Volume 7, Issue 3, Spring2012

Exploration on Amino Acid Content and Morphological Structure

in Chicken Feather Fiber

Kannappan Saravanan
Assistant Professor
Bhaarathi Dhurai, Ph.D. Candidate
Department of Textile Technology
Kumaraguru College of Technology
Coimbatore, India

ABSTRACT

Converting poultry feather biomass into useful products presents a new avenue of
utilization of agricultural waste material. However, not much is understood about the poultry
feather structure or methods to process it. Fibers from non-traditional textile sources have the
potential to offer novel properties at a reduced cost compared to traditional textile fibers.
Feather constitutes over 90% protein, the main component being beta-keratin, a fibrous and
insoluble structural protein extensively cross linked by disulfide bonds. An attempt has been made
to analyze the amino acid content and the morphological structure of chicken feather fibers for
prospective use as natural protein fibers. The study reveals that the presence of both hydrophobic
and hygroscopic nature of amino acid makes the feather partially hygroscopic in nature. The
presence fat content is about 1.53%. Using the cheap and plentiful feathers as protein fibers will
save the cost and benefit the environment.

Keywords: Chicken feather fiber, Keratin, Structure, Amino acid content, SEM

1. Introduction complex branched structure that grow by a

unique mechanism from cylindrical feather
It is possible to find in nature an almost
follicles. This branching structure, a
unlimited source of high performance
distinctive morphological feature of
materials which remain to be critically
feathers, has its origin in the biological
studied to establish them as basis for
evolution of feathers. [McGovern, 2000]
innovative technologies and useful raw
materials. This is the case for keratin fibers
Figure 1 shows the contour feather has a
abundant in chicken feathers. Keratin,
feather shaft and a flat vane extending from
considered as the main structural component
it [Bartels, T. 2003]. Feathers are highly
of these materials, contributes to a wide
ordered, hierarchical branched structures,
range of essential functions, including
ranking among the most complex of keratin
temperature control and physical and
structures found in vertebrates. Feathers not
chemical protection. Structural studies of
only confer the ability of flight, but are
hair fibers, including wool, reveal highly
essential for temperature regulation. [Yu, M,
organized subcomponents that could be also
2002]
found in feather fibers starting from their
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Volume 7, Issue 3, Spring 2012
 then soaping process is carried out and air-
dried.
2.2 Methods
Analysis of Samples for Amino acids by
High Performance Thin Layer
Chromatography (HPTLC)
Sample Digestion
The given Chicken feather samples each
250mg were weighed accurately in an
electronic balance and transferred into
labeled glass test tubes (BOROSIL). 3ml of
Figure 1. A contour feather [Bartels 2003] 6M Hydrochloric acid solution was added
with sample in specified test tubes. All the
2. Materials and Methods sealed tubes were kept in a hot-air oven at
2.1 Materials 110oC for 48hrs continuously.
The Chicken feather fibers (CFF) were Test Solution Preparation
obtained from the poultry farms. Then it is After completion of digestion, broken the
purified by washing and sterilization. The tubes at the top and transferred the digest
untreated CFF was washed with the 5% soap into glass beaker (BOROSIL), rinsed the
solution followed by rinsing. The wet tubes 5 times with distilled water. The acid
washed CFF was dried on moderate heat. in the digest was evaporated to core dry
The barbs are removed from the quill and under vacuum using Roto-vac evaporator.
the short fibers (10 to 32 mm) were The residual content was dissolved with
obtained. Sterilization process is carried out distilled water and made-up to 6ml in a
by washed CFF and were dipped at room centrifuge tubes. This solution contains
temperature (21C for 30 minutes 41.6g dried raw sample in 1l distilled
respectively)in polar solvent and water, with water and used as test solution for amino-
pH adjusted to 8, then rinsed with water, acid profile analysis by HPTLC technique.
HPTLC ANALYSIS
Group I Group II Group III Group IV
Asparagine Aspartic acid Lysine Histidine
Glutamine Glycine Glutamic acid Arginine
Serine Alanine Threonine Cystine
Proline Valine Tyrosine Tryptophan
Methionine Phenyl alanine Isoleucine Leucine

Morphological Structure with gold palladium prior to observation in

the SEM. A 15 kV voltage was used for all
The Scanning Electron Microscope, Optical
the observations.
Microscope and Tunneling Electron
Microscope were used to study the
3. Result and Discussion
longitudinal and cross-sectional features of 3.1 Composition and Amino Acid
the barbs. Barbs were mounted on a Sequence of Chicken Feather Fiber
conductive adhesive tape and sputter coated

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Volume 7, Issue 3, Spring 2012
Chicken feathers are approximately 91% common with reptilian keratins from claws.
protein (keratin), 1% lipids, and 8% water The sequence is largely composed of
[Lederer, R]. The amino acid sequence of a cystine, glutamine, proline, and serine, and
chicken feather is very similar to that of contains almost no histidine, lysine,
other feathers and also has a great deal in Tryptophan, Glutamic acid and Glycine.

Figure 2. 3-D Display of all tracks

From Figure 2, it is confirmed that the following amino acids are present in the chicken feather
fiber and the percentage of the same are also given in Table 1.
Table 1. Amino acid content in keratin fiber from chicken feather
Functional Groups Amino acid % Contents
Positively charged Arginine 4.30
Aspartic acid 6.00
Negatively charged
Glutamine 7.62
Theronine 4.00
Hygroscopic
Serine 16.0
Tyrosine 1.00
Leucine 2.62
Isoleucine 3.32
Valine 1.61
Hydrophobic
Cystine 8.85
Alanine 3.44
Phenylalanine 0.86
Methionine 1.02
Special Proline 12.0
Asparagine 4.00

Serine (16%) is the most abundant amino moisture from the air. Feather fiber is,
acid and the -OH group in each serine therefore, hygroscopic. Chicken feather
residue helps chicken feathers to absorb the

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fibers and quill have a similar content of an average molecular weight of about
moisture, around 6%. 60,500 g/mol.

