See discussions, stats, and author profiles for this publication at: https://www.researchgate.

net/publication/228823994

Silk sericin and its applications: A review

Article  in  Journal of scientific and industrial research · May 2004

CITATIONS READS
121 7,887

2 authors:

Mahesh N. Padamwar Atmaram P Pawar

MSN Laboratories Ltd. Bharati Vidyapeeth Deemed University
13 PUBLICATIONS   464 CITATIONS    34 PUBLICATIONS   797 CITATIONS   

SEE PROFILE SEE PROFILE

Some of the authors of this publication are also working on these related projects:

Tablets and capsules for various molecules for US, Europe, Australia, ROW, etc. View project

All content following this page was uploaded by Mahesh N. Padamwar on 22 May 2014.

The user has requested enhancement of the downloaded file.

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

Introduction industry.
Structure of Silk
Sericulture in India
Silk is a continuous strand of two-filaments
Silk has been a scientific curiosity for centuries
cemented together forming the cocoon of silkworm,
and a new insight about these polymers are surfacing
Bombyx mori. Silk filament is a double strand of
with improved analytical methods and the tools of
fibroin, which is held together by a gummy substance
molecular biology. Silk includes a broad range of
called silk sericin or silk gum. Silk fibroin is the
primarily protein-based high molecular weight
protein that forms the filament of silkworm and gives
polymers often associated with insects, silkworm, and
its unique physical and chemical properties4,5. Silk
orb weaving spiders1. Sericulture, in India, is
adapts various secondary structures, including α-
essentially a cottage industry. The post rearing
helix, β-sheet, and crossed β-sheet6.
operations are fairly cost-effective and silkworm
rearing is still only considered as a side activity to the Fibroin is a glycoprotein composed of two
main farm activity. India is the second largest equimolar protein subunits of 370 and 25 kDa
producer of silk in the world and has the distinction covalently linked by disulphide bonds. Fibroin
of producing all the four varieties of silk. Presently, filament is made of both crystalline and amorphous
India produces nearly 16,700 mt silk/y and reeled silk domains. The amorphous domains are characterized
prices are in the range of Rs 900-1300/kg, the pierced by the presence of amino acids with bulkier side
cocoons and wastesilk generated at the rearing are chains, whereas the crystalline domains are
sold at Rs 80-100/kg. This waste contributes nearly characterized by high percentage of alanine, glycine,
30 per cent of total cocoon production2,3. Wastesilk and serine (12, 30, 44 per cent, respectively), which
can be classified as waste from the cocoon, rearing contains short side chains to permit the close packing
waste, and thread waste. Silk wastes can be used as densities for overlying sheets7. The β-sheet form (silk
coarse yarn and spun silk, which can be incorporated II or β-silk) and crystalline form (silk I) have been
in natural rubber to achieve the physicochemical reported for silk fibroin, having relative molecular
properties4. It is also possible to utilize the silk waste masses of 350 – 415K (refs 3,8).
by extracting fibroin and sericin from silk polymer, Anti-parallel β-sheet structure forming microfibrils
which helps to make sericulture a viable agro is responsible for the crystalline nature of the silk
fibre. The microfibrils are organized into fibril
—————— bundles, with several bundles leading finally to a
*Ph. No: 91-20-5437237 single silk thread7.
Fax No: 91-20-5439383
e-mail: m_padamwar@yahoo.co.in Sericin
p_atmaram@rediffmail.com
324 J SCI IND RES VOL 63 APRIL 2004

