Journal of Scientific & Industrial Research
Vol. 63, April 2004, pp 323-329
Silk sericin and its applications: A review
M N Padamwar and A P Pawar*
Department of Pharmaceutics, Bharati Vidyapeeth Deemed University, Poona College of Pharmacy, Erandwane,
Pune 411 038
Silk consists of two types of proteins, silk fibroin and sericin. Sericin contributes about 20-30 per cent of total cocoon
weight. It is characterized by its high content of serine and 18 amino acids, including essential amino acids. There are
different methods of isolation of sericin from silk thread. Solubility, molecular weight, and gelling properties of sericin
depend on the method of isolation. It has wide applications in pharmaceuticals and cosmetics such as, wound healing,
bioadhesive moisturizing, antiwrinkle and antiaging.
Keywords: Silk, Silk proteins, Sericin, Isolation
IPC: Int. Cl.7: D 01 B 7/00, D 01 C 3/02, A 61 P
Sericulture in India
Silk has been a scientific curiosity for centuries
and a new insight about these polymers are surfacing
with improved analytical methods and the tools of
molecular biology. Silk includes a broad range of
primarily protein-based high molecular weight
polymers often associated with insects, silkworm, and
orb weaving spiders1. Sericulture, in India, is
essentially a cottage industry. The post rearing
operations are fairly cost-effective and silkworm
rearing is still only considered as a side activity to the
main farm activity. India is the second largest
producer of silk in the world and has the distinction
of producing all the four varieties of silk. Presently,
India produces nearly 16,700 mt silk/y and reeled silk
prices are in the range of Rs 900-1300/kg, the pierced
cocoons and wastesilk generated at the rearing are
sold at Rs 80-100/kg. This waste contributes nearly
30 per cent of total cocoon production2,3. Wastesilk
can be classified as waste from the cocoon, rearing
waste, and thread waste. Silk wastes can be used as
coarse yarn and spun silk, which can be incorporated
in natural rubber to achieve the physicochemical
properties4. It is also possible to utilize the silk waste
by extracting fibroin and sericin from silk polymer,
which helps to make sericulture a viable agro
Structure of Silk
Silk is a continuous strand of two-filaments
cemented together forming the cocoon of silkworm,
Bombyx mori. Silk filament is a double strand of
fibroin, which is held together by a gummy substance
called silk sericin or silk gum. Silk fibroin is the
protein that forms the filament of silkworm and gives
its unique physical and chemical properties4,5. Silk
adapts various secondary structures, including α-
helix, β-sheet, and crossed β-sheet6.
Fibroin is a glycoprotein composed of two
equimolar protein subunits of 370 and 25 kDa
covalently linked by disulphide bonds. Fibroin
filament is made of both crystalline and amorphous
domains. The amorphous domains are characterized
by the presence of amino acids with bulkier side
chains, whereas the crystalline domains are
characterized by high percentage of alanine, glycine,
and serine (12, 30, 44 per cent, respectively), which
contains short side chains to permit the close packing
densities for overlying sheets7. The β-sheet form (silk
II or β-silk) and crystalline form (silk I) have been
reported for silk fibroin, having relative molecular
masses of 350 – 415K (refs 3,8).
Anti-parallel β-sheet structure forming microfibrils
is responsible for the crystalline nature of the silk
fibre. The microfibrils are organized into fibril
bundles, with several bundles leading finally to a
single silk thread7.
*Ph. No: 91-20-5437237
Fax No: 91-20-5439383
J SCI IND RES VOL 63 APRIL 2004
Sericin is a second type of silk protein, which
contains 18 amino acids including essential amino
acids and is characterized by the presence of 32 per
cent of serine. The total amount of hydroxy amino
acids in sericin is 45.8 per cent. There are 42.3 per
cent of polar amino acid and 12.2 per cent of
nonpolar amino acid residues. Sericin contributes
about 20-30 per cent of total cocoon weight. Their
main role is to envelop the fibroin. In presence of
sericin the fibres are hard and tough and become soft
and lustrous after its removal. Sericin occurs mainly
in an amorphous random coil and to a lesser extent, in
a β-sheet organized structure. The randomly coiled
structure easily changes to β-sheet structure, as a
consequence of repeated moisture absorption and
Forms of Silk Sericin
Sericin can be classified into three fractions,
depending on their solubility as sericin A, sericin B,
and sericin C. Sericin A is the outermost layer and
insoluble in hot water. It contains about 17.2 per cent
of nitrogen and amino acids like, serine, threonine,
glycine, and aspartic acid. Sericin B is the middle
layer and on acid hydrolysis it yields amino acid of
sericin A, in addition to tryptophan. It contains 16.8
per cent of nitrogen. Sericin C is the innermost layer,
which is adjacent to fibroin and is insoluble in hot
water and can be removed from fibroin by treatment
with hot dilute acid or alkali. On acid hydrolysis it
yields proline in addition to amino acids of sericin B.