The presence of amino acids in the chicken The human hair contains -helical
feather fiber which is hydrophobic in nature polypeptide feather keratin can contain both
contributes to a percentage of about 22%, -helical and -sheet conformations.
therefore, hydrophobic. Hence, the chicken Chicken feather fiber primarily consists of
feather fiber posses both Hydrophobic and -helical conformations, and some -sheet
Hygroscopic character and approximately conformations are present [Naresh et al
the ratio will be 60:40 percentages. 1991]. Chicken feather outer quill consists
almost entirely of -sheet conformations,
The estimated value of total Fat content in and few -helical conformations are present
Chicken Feather is 1.53% [Schmidt, W.F. et al 2003]. Hard -sheet
Feather keratins are composed of about 20 keratins have a much higher cystine content
kinds of proteins, which differ only by a few than soft -helix keratins and thus a much
amino acids. The distribution of amino acids greater presence of disulfide (S-S) chemical
is highly non-uniform, with the basic and bonds which link adjacent keratin proteins
acidic residues and the cystine residues (Fig 3). These strong covalent bonds
concentrated in the N- and C-terminal stabilize the three-dimensional protein
regions. The central portion is rich in structure and are very difficult to break
hydrophobic residues and has a crystalline [Alberts, B, 1994].
-sheet conformation.

Feather keratin is a special protein. It has a

high content of cystine (8.85%) in the amino
acid sequence (see Table 1), and cystine has
-SH groups and causes the sulfursulfur
(disulfide) bonding. The high content
cystine makes the keratin stable by forming
network structure through joining adjacent
polypeptides by disulfide cross-links.

The feather keratin fiber is semi-crystalline

and made up from a crystalline fiber phase
and an amorphous protein matrix phase
linked to each other [Schmidt, W.F., 1998]. Figure 3. Diagrammatic representation of
The crystalline phase consists of -helical the diamino-acid cystine residue
protein braided into micro-fibrils where the linking two polypeptide chains
protein matrix is fixed by intermolecular by covalent bonding (Alberts,
interactions, especially hydrogen bonds. In B, 1994)
protein, hydrogen bonds are many and
strong.

The feather barb fraction has slightly more

-helix over sheet structure, whose melting
point is 240 C. The quill has much more
sheet than -helix structure and has a
melting point of 230 C. Feather keratin has

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3.2 Structural Study

Figure 4. A schematic diagrams of

chicken feathers

Barbs coming from the thick central quill

and also nodes along each barb are shown in
Figure 4; it can be assumed that the nodes
are similar to the cuticle scales in wool. The
cuticle consists of layers of scales and its Figure 5. A & B: SEM figures -
function is to protect the fiber's cortex. Longitudinal structure of chicken
Nodes and barbs on the feather fiber are feather fiber
related to memory properties and improve
structural strength. Keratin fibers have a Figure 5 A & B shows the SEM. The micro-
high degree of flexibility, mechanical fibrils are twisted forming a helix that is
property that depends on its small diameter, responsible of the fibers high mechanical
high elastic modulus and shape, and that strength. It is clear from the picture that the
should be used to modify bulk elastic barbs are having branches called as
properties of new materials. barbules, which can contribute to the
resilience property of the feathers. The
cleave lines or striations along the fibers
give rise to a certain surface roughness,
which can contribute to interfacial strength
that in addition to the high length to
diameter ratio reached for the fiber can be
useful for reinforcing composites (one of the
possible applications for this fiber).

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 exceptional shape, a center fiber with many
branching fibers, makes feather fibers,
useful for different applications like filter
material, storing material, composite
material etc.

Acknowledgement
The authors would like to thank the
management of Kumaraguru College of
Technology, Coimbatore, for funding to
carry out this work.

References
[1] Alberts, B., Bray, D., Lewis, J., Raff,
M., Roberts, K., Watson, J.D. 1994,
Molecular Biology of the Cell , 3rd
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[2] Bartels, T. 2003, Variations in the
morphology, distribution, and
arrangement of feathers in domesticated
birds Journal of Experimental Zoology
(Mol. Dev. Evol.), 298B, pp.91-108.
[3] Lederer, R. Integument, Feathers, and
Molt Ornithology: The Science of Birds
http://www.ornithology.com.
Figure 6. Optical Microscope (A) and TEM
(B) - cross sectional views of [4] McGovern, Victoria 2000, Recycling
chicken feather fiber Poultry Feathers: More Bang For The
Cluck Environmental Health
Figure 6A shows the honeycomb structure
Perspectives.
of the feather and confirms the possibility of
more air pockets in the feather which [5] Naresh, M.D., Subramanian, V.,
contributes to the high thermal resistance Arumugam, V., Sanjeevi, R. 1991, A
characteristic. Figure 6B confirms the Study on the Mechanism of Failure in
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The former has a more order and crystalline [6] Schmidt, W.F. 1998, Innovative Feather
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4. Conclusion [7] Schmidt, W.F. and Jayasundera, S. 2003,
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The amino acid content reveals that the fiber Fibers, Plastics, and Composites Recent
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hygroscopic in nature. The microscopic pp.51-66.
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feather fibers characteristics that it is [8]. Yu, M., Wu, P., Widelitz, R.B., Chuong,
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