Sericin is a second type of silk protein, which depends on the casting temperature. Lower the
contains 18 amino acids including essential amino casting temperature more the sericin molecules
acids and is characterized by the presence of 32 per assume β-sheet structure rather than random coil12,13.
cent of serine. The total amount of hydroxy amino Properties of Silk Sericin
acids in sericin is 45.8 per cent. There are 42.3 per
cent of polar amino acid and 12.2 per cent of Gelling Property
nonpolar amino acid residues. Sericin contributes Sericin contains random coil and β-sheet structure.
about 20-30 per cent of total cocoon weight. Their Random coil structure is soluble in hot water and as
main role is to envelop the fibroin. In presence of the temperature lowers the random coil structure
sericin the fibres are hard and tough and become soft converts to β-sheet structure, which results in gel
and lustrous after its removal. Sericin occurs mainly formation14, 15.
in an amorphous random coil and to a lesser extent, in Sol-Gel Transition
a β-sheet organized structure. The randomly coiled Sericin has sol-gel property as it easily dissolves
structure easily changes to β-sheet structure, as a into water at 50-60oC and again returns to gel on
consequence of repeated moisture absorption and cooling16.
mechanical stretching7,9.
Isoelectric pH
Forms of Silk Sericin As there are more acidic than basic amino acid
Sericin can be classified into three fractions, residues the isoelectric point of sericin is about 4.0
depending on their solubility as sericin A, sericin B, (ref. 7).
and sericin C. Sericin A is the outermost layer and
Solubility of Sericin
insoluble in hot water. It contains about 17.2 per cent
Solubility of sericin in water decreases when the
of nitrogen and amino acids like, serine, threonine,
sericin molecules are transformed from random coil
glycine, and aspartic acid. Sericin B is the middle
into the β sheet structure. The solubility of sericin
layer and on acid hydrolysis it yields amino acid of
increases by addition of poly (Na acrylate) and
sericin A, in addition to tryptophan. It contains 16.8
decreases by the addition of polyacrylamide,
per cent of nitrogen. Sericin C is the innermost layer,
formaldehyde, or resin finishing agents17-19.
which is adjacent to fibroin and is insoluble in hot
water and can be removed from fibroin by treatment Molecular Weight
with hot dilute acid or alkali. On acid hydrolysis it Extracting sericin using 1 per cent sodium
yields proline in addition to amino acids of sericin B. deoxycholate solution followed by precipitation,
It also contains sulphur and 16.6 per cent of nitrogen using equal volume of 10 per cent trichloroacetic
9,10
. Sericin has been divided into various species acid, shows molecular weight in the range of 17100 to
based on relative solubilities. Various fractions of 18460 (ref. 20).
sericin are also designated by other researchers Extraction of sericin by hot water shows molecular
depending on their dissolution behaviour as sericin A weight of 24000 by gel electrophoresis, whereas
and B, or sericin I, II, III, and IV, or S1, S2, S3, S4, spray-drying method produced sericin of molecular
and S5, and as α, β, and γ modification6,7. The major weight 5000-50,000, with enzyme action 300-10,000
molecular conformation of easily soluble sericin is and 50,000 when it is extracted with aqueous urea at
random coil, whereas the β-sheet structure is more 100ºC (ref. 21).
difficult to dissolve. The repeated moisture
absorption makes molecular aggregation structure
Isolation of Silk Sericin
denser and forms more crystalline structure, which is
having reduced solubility. Isolation with Aid of Heat
The γ-ray study shows the three layers in the The removal of gum from crude silk is based
sericin structure. The outer layer contained some fibre entirely upon its solubility in hot water. The number
direction filaments, middle layer exhibits cross-fibre of methods illustrated by researchers for removing
direction filaments, and the inner layer shows gum are as follows:
longitudinal filaments11. The structure of sericin also
 PADAMWAR & PAWAR: SILK SERICIN AND ITS APPLICATIONS 325

