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Krystyna Wrzeniewska-Tosik,

*Janusz Adamiec
Biocomposites with a Content of Keratin
from Chicken Feathers
Institute of Biopolymers and Chemical Fibres,
Member of EPNOE, Abstract
European Polysaccharide Network of Excellence, The markets demand for fibrous materials with increased moisture retention is principally
connected with the essential development of sanitary and cosmetic products. Keratin,
ul. M. Skodowskiej-Curie 19/27, 90-570 d, Poland which is included in feathers, appears to be an original raw material which enables fibrous
composite materials of this kind to be manufactured. The aim of our investigation was to
*Department of Thermal and Diffusive Processes, obtain different keratin forms from feathers, to identify and determine these forms, and to
Faculty of Process Engineering indicate new application directions connected with fibres and fibrous products. An optimum
and Environmental Protection, extraction method for obtaining keratin from chicken feathers was developed, and an
Technical University of d attempt was made to obtain stable keratin solutions with the addition of other biopolymers,
ul. Wlczaska 223, 90-924 d, Poland such as cellulose and alginate.

Key words: keratin, feathers, fibrous biocomposites, sorption, keratin solutions, cellulose,

chicken feathers are undoubtedly novel extracting keratin from chicken feathers
directions of use. and attempts to obtain keratin solutions
with a content of other biopolymers, such
Keratin is insoluble in water, weak acids as cellulose or alginates, were included in
and bases, as well as in organic solvents. the scope of our research work.
The amino-acid content of keratin is
characterised by a high cystine content
n (and at the same time sulphur), which Materials and methods
may change within 2% wt and 18% wt, Materials
Recently, researchers and manufacturers
a significant amount of hydroxyamino-
have been searching for new directions Raw material
acids, especially serine (about 15% wt),
for applying polymers which up to the The raw material for obtaining keratin
and a lack of hydroxyproline and hy-
present have not been well known. Kera- came from chicken feathers which were
droxylisine, among other substances
tin from chicken feathers is a by-product characterised by the following contents:
[10,11]. The chemical activity of keratin
which is available in great amounts, and n a sulphur content of 2.9%,
is connected in a significant degree to the
which is only used in a small degree. The n a nitrogen content of 15.5%, and
cystine content. The disulphide bonds
amount of this waste is continuously in- n an ash content of about 1%.
creasing, in connection with the increase which is formed between two cysteine
in fowl meat production. molecules is responsible for the high
strength of keratin and its resistance The chemical agents used for obtaining
against the action of proteolitic enzymes. the keratin were of analytical purity.
The keratin included in chicken feathers
is a very inconvenient and troublesome On the other hand, keratin is very reac-
tive, as cystine can easily be reduced, ox- Methods
waste product of the poultry-farming in-
idised, and hydrolysed [12-15]. In order Preliminary processing of the chicken
dustry, and therefore it is presently the
to precisely determine the possible future feathers
object of intensive investigations in many
applications of keratin, it is necessary to Before dissolution, the feathers were
research centres. Many publications and
patents proposing applications for this learn in detail the structure and the poten- washed many times with hot water
biopolymer have been issued as a result tial possibilities of this valuable protein. with detergent addition, dried, filtered,
of these research works. Applications of and again washed with ethylene alcohol
(Trademark: ETOH Antibacterial 96%),
keratin preparations in the cosmetic in- The aim and scope and dried. After drying, the feathers were
dustry are the best known and described of the investigation
in literature. However, opportunities to cut into short segments or milled.
use this interesting protein in other fields The above-mentioned reasons formed the
have arisen, for example as component of outlines defining the aims of the research Solubilisation of keratin
various kinds of composites [1-5], as a work which we undertook. We provided in alkali medium
component of biodegradable nonwovens and carried out tests estimating sorption The cleaned, dried, and cut feathers
[6-8], and in biotechnology [9]. properties and evaluating the particles were dissolved in an aqueous solution
dimensions, as well as preliminary in- of 5% wt NaOH and 0.1M solution of
Considering the hydrophilic properties of vestigations into preparing spinning Na2S. The process was conducted under
keratin, it would be appropriate to use it solutions of keratin with alginates and dynamic conditions, at a temperature of
for manufacturing fibres with increased biomodified cellulose. The aim of our re- 40C over 2 hours. After the process was
sorption features, which would in turn search work was to obtain various forms finalised, the keratin solution was filtered
be useful for producing textile products of keratin from feathers, to identify and in order to separate the insoluble parts of
dedicated to sanitary & medical applica- determine these forms, and to define new feathers, and next submitted to dialysis.
tions, and as a technical sorption mate- directions for applications. In particular, The dialysis was conducted with the
rial. Such applications of keratin from the elaboration of an optimum method for use of a 7649 mm cellulose dialysis