It also contains sulphur and 16.6 per cent of nitrogen
9,10. Sericin has been divided into various species
based on relative solubilities. Various fractions of
sericin are also designated by other researchers
depending on their dissolution behaviour as sericin A
and B, or sericin I, II, III, and IV, or S1, S2, S3, S4,
and S5, and as α, β, and γ modification6,7. The major
molecular conformation of easily soluble sericin is
random coil, whereas the β-sheet structure is more
difficult to dissolve. The repeated moisture
absorption makes molecular aggregation structure
denser and forms more crystalline structure, which is
having reduced solubility.
The γ-ray study shows the three layers in the
sericin structure. The outer layer contained some fibre
direction filaments, middle layer exhibits cross-fibre
direction filaments, and the inner layer shows
longitudinal filaments11. The structure of sericin also
depends on the casting temperature. Lower the
casting temperature more the sericin molecules
assume β-sheet structure rather than random coil12,13.
Properties of Silk Sericin
Sericin contains random coil and β-sheet structure.
Random coil structure is soluble in hot water and as
the temperature lowers the random coil structure
converts to β-sheet structure, which results in gel
Sericin has sol-gel property as it easily dissolves
into water at 50-60oC and again returns to gel on
As there are more acidic than basic amino acid
residues the isoelectric point of sericin is about 4.0
Solubility of Sericin
Solubility of sericin in water decreases when the
sericin molecules are transformed from random coil
into the β sheet structure. The solubility of sericin
increases by addition of poly (Na acrylate) and
decreases by the addition of polyacrylamide,
formaldehyde, or resin finishing agents17-19.
Extracting sericin using 1 per cent sodium
deoxycholate solution followed by precipitation,
using equal volume of 10 per cent trichloroacetic
acid, shows molecular weight in the range of 17100 to
18460 (ref. 20).
Extraction of sericin by hot water shows molecular
weight of 24000 by gel electrophoresis, whereas
spray-drying method produced sericin of molecular
weight 5000-50,000, with enzyme action 300-10,000
and 50,000 when it is extracted with aqueous urea at
100ºC (ref. 21).
Isolation of Silk Sericin
Isolation with Aid of Heat
The removal of gum from crude silk is based
entirely upon its solubility in hot water. The number
of methods illustrated by researchers for removing
gum are as follows:
PADAMWAR & PAWAR: SILK SERICIN AND ITS APPLICATIONS
• The removal of gum by dilute solution of
• Hot water extraction of raw silk, followed by
evaporation to obtain powder.
• Boiling of the crude silk in water and renewing
the water until the extract no longer gives a
precipitate with gallic acid.
• Three successive 1 h extractions of silk or
simply heating in water at 100ºC or autoclaving
at 118°C or autoclaving for 3 h under 2.5-3
• Sericin with average molecular weight of 50,000
extracted with aqueous solution of urea at 100ºC
• Using water at 50-60ºC for 25 d to avoid the
• Silk fibres can be completely degummed in
boiling solutions of pH 11 containing 5-6 per
In a series of experiments, it is demonstrated that
most of the sericin is removed by autoclaving for one
and half hour under pressure of 600-700 mm Hg (14
lb), whereas increasing the time of treatment to 2 h
causes no greater loss in weight of fibres. It is also
observed that the extracting sericin at low pressure
(25 cm Hg, 5 lb) shows good results.
When sericin is extracted from cocoons of Bombyx
mori by heating on water bath and autoclaving at
different temperatures the satisfactory yield is
obtained by autoclaving at 105°C for 30 min with
good gelling property and yield. Further increase in
temperature increases the yield but looses its gelling
Extraction of Silk Sericin using Enzymes
Extraction is carried out by using enzyme
alkylase25 or with 2-2.5g/L alkaline protease at 60°C
for 90 min, at pH 10 (ref. 26).