• The removal of gum by dilute solution of Several methods22 proposed for precipitations of
sodium carbonate. sericin from its aqueous solution are as follows:
• Hot water extraction of raw silk, followed by • Precipitation of sericin with lead acetate from
evaporation to obtain powder. aqueous solution, which is decomposed by
• Boiling of the crude silk in water and renewing hydrogen sulphide and the protein is separated
the water until the extract no longer gives a by alcohol.
precipitate with gallic acid. • Evaporation of sericin solution and dissolution
• Three successive 1 h extractions of silk or of obtained residue in alkali followed by
simply heating in water at 100ºC or autoclaving precipitation by alcohol.
at 118°C or autoclaving for 3 h under 2.5-3 • Precipitation of sericin from aqueous extract by
atmosphere pressure. acetic acid and then treating the precipitate with
• Sericin with average molecular weight of 50,000 alcohol and ether.
extracted with aqueous solution of urea at 100ºC • According to Shelton and Johnson22 the method
from cocoons21. of recovery by evaporation to dryness is least
• Using water at 50-60ºC for 25 d to avoid the satisfactory. Protein molecule on continuous
decomposition.22 boiling of the aqueous solution in an open kettle
• Silk fibres can be completely degummed in loses its capacity to form gel. A method in
boiling solutions of pH 11 containing 5-6 per which hot concentrated sericin solution is
cent bentonite23. poured directly from the autoclave into 7 to 8
In a series of experiments, it is demonstrated that vol of 95 per cent alcohol is found to be
most of the sericin is removed by autoclaving for one satisfactory. The clear supernatant liquor is
and half hour under pressure of 600-700 mm Hg (14 separated from the precipitate and the
lb), whereas increasing the time of treatment to 2 h precipitate is washed with 95 per cent alcohol.
causes no greater loss in weight of fibres. It is also The obtained cake is dried slowly over calcium
observed that the extracting sericin at low pressure chloride in a desiccator to get white and easily
(25 cm Hg, 5 lb) shows good results. pulverized powder.
When sericin is extracted from cocoons of Bombyx • Salting out of sericin solution by addition of
mori by heating on water bath and autoclaving at 15 g solid ammonium sulphate to each 100 mL
different temperatures the satisfactory yield is of solution results in gelatinous precipitate,
obtained by autoclaving at 105°C for 30 min with which does not support bacterial growth.
good gelling property and yield. Further increase in • Hamaoka et al.28 have extracted silk with
temperature increases the yield but looses its gelling hexane to remove oils and fats and by heating in
property24. water at 120°C for 30 min. After freeze thawing
the sericin deposited in thawing is washed with
Extraction of Silk Sericin using Enzymes hydrophilic organic solvent and the powdered
Extraction is carried out by using enzyme sericin is recovered.
alkylase25 or with 2-2.5g/L alkaline protease at 60°C
for 90 min, at pH 10 (ref. 26). Applications of Silk Sericin
Hydrolysis with trypsin at different concentrations, Silk sericin due to its proteinous nature is
temperatures and treatment times is employed for susceptible to the action of proteolytic enzymes
extraction of sericin. For 1 per cent of trypsin present in body and hence it is digestible. This
solution the hydrolysis is almost complete in 10 and property makes it a biocompatible and biodegradable
32 h at 37 and 20°C, respectively. The amount of material. Because of some additional properties like,
sericin obtained by 4 h treatment with 1 and 8 per gelling ability, moisture retention capacity, and skin
cent of trypsin solution is 26.4 and 28.7 per cent, adhesion. it has wide applications in medical,
respectively27. pharmaceutical, and cosmetics.

Precipitation of Silk Sericin from Aqueous Solution Medical and Pharmaceutical Applications
326 J SCI IND RES VOL 63 APRIL 2004