106 FIBRES & TEXTILES in Eastern Europe January / March 2007, Vol. 15, No. 1 (60)
sleeve, made by Sigma-Aldrich. The the keratin samples were placed into an reagent (DTNB), i.e. 5,5-dithiobis
dialysis was performed at environmental exsiccator with a relative humidity of (2-nitro-benzoic acid). Cysteine was
temperature over 48 hours. 93C (KNO3) and for the second time used as the standard substance. The
the sample mass changes were estimated calibration curve was elaborated for four
Extraction of keratin as a function of time. After stabilisation standards with concentrations from 3.3 to
After the dialysis, 2N hydrochloric acid of the sample mass, the samples were 13.2 mmol/l. The measurements were
was added to the keratin solution in order repeatedly placed into the exsiccator of carried out at a wavelength of 485 nm in
to precipitate the keratin at pH 4.2. The 65% RH in order to estimate the moisture a cell of 1 cm thickness, using the Ellman
precipitated keratin was centrifuged, desorption of the samples tested. reagent as a carrier.
washed several times with distilled water
in order to obtain neutral pH, and dried Chromatographic investigations Determining method
by lyophilisation. In order to obtain a mi- Chromatographic system The cell was filled with 0.1 cm3 of the
cro-spherical keratin form, after dialysis For the gel permeation chromatogra- tested keratin solution and 2.4 cm3 of
the solution was directly transmitted to phy (GPC) analysis, we used a module the Ellman reagent. Absorption measure-
spatter-drying. Drying was carried out HP1050 liquid chromatograph from ments were carried out after 10 minutes,
over some seconds at different tempera- Hewlett Packard equipped with the fol- using the Ellman reagent as the blank
tures selected within the ranges of 140C lowing devices: test; the content of the sulfhydril groups
to 160C at the inlet, and within 85C to n a Viscotek DG 700 four-channel was measured in mmol/l.
90C at the outlet. vacuum degasifier,
n a HP 1050 isocratic pump from Determining the sulphur
Lyophilisation of keratin Hewlett Packard, and nitrogen content
The lyophilisation was carried out over n a HP 1047 refractometric detector The nitrogen content was determined by
25 hours with the use of an Alpha 1-4 from Hewlett Packard, and the Kjejdahl method, whereas the sulphur
type lyophilisator from Christ Co., at an n a system of appropriate columns. content was assessed by the Sheniger
initial plate temperature of -20C and a The PL CaliberTM GPC/SEC software standard method [19, 20].
final temperature of 10C, whereas the program from Polymer Laboratories Ltd
preparation temperature was within the was used. Estimating the keratin particle sizes
range of 2C to 6C.
The keratin particle sizes were estimated
Preparing keratin solutions
with scanning electron microscopy
Chemical modification of keratin A keratin sample of 5 mg was placed
(SEM). Sample photos were taken by
Monochloroacetic acid was used for ker- in a graduated flask of 10 cm3 volume,
a Quanta 200 scanning electron micro-
atin modification [4]. Various amounts of 7 cm3 of the solvent (0.05 mol/dcm3
scope made by FEI, at magnifications of
monochloroacetic acid (1, 2, or 4g de- Tris + 0.02% NaN3 + HCl) was added,
2000 and 5000. The sample tested was
pending on the variant performed) were and then set for 16 hours for dissolution.
spread on the table and glued with carbon
added to alkali solutions of keratin at Next, the keratin solution was mixed by
glue. The keratin preparation structure
environmental temperature over 1hour. shaking for about 30 minutes, and added
was tested under high vacuum in natural
The keratin modified was precipitated the solvent to the volume of 10 cm-3.
state, without sputtering a gold layer on
with 2 N HCl from these solutions. Af- After mixing and filtration (0.45 m,
the sample. We estimated the size of the
ter centrifugation and being carefully Milex), clear keratin solution were ob-
particles which the keratin preparations
washed, the keratin sediment was sub- tained, suitable for the GPC analysis.
obtained were composed of.
jected to lyophilisation.
Chromatographic parameters of keratin
Microscope analysis of the solutions
Assessing the water retention value analysis
The solutions containing keratin, as well as
(WRV) n Columns: 1 TSKgel PWXL guard
the cellulose and alginate solutions, were
The water retention value was assessed in (7.8mm 4 cm from TosoHaas,
evaluated with the use of a Biolar-type
accordance with the standard method [16]. 2 TSKgel GM PWXL guard
(7.8 mm 4 cm from TosoHaas, polarisation microscope made by ZPO,
Assessing the sorption coefficient n Eluent: 0.05 mol/dcm3 Tris-HCL Warsaw. The images were recorded with
The sorption coefficient was in accord- (pH 8.5) + 0.02% NaN3, a computer analyser made by IMAL Co.
ance with the standard method [17]. n Column temperature: 30C,
n Flow speed of eluent: 0.5 cm3/min, n Estimating keratin properties:
Testing the moisture absorption n Volume of sample: 100 l,
results and discussion
The moisture absorption was determined n Calibration: set of standard proteins
on keratin samples dried to a constant within the range of molecular weights It is generally known that the keratin
mass preliminary with the use of an from 17 kDa to 158 kDa and polydis- included in feathers is resistant to the ac-
exsiccator at a relative humidity of 65% persion of Mw/Mn < 1.2 (BioRad). tion of polar solvents thanks to the high
(NH4NO3) and at an environmental content of disulphide bonds and the great
temperature of 20-21C. The moisture Determining the content of sulfhydril amount of hydrophobic amino-acids.
sorption was monitored by assessing the groups in keratin Therefore, keratin is a very difficult sub-
sample mass as a function of time. After The method applied uses the spectro- ject for analytical research.
stabilising the sample mass at a constant photometric technique for visible radia-
level, which means at full saturation by tion[18]. The basis of this measurement As the result of the process of extracting
moisture under the given conditions, is the colour reaction with the Ellman keratin from chicken feathers with the