Hydrolysis with trypsin at different concentrations,
temperatures and treatment times is employed for
extraction of sericin. For 1 per cent of trypsin
solution the hydrolysis is almost complete in 10 and
32 h at 37 and 20°C, respectively. The amount of
sericin obtained by 4 h treatment with 1 and 8 per
cent of trypsin solution is 26.4 and 28.7 per cent,
Precipitation of Silk Sericin from Aqueous Solution
Several methods22 proposed for precipitations of
sericin from its aqueous solution are as follows:
• Precipitation of sericin with lead acetate from
aqueous solution, which is decomposed by
hydrogen sulphide and the protein is separated
• Evaporation of sericin solution and dissolution
of obtained residue in alkali followed by
precipitation by alcohol.
• Precipitation of sericin from aqueous extract by
acetic acid and then treating the precipitate with
alcohol and ether.
• According to Shelton and Johnson22 the method
of recovery by evaporation to dryness is least
satisfactory. Protein molecule on continuous
boiling of the aqueous solution in an open kettle
loses its capacity to form gel. A method in
which hot concentrated sericin solution is
poured directly from the autoclave into 7 to 8
vol of 95 per cent alcohol is found to be
satisfactory. The clear supernatant liquor is
separated from the precipitate and the
precipitate is washed with 95 per cent alcohol.
The obtained cake is dried slowly over calcium
chloride in a desiccator to get white and easily
• Salting out of sericin solution by addition of
15 g solid ammonium sulphate to each 100 mL
of solution results in gelatinous precipitate,
which does not support bacterial growth.
• Hamaoka et al.28 have extracted silk with
hexane to remove oils and fats and by heating in
water at 120°C for 30 min. After freeze thawing
the sericin deposited in thawing is washed with
hydrophilic organic solvent and the powdered
sericin is recovered.
Applications of Silk Sericin
Silk sericin due to its proteinous nature is
susceptible to the action of proteolytic enzymes
present in body and hence it is digestible. This
property makes it a biocompatible and biodegradable
material. Because of some additional properties like,
gelling ability, moisture retention capacity, and skin
adhesion. it has wide applications in medical,
pharmaceutical, and cosmetics.
Medical and Pharmaceutical Applications
J SCI IND RES VOL 63 APRIL 2004
Sericin is soluble in hot water and as the time
precedes it converts into gel. Jun et al.29 have found
that conversion of α-random coil to β-sheet structure
gives gel. One per cent aqueous sericin solution
produces gel at pH 6-7 at room temperature and
gelation speed increases as the concentration of
sericin increases30-32. The aqueous sericin solution
containing 1.5 and 2 per cent w/w of sericin obtained
by autoclaving at 105°C for 30 min does not show
good gelling. Sericin gel in the presence of glycerin,
propylene glycol, and tween-80 shows synerisis,
whereas sericin with pluronic and carbopol gives
stable gels. In the presence of pluronic sericin gel it
shows concentration dependance24. Kewon et al.33
have shown the effect of concentration of pluronic
and temperature on the gel property of sericin. The
gelling of sericin is accelerated with increase in
temperature and with increase in poloxamer
concentration, whereas the sol-gel transition of
sericin becomes irreversible. Blends of polyvinyl
alcohol and sericin are cross-linked to give hydrogels.
Hydrogels with good mechanical strength and water
resistance are produced by casting aqueous solution
containing sericin and dimethyl urea on a glass plate
and heating at 80 and 120°C for 1 and 3 h,
Sericin gives a very stable emulsion when shaken
with water immiscible liquid22,35. The sericin protein
is also used as horizontal alignment film for the liquid
crystal to achieve uniform optical properties and to
increase the stability of product36.
Fibroin and sericin, when sulphonated show anti-
thrombotic effect37. One stage condensation of
salicylic acid, formaldehyde, and sericin creates a co-
polymer with a molecular mass of 6000-8000 Da. A
concentration of 0.01-1 mg/mL in blood exhibits anti-
coagulant, fibrinolytic, and anti-aggregation activity
towards thrombocytes at 0.5 mg/mL (ref. 38). Sericin
with molecular weight of 1,00,000 shows an
inhibitory action for tyrosinase and lipid per
oxidation with rat brain homogenates39,40. The
addition of 0.1-2 mg/mL of sericin into the aqueous
solution shows heat resistant DNA polymerase
activity41. Sericin has been found to possess wound-
healing property and can be used as wound healing
covering material in the form of film42. Sericin also
has adhesive property due to its chemical
composition. It has affinity to keratin7. Silk threads
obtained from mulberry silkworm can be used for
making surgical sutures43. Silk sericin membranes are
good bandage materials and the film has adequate
flexibility and tensile strength. Due to its good
biocompatibility and infection resistant nature, it is a
novel wound coagulant material. Additionally, its
flexibility and water absorption properties promote
smooth cure for defects in the skin and do not cause
any peeling of the skin under regeneration when
detached from the skin44.