Sericin is soluble in hot water and as the time making surgical sutures43. Silk sericin membranes are
precedes it converts into gel. Jun et al.29 have found good bandage materials and the film has adequate
that conversion of α-random coil to β-sheet structure flexibility and tensile strength. Due to its good
gives gel. One per cent aqueous sericin solution biocompatibility and infection resistant nature, it is a
produces gel at pH 6-7 at room temperature and novel wound coagulant material. Additionally, its
gelation speed increases as the concentration of flexibility and water absorption properties promote
sericin increases30-32. The aqueous sericin solution smooth cure for defects in the skin and do not cause
containing 1.5 and 2 per cent w/w of sericin obtained any peeling of the skin under regeneration when
by autoclaving at 105°C for 30 min does not show detached from the skin44.
good gelling. Sericin gel in the presence of glycerin, Kurioka45 has explained silk sericin as a
propylene glycol, and tween-80 shows synerisis, biomaterial. The silk sericin has the potential to find
whereas sericin with pluronic and carbopol gives application in the development of contact lenses. The
stable gels. In the presence of pluronic sericin gel it graft polymers are prepared with methyl methacrylate
shows concentration dependance24. Kewon et al.33 or styrene and are also biocompatible46,47.
have shown the effect of concentration of pluronic Intake of sericin containing food relives
and temperature on the gel property of sericin. The constipation, suppresses development of bowel
gelling of sericin is accelerated with increase in cancer and accelerates the absorption of minerals. In
temperature and with increase in poloxamer rats, consumption of sericin elevates the apparent
concentration, whereas the sol-gel transition of absorption of zinc, iron, magnesium, and calcium by
sericin becomes irreversible. Blends of polyvinyl 41, 41, 21, and 17 per cent, respectively48. A dietary
alcohol and sericin are cross-linked to give hydrogels. supplementation of 4 per cent of sericin suppresses
Hydrogels with good mechanical strength and water induced constipation in rats because of its low
resistance are produced by casting aqueous solution digestibility along with water holding capacity49.
containing sericin and dimethyl urea on a glass plate Sericin, when given orally, causes a dose dependent
and heating at 80 and 120°C for 1 and 3 h, decrease in the development of colonic aberrant crypt
respectively34. foci. The incidence and the number of colon tumours
Sericin gives a very stable emulsion when shaken are suppressed by consumption of sericin. Sericin
with water immiscible liquid22,35. The sericin protein have anti-tumor activity50-52.
is also used as horizontal alignment film for the liquid Oxygen permeable membranes are made up of
crystal to achieve uniform optical properties and to fibroin and sericin with 10-16 per cent water and are
increase the stability of product36. used for contact lenses, and as artificial skin53. Agar
Fibroin and sericin, when sulphonated show anti- and/or compounds containing agarose and sericin are
thrombotic effect37. One stage condensation of mixed with water to form sheet shaped gels and
salicylic acid, formaldehyde, and sericin creates a co- which when dried at 0-40°C under load of 0.01-2
polymer with a molecular mass of 6000-8000 Da. A kg/cm2 give the polymer membranes54.
concentration of 0.01-1 mg/mL in blood exhibits anti-
coagulant, fibrinolytic, and anti-aggregation activity Cosmetic Applications
towards thrombocytes at 0.5 mg/mL (ref. 38). Sericin In addition to above-mentioned medical and
with molecular weight of 1,00,000 shows an pharmaceutical uses of sericin, it has been used as
inhibitory action for tyrosinase and lipid per component of cosmetics. Sericin alone or in
oxidation with rat brain homogenates39,40. The combination with silk fibroin has been used in skin,
addition of 0.1-2 mg/mL of sericin into the aqueous hair, and nail cosmetics. Sericin when used in the
solution shows heat resistant DNA polymerase form of lotion, cream and ointment shows increased
activity41. Sericin has been found to possess wound- skin elasticity, antiwrinkle, and antiaging effects7,55-57.
healing property and can be used as wound healing Padamwar et al.58 have shown the moisturizing
covering material in the form of film42. Sericin also property of the sericin gel, evaluated by
has adhesive property due to its chemical hydroxyproline assay, impedance measurement,
composition. It has affinity to keratin7. Silk threads trance epidermal water loss (TEWL), and scanning
obtained from mulberry silkworm can be used for electron microscopy (SEM). Sericin gels increase the
 PADAMWAR & PAWAR: SILK SERICIN AND ITS APPLICATIONS 327