FIBRES & TEXTILES in Eastern Europe January / March 2007, Vol. 15, No. 1 (60) 107
use of NaOH and Na2S, solutions are Table 1. The keratin forms differentiated by processing; Remarks: * - modification by 1, 2,
obtained from which keratin is isolated or 4 g of monochloroacetic acid per 1000 ml keratin solution; ** - additional processing:
- solution after dialysis subjected to ultrasounds; - processing in greatlaboratory scale;
by dialysis. Keratin may be precipitated A D: all dried by lyophilisation; R all spatter-dried, differentiated by keratin concentration
by hydrochloric acid at pH4.5 and in the solution and by initial & final drying temperature, all presented in Table 2.
subjected to lyophilisation, or the keratin
solution after the dialysis can be directed Keratin form Disintegrating Dissolution Drying Additional
Modified *
designation by: by: processing **
to spatter-drying. In addition, keratin A Cut Na2S Lyoph. - -
may be modified by monochloracetic B Milled Na2S Lyoph. - -
acid. We applied all these methods, and B/m1 Milled Na2S Lyoph. 1 g/ 1000 ml -
the keratin forms obtained are marked as B/m2 Milled Na2S Lyoph. 2 g/ 1000 ml -
shown in Tables 1 and 2. B/m4 Milled Na2S Lyoph. 4 g/ 1000 ml -
C Milled NaOH Lyoph. - -
Basic properties of the keratin D Cut NaOH Lyoph. - -
preparations KI Cut Na2S Spatter - -
The properties of non-modified and K II Cut Na2S Spatter - -
modified keratin are presented in Table3. K III Cut Na2S Spatter - -

