it can be seen that the values of protection factors
to PEG matrix also depend on temperature; however, much less
steeply as the values of OIT. A substance exhibits a protective
effect, i.e. it behaves as an antioxidant, if the value PF > 1. This
condition is fulfilled for all keratin samples.
The protective effect of an antioxidant depends on its
concentration in the matrix. Previous studies 28-29 have
introduced the antioxidant efficiency as the increment of
protection factor per one part of the antioxidant in matrix:
PF −1
AEX = (4)
X
The antioxidant efficiency does not depend on its concentration
in the matrix and represents the quantity suitable for the
comparison of individual antioxidants. The antioxidant
efficiency of individual keratin samples as a  function of
temperature is depicted in Figure 10.
From Figure 10 it is clear that the antioxidant efficiency of
keratin hydrolysates K and K-T is small. A substantially better
result has been reached for the sample K-3, where the AEX value
is from 13 for 125°C up to 87 for the temperature 25°C.
Figure 8. Estimation of OIT values for PEG pure and stabilized with
keratin hydrolysates calculated by Eq. (2).
JALCA, VOL. 114, 2019
27 Antioxidant Activity of Keratin Hydrolysates
Reduction of Formaldehyde Emission
Formaldehyde emissions were tested from five-layer plywood
according to the test method JIS A 1460. Keratin hydrolysates K,
K-3 and K-T were tested to determine their influence on release
of formaldehyde from wood based panel – plywood bonded with
UF resins (Table V, Figure 11).
Figure 9. Values of protection factor for individual samples of
keratin hydrolysates.
Figure 10. Antioxidant efficiency of keratin hydrolysates in the
PEG matrix.
Figure 11. Decrease of formaldehyde emission from  UF bonded
plywood with the application of keratin hydrolysates.
JALCA, VOL. 114, 2019
Measured values of extinctions of tested samples confirmed the
lowering of formaldehyde emissions for each concentration of
keratin hydrolysate in comparison with the reference sample.
The most significant decrease of formaldehyde up to 38.4% was
obtained for 5% dosage of keratin K-3. Samples of keratin K and
Keratin K-T lowered formaldehyde emission about  19% in
comparison with the reference sample. Tested keratins might
have a great potential for application as environmentally friendly
formaldehyde scavengers.30
Conclusions
This investigation has focused on modifications of natural
polymer keratin and its hydrolytic treatment directed mainly to
cleavage of the disulfide bond to the S–H thiol groups (the O–
SO3 bond, respectively). Moreover, this work has studied the
inf luence of these changes on antioxidant properties and
formaldehyde emissions reduction.
It was confirmed that the technologic process of keratin
hydrolysates preparation inf luences their composition
and parameters. According to the AEX value, the sample K-3 can
be characterized as only slightly efficient antioxidant for higher
temperatures and moderately efficient on for low temperatures.
Efficiency of the samples K and K-T is negligible. This conclusion
is strictly valid for the PEG matrix and for the experimental
conditions applied, i.e. for the oxygen atmosphere and thin layer
of PEG sample. The assessment of AEX for the ambient
temperature represents an extrapolation very far from the
temperature interval of the measurement. Thus, the results may
convey a great uncertainty. In spite of this finding, based on our
experience we suggest that the qualitative trend reported in this
paper will also be followed for other matrices and for the air
atmosphere.
The new application of Keratin K-3 into UF adhesives resulted in
the highest decrease in formaldehyde emissions compared to the
reference UF bonded sample. This allowed the glued wood
products to be transferred to a qualitatively higher emission
class.
Acknowledgement
Financial support from the Slovak Research and Development
Agency under the contracts No. APVV-14-0506, APVV-15-0124
and APVV-16-0177 is greatly acknowledged. Processed within
the COST CA15216 action.
 Antioxidant Activity of Keratin Hydrolysates 28
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JALCA, VOL. 114, 2019