hydroxyproline content in stratum corneum and 2 Sericulture, Chapter VIII, Annual Report 2002-2003
decrease skin impedance, which reveals moisturizing (Ministry of Textile, Central Silk Board, Bangalore) pp 73-
78.
property of sericin. Sericin gels with pluronic and
3 Lesile M, Stephen M & Robert S, Cotton and wool outlook,
carbopol, act as moisturizer by repairing natural Econ Res Service, USDA, CWS-0303, (11 April 2003) 1-15.
moisturizing factor (NMF) as well as prevent TEWL 4 Iizuka E, Silk (physicochemical properties), the polymeric
by preventing water loss from the skin. SEM has materials encyclopedia (CRC Press) 1996.
shown the decrease cracking and flaking as compare 5 Cook J G, Natural fibres of animal origin (Silk); Handbook
to dry skin and normal skin replicas. of textile fibres (Marrow publishing Co Ltd, England), 3rd
ed, 1964, pp 154-165.
Powder containing 5-30 per cent sericin with
6 Komatsu K, Silk (its formation, structure, character, and
average molecular weight 7,000-3,00,000 and 70-95 utilization), the polymeric materials encyclopedia, (CRC
per cent silk fibroin when applied as film shows Press) 1996.
antistaticity and moisture absorbability59. Sericin 7 Voegeli R, Meier J & Blust R, Sericin silk protein: unique
hydrolysate solution shows that dermatitis is structure and properties, Cosmet Toilet, 108 (1993) 101-108.
controlled60. Sweat and sebum absorbing type of 8 Magoshi J, Biospinning (silk fibre formation), the polymeric
cosmetics containing cellulose fibres impregnated materials encyclopedia (CRC Press) 1996.
9 Shaw J T B & Smith S G, Amino acid of silk sericin, Nature,
with fibroin dispersion and aqueous sericin solution
4278 (1951) 745.
are also reported61. Lotion containing 1 per cent w/w 10 Sprange K U, The Bombyx mori silk proteins:
sericin and 4 per cent w/w D-glucose shows characterization of large polypeptides, Biochemistry, 14(5)
moisturizing and conditioning effect62. Creams (1975) 925-931.
containing 0.001-30 per cent w/w of sericin have 11 Wang T, Wang J & Zhou J, γ- Ray study on the sericin
improved cleansing properties with less skin structure of cocoon silk, Fangzhi Xuebao, 6(3) (1985) 133-
134.
irritation63. Sericin powder in the form of sericin
12 Tsukada M, J Polym Sci: Polym Lett Ed, 18 (1980) 133-134.
hydrolysate coated talc, mica, titania, iron oxide, and 13 Ayub Z H, Arai M & Hirabayashi K, Biosci Biotechnol
nylon have been used to formulate foundation cream Biochem, 57 (11) (1993) 1910-1912.
and eyeliners64. The microcapsules or nanocapsules 14 Zhu L J, Yao J & Youlu L, Structural transformation of
consisting of polysiloxane gel, UV absorbent core sericin dissolved from cocoon layer in hot water, Zhejiang
and UV scattering agent, silicone treated mica, silicon Nongye Daxue Xuebao, 24(3) (1998) 268-272.
treated titanium dioxide, silicon treated iron oxides, 15 Huddar P H, A study of natural and synthetic compound with
reference to chemistry of formation of silk in silkworm, Ph D
squalene, glycerin trioctanoate, and talc have resulted Thesis, Submitted to University of Pune, India, 1985, 23-75.
in cosmetic foundation having a SPF value of 25.7. 16 Zhu L J, Arai M & Hirabayashi K, Sol-gel transition of
Sericin in sunscreen composition enhances the light sericin, (Fac Technol, Tokyo Univ Agirc, Japan) Nippon
screening effect of UV filter like triazines, and Sanshigaku Zasshi, 65(4) (1996) 270-274.
cinnamic acids ester65. 17 Kataoka K, The solubility of sericin in water (Seric Exp Stu,
Minist Agric For, Tokyo, Japan), Nippon Sanshigaku Zasshi,
Nail cosmetics, containing 0.02-20 per cent sericin 46(3) (1977) 227-230.
are reported to prevent nail from chapping, 18 Ishizaka H & Kakinoki H, Solubility of sericin from cocoons
brittleness, and imparting the inherent gross to nails66. of poor reliability. II Effect of addition of water soluble high
Hair and bath preparations, containing 0.02-2 per cent polymers and resin finishing agents to cocoon cooking feed
sericin and 0.01-1 per cent olive oil, fatty acid or their water on sericin solubility, Nippon Sanshigaku Zasshi, 49(1)
(1980) 18-22.
salts show reducing damage of hair surface by
19 Zhu L J, Arai M & Hirabayashi K, Relationship between
binding of sericin to hairs67. Sericin hydrolysates with adhesive properties and structure of sericin in cocoon
average molecular weight 300-3000 are used as filament, J Sericult Sci Jap, 64(5) (1995) 420-426.
conditioners for skin and hair68. Shampoo containing 20 Rassent J, The molecular weight of sericin, Biochem Biophys
sericin and pelarogenic acid of pH less than six are Acta, 147 (1967) 595-597.
useful for the care and cleaning of hairs69. 21 Tsubouchi K, Yamada H & Yoko T, Manufacture of high
molecular weight sericin by extraction, Jpn Kokai Tokkyo
Koho Jap 11092564 A2 (to Norin Suisansho Sanshi Konchu
References Nogyo Gijutsu Kenkyusho, Japan) 06 April 1999, Heisei, pp
1 Raje S S & Rekha V D, Man-made Text India, 41(6) (1998) 6; Chem Abstr, 130(22) (1999) 301746.
249-254.
328 J SCI IND RES VOL 63 APRIL 2004