The keratins obtained have the form of K IV Cut Na2S Spatter - -

KV Cut Na2S Spatter -
white or beige powder depending on the
K VI Cut Na2S Spatter -
extracting agent (NaOH or Na2S). They
K VIII Cut Na2S Spatter -
are characterised by nitrogen content
from 9.5 to 15.2%, and sulphur content
from 1.70 to 2.37%. The dissolution Table 2. Spatter-drying conditions of keratin preparations.
process efficiency (the percentage value
Keratin form Keratin concentration Drying temperature
of extracted keratin per 100 g of feathers) designation in solution, % wt. Initial, C Final, C
was within the range of 30 40%.
KI 1.0 85 147
K II 0.75 83 153
Cystine, cysteine and small amounts of K III 0.5 83 153
metionine are sulphuric amino-acids which K IV 0.5 85 128
are composed of proteins. Therefore the KV 1.0 78 153
K VI 0.5 78 153
amount of sulphur in keratin is mainly
K VIII 1.0 85 147
decided by the sulphur of the disulphide
cystine bonds (-SS-) as well as that origi-
nating in the free sulfhydryl groups (-SH-) Table 3. Basic properties of keratin preparations. Remark: efficiency - percentage value of
of cysteine. The keratin can be extracted extracted keratin per 100 g feathers.
from the feathers by breaking the disul- Keratin form Colour Nitrogen Sulphur Humidity, Efficiency*,
phide bonds in cystine, which results in designation content, % content, % % %
the creation of sulfhydryl groups (-SH-) A white 15.20 2.30 5.9 40
of cysteine. One investigation [18] has in- B white 14.80 2.10 6.0 38
C beige 9.53 2.10 6.1 40
dicated that if all disulphide bonds break,
D beige 11.40 1.71 5.8 41
the amount of cysteine equals 720 mol/g K I white 15.23 2.30 4.2 30
of feathers. After extracting the feathers, K VIII white 15.09 2.07 5.9 37
we obtained a keratin solution with a sulf- K IV white 14.46 2.10 6.0 35
hydril group content of 360 mol/g, which B/m1 white 14.79 2.37 5.9 35
B/m2 white 14.90 2.17 6.9 30
indicates that about 50% of the disulphide
B/m4 white 14.07 2.07 6.2 32
bonds were broken, and at the same time
the native keratin was significantly struc-
turally modified. To protect the cysteine Table 4. Content of sulfhydril groups (SH) in keratin solutions; *) Amount of monochloroacetic
acid in g/1,000 cm3 of keratin solution.
remains before the secondary creation
of intra- and intermolecular disulphide Type of solution Amount of monochloroacetic Amount of SH groups,
acid*, g mol/g
bonds between the molecules of the dis-
keratin solution after filtration 0.0 360
solved keratin, monochloroacetic acid was
solution of Bm/1 1.0 358
added to the solution of this protein. The Solution of Bm/2 2.0 335
keratin solutions were diluted 10 times Solution of Bm/4 4.0 305
before the measurements were made.
The amounts of sulfhydril groups in the
On the basis of the results obtained, we Sorption properties
keratin solutions are measured in mmol/l.
Dividing this result by the amount of could state that adding monochloroacetic Considering the possibilities of apply-
feathers dissolved in 1 l of the solution, acid in an amount of 4 g/1000 cm3 causes ing keratin as an addition to products
we obtain the result in mol of cysteine a modification of the sulfhydril groups for increased moisture absorption, we
per g of feathers. These results are pre- (SH) of the cystein remains at the level carried out tests in order to estimation the
sented in Table 4. of 15% in relation to unmodified keratin. usability of keratin for such applications.

108 FIBRES & TEXTILES in Eastern Europe January / March 2007, Vol. 15, No. 1 (60)
Table5 presents the sorption properties Table 5. WRV and sorption coefficient of unmodified and modified keratins.
(water retention value WRV, and sorp-
tion coefficient) of unmodified and modi- Type of solution WRV, % Sorption coefficient, %

fied keratins. A 105.4 130.5

D 65.1 87.5
On the basis of the results obtained, it is K I 153.4 186.2
clearly apparent that modification of the K VIII 155.5 188.5
keratin structures and the type of drying B/m1 131.4 155.7

employed influence the sorption features B/m2 138.5 160.0

of this protein. The highest sorption pa- B/m4 140.2 160.5

rameters were obtained for spatter-dried

keratins, and slightly lower for modified
keratins. In the case of modified and
lyophilised keratins, the water reten-
tion value and the sorption coefficient
reached higher values in comparison
to those keratin samples which were
lyophilised but not modified.