Kurioka45 has explained silk sericin as a
biomaterial. The silk sericin has the potential to find
application in the development of contact lenses. The
graft polymers are prepared with methyl methacrylate
or styrene and are also biocompatible46,47.
Intake of sericin containing food relives
constipation, suppresses development of bowel
cancer and accelerates the absorption of minerals. In
rats, consumption of sericin elevates the apparent
absorption of zinc, iron, magnesium, and calcium by
41, 41, 21, and 17 per cent, respectively48. A dietary
supplementation of 4 per cent of sericin suppresses
induced constipation in rats because of its low
digestibility along with water holding capacity49.
Sericin, when given orally, causes a dose dependent
decrease in the development of colonic aberrant crypt
foci. The incidence and the number of colon tumours
are suppressed by consumption of sericin. Sericin
have anti-tumor activity50-52.
Oxygen permeable membranes are made up of
fibroin and sericin with 10-16 per cent water and are
used for contact lenses, and as artificial skin53. Agar
and/or compounds containing agarose and sericin are
mixed with water to form sheet shaped gels and
which when dried at 0-40°C under load of 0.01-2
kg/cm2 give the polymer membranes54.
In addition to above-mentioned medical and
pharmaceutical uses of sericin, it has been used as
component of cosmetics. Sericin alone or in
combination with silk fibroin has been used in skin,
hair, and nail cosmetics. Sericin when used in the
form of lotion, cream and ointment shows increased
skin elasticity, antiwrinkle, and antiaging effects7,55-57.
Padamwar et al.58 have shown the moisturizing
property of the sericin gel, evaluated by
hydroxyproline assay, impedance measurement,
trance epidermal water loss (TEWL), and scanning
electron microscopy (SEM). Sericin gels increase the
PADAMWAR & PAWAR: SILK SERICIN AND ITS APPLICATIONS
hydroxyproline content in stratum corneum and
decrease skin impedance, which reveals moisturizing
property of sericin. Sericin gels with pluronic and
carbopol, act as moisturizer by repairing natural
moisturizing factor (NMF) as well as prevent TEWL
by preventing water loss from the skin. SEM has
shown the decrease cracking and flaking as compare
to dry skin and normal skin replicas.
Powder containing 5-30 per cent sericin with
average molecular weight 7,000-3,00,000 and 70-95
per cent silk fibroin when applied as film shows
antistaticity and moisture absorbability59. Sericin
hydrolysate solution shows that dermatitis is
controlled60. Sweat and sebum absorbing type of
cosmetics containing cellulose fibres impregnated
with fibroin dispersion and aqueous sericin solution
are also reported61. Lotion containing 1 per cent w/w
sericin and 4 per cent w/w D-glucose shows
moisturizing and conditioning effect62. Creams
containing 0.001-30 per cent w/w of sericin have
improved cleansing properties with less skin
irritation63. Sericin powder in the form of sericin
hydrolysate coated talc, mica, titania, iron oxide, and
nylon have been used to formulate foundation cream
and eyeliners64. The microcapsules or nanocapsules
consisting of polysiloxane gel, UV absorbent core
and UV scattering agent, silicone treated mica, silicon
treated titanium dioxide, silicon treated iron oxides,
squalene, glycerin trioctanoate, and talc have resulted
in cosmetic foundation having a SPF value of 25.7.
Sericin in sunscreen composition enhances the light
screening effect of UV filter like triazines, and
cinnamic acids ester65.
Nail cosmetics, containing 0.02-20 per cent sericin
are reported to prevent nail from chapping,
brittleness, and imparting the inherent gross to nails66.
Hair and bath preparations, containing 0.02-2 per cent
sericin and 0.01-1 per cent olive oil, fatty acid or their
salts show reducing damage of hair surface by
binding of sericin to hairs67. Sericin hydrolysates with
average molecular weight 300-3000 are used as
conditioners for skin and hair68. Shampoo containing
sericin and pelarogenic acid of pH less than six are
useful for the care and cleaning of hairs69.
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