22 Shelton E M & Johnson T B, Research on protein VII The 39 Yamada H, Fuwa N & Nomura M, Use of sericin as
preparation of the protein “sericin” from silk, J Am Chem antioxidants and tyrosinase inhibitors, Eur Pat Appl, EP
Soc, 47 (1925) 412-418. 841065 A2 (to Seiren Co Ltd Japan) 13 May 1998, pp 9;
23 Buadze E, Study of bentonites application possibility in Chem Abstr, 129(1) (1998) 8425.
boiling of fibrics from natural silk, Bull Georgian Acad Sci, 40 Kato N, Sato S, Yamanaka A, Yamada H, Fuwa N &
159 (1) (1999) 110-112. Nomura M, Silk protein sericin inhibit lipid peroxidation and
24 Padamwar M N & Pawar A P, Preparation and evaluation of tyrosinase activity, (Hiroshima Univ), Biosci Biotechnol
sericin gels containing choline salicylate, Indian Drugs, Biochem, 62(1) (1998) 145-147.
40(9) (2003) 526-531. 41 Yamaji M, Sericin for enhancement of the heat resistant
25 Iida Hiroshi, Softening method of raw silk by enzyme, Jpn DNA plymerase activity, Jpn Kokai Tokkyo Koho,
Kokai Tokkyo Koho Jap 11061547 A2 5 March 1999, Heisei, Jap10262659 A2 (to Somar Corp Japan) 6 October 1998,
P 4; Chem Abstr, 130(16) (1999) 210758. Heisei, P 3; Chem Abstr, 129(24) (1998) 312831.
26 Pak P K, A comparative study on the raw cocoons 42 Wu C, Tian B, Zhu D, Yan X, Cheng W, Xu G, Guo Y, Wu
degumming by soap and protease, Sumyu Konghak Hoeji, Y & Jia S, Wound protection film and its preparation
14(3) (1977) 94-98. method, Faming Zhuanli Shenqing Gongkai Shuomingshu
CN 1121836 (to Suzhou Silk Engineering College, China), 8
27 Krysteva M, Arsov A, Dobrev I & Konsulov D, Enzyme
May 1996, pp 7; Chem Abstr, 130 (1996) 100662.
removal of sericin from crude silk fibres, Proc Int Conf
43 Gapurova G N, Chemical and physicochemical properties of
Chem, Biotechnol Biol Act Nat Prod, 3(2) (1981) 150-154.
surgical sutures, (Turk Gos Med Inst, Ashkhzbad, USSR),
28 Hamaoka Y, Kobayashi T, Asata S, Yamazaki M & Zdravookhr Turkm, 27(7) (1983) 15-17.
Hayakawa K, Separation and recovery method of sericin, Jpn 44 Tsubouchi K, Wound covering material containing silk
Kokai Tokkyo Koho Jap 1131318 A2 (to Kyoto Prefecture, fibroin and silk sericin as the main components and process
Japan) 21 July 1999, Heisei, pp9; Chem Abstr, 130(25) for producing the same, PCT Int Appl WO 9857676 A1 (to
(1999) 339325. National Institute of Sericulture, Japan) 23 December, 1998,
29 Jun L, Yaw J, Li Y, Hirabayashi K & Arai M, Studies on pp 34; Chem Abstr, 130(4) (1999) 43418.
physical properties of sericin gel, Canye Kexe, 23(1) (1997) 45 Kurioka A, Application of silk proteins to new biomaterial
47-52. (Silk Sci Res Inst Tokyo, Japan), Zairyo Gijutsu, 16(5)
30 Hirabayashi K, Arai M & Zhu L J, Gelation of silk sericin (1998) 195-201.
(Tokyo Agric Technol Univ, Tokyo 184, Jpan) Nippon 46 Nakamura K, Sato R & Shioraki H, Sericin containing vinyl
sanshigaku, Zasshi, 58(1) (1989) 81-82. graft polymers Jpn Kokai Tokkyo Koho Jap 60233119 A2