Another method of estimating the sorp-

tion properties is to test the moisture
absorption of the samples prepared. The
sorption and de-sorption process was
tested for selected keratin samples, and
the dependencies of the moisture content
as a function of time are presented in
Figure 1.

The sorption process under the condition

of 65% RH is not intensive, and a greater
jump does not appear until the samples
are placed in the exsiccator of 93% RH.
The highest absorbing capacity of about
45% was observed for spatter-dried kera-
tin, whereas the keratin preparations dried
by lyophilisation are characterised by a
significantly smaller absorbing capacity Figure 1. Sorption and de-sorption of selected keratin preparations.
at the level of about 20%, not essentially
more than the keratin which was sput- less often. The main reason for this is the All the tested samples were differenti-
ter-dried under conditions of 65% RH. difficulty in choosing an appropriate sol- ated by the kind of preparing keratin.
Lyophilised keratin after the de-sorption vent which would fulfil the demands for The data presented in Table 6 and Fig-
process bonds about 15% of moisture, eluents in the HPSEC/HPGFC method. ure2 indicate essential differences in
whereas the spatter-dried only bonds their molecular characteristics, which
about 20%. These keratin properties, Investigation was carried out in order to means that the method of obtaining the
especially those of spatter-dried keratin, select a composition of the keratin sol- keratin preparations significantly influ-
indicate the possibilities of its application vent which would be useful for HPSEC/ ences their molecular weight distribution.
as an addition to increase the hygroscopic HPGFC analysis. Finally the following Keratin obtained with the use of so-
properties of different kinds of products, composition content was elaborated: dium sulphide and spatter-dried (K IV and
such as hygienic products. 0.5 mol/dcm3 Tris-HCl (pH 8.5) + 0.02% K VIII) is degraded to a higher degree, but
NaN3. is more uniform in its molecular structure
Molecular weight tests of keratin by than all the other keratin samples. The
the GPC method Some of the solutions obtained were polydispersion degree is at the level of 2.2
Keratin is a very difficult object to test, characterised by a minimal opalisation, to 2.6. The keratin modified by monochlo-
considering chromatographic analysis, as which means that a part of the sample roacetic acid (B/m4) has a relatively high
it is insoluble in typical solvents. Elec- (below 5%) is in a state of suspension molecular weight, but is molecularly non-
trophoresis in a Polyacryloamide Gel and not a solution. Tests were carried out uniform (Mw/Mn = 5.6). From the data
(PAGE) is a standard method for deter- on five keratin samples. Table 6 listed the presented, it is clear that the drying temper-
mining the molecular weight of proteins. numerical results of the molecular char- ature has the greatest influence on keratin
The method of High Performance Size acteristics of selected keratin samples, degradation. Keratin preparations dried at
Exclusion Chromatography / High Per- whereas in Figure 2 the differential mo- temperatures from 85C to 147C (K VIII)
formance Gel Filtration Chromatography lecular weight distribution dependencies are characterised by the lowest molecular
(HPSEC/HPGFC) is used significantly of these samples are presented. weight.

FIBRES & TEXTILES in Eastern Europe January / March 2007, Vol. 15, No. 1 (60) 109
a) b) c)

Figure 2. Differential molecular weight distributions of selected keratin samples; a) comparison of unmodified and modified keratin (B
and Bm4); b) comparison of keratin dissolved in Na2S and NaOH (A and D); c) comparison of lyophilised and spatter-dried keratin (A
and K VIII).

Microscopic observations of keratin keratin (Figure 4.d) show the best-devel- these differences, the keratin prepara-
The particle sizes of the keratin prepara- oped surface and smaller particles . These tions in Figure 3.b to 3.d are presented at
tions obtained, for samples dried under keratin forms are also characterised by higher magnitude that those in Figure 4.
different conditions according to Table2, the best sorption properties. A decidedly
were measured with the use of a scan- more packed structure of the preparation Keratin solutions with biomodified
ning electron microscope. The results are is visible in the case of keratin which is cellulose and sodium alginate
listed in Table 7. non-modified and dried by lyophilisation
Considering the hydrophilic properties
(Figure 3.d). For better visualisation of
of keratin extracted from feathers, we
On the basis of the results obtained,
we stated that in all cases, irrespective Table 7. Particle sizes of spatter-dried keratin preparations.
of the drying conditions, the keratin
preparations obtained are characterised Keratin Number of Minimum Maximum Average value, Standard
form measurements diameter, m diameter, m m deviation, m
by particle sizes below 20 m. The
KI 13 3.83 16.08 9.2 4.23
K II 16 2.88 13.,29 6.6 3.19
Table 6. Numerical parameters of the K III 24 3.26 19.45 6.4 4.64
molecular characteristic of keratin. K IV 33 1.68 15.33 6.2 3.32
KV 22 3.56 12.28 6.9 2.31
Keratin Mn, Mw, Mw/Mn, K VI 13 4.82 13.12 8.4 2.31
form kDa kDa (-)
K VIII 17 4.78 13.04 8.3 3.18
K IV 12.5 27.3 2.2
K VIII 12.4 32.2 2.6
34.8 137.0 3.9
D a) b)
A 22.2 144.4 6.5
B 19.6 86.2 4.4
B/m4 22.4 130.3 5.8

average diameter values are within the

range of 6.2 to 9.2 m, at a maximum
standard deviation of 4.64. The shape
of the microspheres would significantly
facilitate the introduction of keratin into
the solutions of other polymers in order
to manufacture biocomposites.
c) d)
The estimation of the appearance of kera-
tin preparations obtained from chicken
feathers was also carried out with the use
of SEM. The photos of keratin prepara-
tions and of a chicken feather are pre-
sented in Figures 3 and 4.

The SEM photos show a wet keratin

preparation, the so-called never dry
form, spatter-dried and dried by lyophili-
sation, and modified by monochloro-
acetic acid. Essential differences in the
Figure 3. SEM photos of a) chicken feather, b) wet keratin preparation, called never dry,
particle structure are clearly visible. The c) keratin preparation modified after lyophilisation, d) keratin preparation non-modified
modified (Figure 3.c) and spatter-dried after lyophilisation.

110 FIBRES & TEXTILES in Eastern Europe January / March 2007, Vol. 15, No. 1 (60)
Clear, aqueous solutions of sodium algi-
a) b)
nate and alkali solutions of biomodified
cellulose [21] with properties typical of
spinning solutions used for fibre spinning
were prepared. Alkali keratin solutions
with different concentration within the
range from 5% to 20% were also pre-
pared. The keratin solutions were mixed
in different ratios with the polysaccharide
spinning solutions. This stage of research
was limited to microscopic observations
of the solutions (Figures 5 and 6) and the
preliminary estimation of their abilities
to obtain fibrous forms from the two-
c) d)
component solutions.

The presence of non-solute particles was

not stated by an optical microscope in
the alkali solutions of keratin which had
been lyophilised and that spatter-dried .
Also in keratin-cellulose solutions with
a concentration not exceeding 10-12%,
such particles were not stated (see Fig-
ure 6.b). Above this concentration level,
many particles of sizes from 2 m to
3 m could be seen in the solution. On
Figure 4. SEM photos (magnification 2000) of spatter-dried keratin preparations; a) K I, the other hand, many particles are visible
b) K II, c) K III, d) K IV. in keratin-alginate solutions with keratin
content above 15% (Figure 6.d).
assume that within the scope of further ers are compatible with cellulose and
investigations this biopolymer will be alginate solutions. With the aim of pre- The preliminary tests of coagulation car-
used to obtain composite fibrous materi- liminarily evaluating the quality of kera- ried out with keratin-cellulose and kera-
als with increased sorption properties. tin solutions, as well as keratin-cellulose tin-alginate solutions were successful,
Our preliminary investigations indicated and keratin-alginate solutions, all of them and allowed us to obtain fibrous prod-
that alkali solutions of keratin from feath- were analysed by an optical microscope. ucts. Further investigations into spinning
test are planned.

a) b)
n The method of drying the keratin
preparations has an essential influence
10 m 10 m
on their properties.
n Spatter-dried keratin preparations are
characterised by better sorption prop-
Figure 5. Microscopic photos; a) solution of keratin after lyophylisation, b) solution of
keratin after spatter drying. erties than lyophilised keratins. The
moisture absorption of spatter-dried
keratin, of about 45%, is significantly
a) b) higher than that of lyophilised keratin,
which is equal to about 20%.
n Modification with monochloroacetic
10 m 10 m
acid also influences the keratin sorp-
tion properties.
n As the result of spatter-drying, kera-
tin preparates were obtained which
c) d) were characterised by particle sizes
below 20 m. The average diameter
values are within the range of 6.2 to
10 m 10 m 9.2 m at a maximum standard devia-
tion of 4.62.
n Solutions with the content of sulf-
hydril groups of 360 mol/g were
Figure 6. Microscopic photos; a) cellulose solution, b) cellulose-keratin solution with
keratin content below 12%, c) alginate solution, d) alginate-keratin solution with keratin obtained after extracting the keratin
content over 15%. from feathers, which indicates that

FIBRES & TEXTILES in Eastern Europe January / March 2007, Vol. 15, No. 1 (60) 111
about 50% of the disulphide bonds 7. Misra M. Kar P., Priyadarshan, G. Keratin
were broken, and at the same the na- Protein Nano-fiber for Removal of Heavy Textile Faculty, TU
tive keratin was significantly structur- Metals and Contaminants. MRS Sympo-
ally modified. sium Proccedings, 2002, 702: U2.1 1-7.
n Spatter-dried keratin is characterised 8. Kar, P. Keratin protein fiber for removal Celebration
of heavy metals from solutions. M.Sc.
by the highest molecular uniform- of the 60th anniversary
ity, with a polydispersion coefficient Thesis. Reno, Nevada: Univ. of Nevada
Reno, 2003. of the Faculty of Engineering
at the level of 2.2 to 2.6, whereas and Marketing of Textiles
9. Novel approach to fabricate keratin
the modified keratin has a relatively (formerly Textile Faculty),
sponge scaffolds with controlled pore Technical University of d
high molecular weight, but is mostly
size and porosity, Biomaterials, Vol. 25,
non-uniform in its molecular structure 8 October 2007
Issue:18, August, 2004, pp. 4255-4262.
(Mw/Mn = 5.8).
10. Fraser R.D., McRae T.P., Rogers G.E.,
n The preliminary tests with the prepa- Keratins. Their composition, structure Invitation
ration and coagulation of keratin- and biosynthesis; Charles C. Thomas:
(sodium alginate) and keratin-(bio- Rector Prof. Jan Krysiski
Springfield, IL, 1972. Ph.D., D.Sc., Dean Prof. Izabella
modified cellulose) spinning solutions 11. Arai K., Takahashi R., Yokote Y.,Akahane Kruciska Ph.D., D.Sc., and the
which we carried out proved that our K. Amino acid sequence of feather kera- Faculty Senate
method for obtaining fibres from these tin from fowl, Eur. J. Biochem. 1983, 132, have the honour
solutions is very promising. of inviting graduates and
501-507. friends to a celebration of the
12. Thannhauser T., Konishi Y., Scherega H., 60th anniversary of the Faculty
Sensitive quantitative analisys of disul- of Engineering and Marketing
n fide bonds in polypeptides and proteins, of Textiles, the Technical
Anal.Biochem. 1984, 138, 181-188.
University of d (TU), on
Further investigation into obtaining fi- 8 October 2007.
bres and fibrous products from spinning 13. Akahane K., Murozono S., Murayama
K., Soluble protens from fowl feather
solutions with keratin content should be After the ceremony,
keratin I. Fractionation and properties, the 9th International
carried out.
J. Biochem. (Tokyo) 1977, 81, 11-18. Conference IMTEX2007
14. Flow behaviour of regenerated keratin will be opened, and then the
proteins in different mediums, Int. J. of first days lectures presenting
the scientific achievements of
Biological Macromolecules Vol. 35, Issue:
Acknowledgment 3-4, April, 2005, pp.151-153.
the academic staff members
will be given.
The investigation presented in this paper was 15. Wolski T., Gliski I., Natural biopolymers
carried out as a part of research project No. and their application based on the exam- Honorary committee:
3 T08 E 078 27 financially supported by the ple of keratin and raw materials composed Chairman:
Polish Ministry of Science and Higher Educa- of lignin (in Polish), Proceed. of the Poly- Prof. Jan Krysiski Ph.D., D.Sc.,
tion over the years 2004 2007. mers Environment Recycling Polish Rector of the TU
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