31 Hu G & Zhu L J, Characteristics and structure of gel with (Kanagawa Prefecture Japan), 19 November 1985, Showa, P
fibroin and sericin, Gongxueyuan Xuebao, 14(3) (1997) 154- 4; Chem Abstr, 104(20) (1986) 169122.
158. 47 Wei D, Li G, Taw J, Liu Z & Xinmin Z, Graft
32 Zhu, L J, Hizahayashi K & Aari M, Gelation of sericin and copolymerization of styrene onto silk sericin, Gaofenzi
its structure and properties, Canye Kexue, 17(1) (1991) 33- Xuebao, 6 (1989) 740-749.
38. 48 Sasaki M, Yamada H & Kato N, Composition of silk protein,
33 Kewon H Y, Yeo J H, Lee K G, Lee Y W, Park Y H, Nahm J sericin elevates intestinal absorption of Zn, Fe, Mg, and Ca
H & Cho C S, Effect of poloxamer on the gelation of silk in rats, Nutr Res, 20(10) (2000) 1505-1511.
sericin, Macromol Rapid Commun, 21 (2000) 1302-1305. 49 Sasaki M, Yamada H & Kato N, A resistant protein sericin
34 Nakamura K & Koga Y, Sericin containing polymer improves atropine induced constipation in rats, Food Sci
hydrogels and their manufacturer, Jpn Kokai Tokkyo Koho Tech Res, 6(4) (2000) 280-283.
Jap 2001106794 A2 (to Mochida Shoko K K Japan) 17 April 50 Sasaki M, Kato N, Watanabe H & Yamada H, Silk protein
2001, P 5; Chem Abstr, 134(21) (2001) 296862. sericin suppresses colon carcinogenesis, Oncol Rep, 7(5)
35 Shiomi H, Yamada H & Nomura M, Surfactants, Jpn Kodai (2000) 1049-1052.
Tokkyo Koho Jap 11276876 A2 (to Seiren Co Ltd Jpn) 12 51 Kato N & Sasaki M, New physiological function of sericin
October 1999, Heisei, pp 6; Chem Abstr, 131(18) (1999) and its application for cosmetic and food, Fragrance J, 28(4)
245154. (2000) 28-33.
36 Yasushi N, Liquid crystal device using sericin as alignment 52 Kato N, Tomotake H & Sasaki M, Nutritional function of
film, Jpn Kokai Tokkyo Koho Jap 06018892 A2 (to Casio resistant protein (Fac Appl Biol Sci, Hiroshima Univ, Japan),
Computer Co Ltd Japan) 28 January 1994, Heisei, P 3; Chem Rinsho Eiyo, 97(7) (2000) 789-796.
Abstr, 121(12) (1994) 145577.
53 Minora N & Tsukada M, Oxygen permeable membranes, Jpn
37 Yasushi T, Antithrombotic agent and its production method, Kokai Tokkyo Koho Jap 02233128 A2 (to Agency of Ind Aci
Jpn Kokai Tokkyo Koho JAP 09227402 A2 (to Norin & Tech, Japan; Ministry of agriculture & forstry sericulture,
Suisansho Sanshi Konchu, Nagyo Gijitsu Kenkyusho, Japan) Japan) 14 September 1990, Heisei, P 3; Chem Abstr, 114(6)
2 September 1997, Heisei, pp 5; Chem Abstr, 127(16) (1997) (1991) 45871.
225274.
54 Msakazul Y, Akira M & Yuri O, Manufacture of membranes
38 Khudaiberdiev M A, Synthesis of co-polymer processing an from agar and/or compound containing agarose sericin, Jpn
anticoagulant action, Chem Nat Compd, 33(5) (1997) 603- Kokai Tokkyo Koho Jap 2001129371 A2 (to Ube Industries
604. Ltd Jpn) 15 May 2001, P 6; Chem Abstr, 134(23) (2001)
328343.
 PADAMWAR & PAWAR: SILK SERICIN AND ITS APPLICATIONS 329

55 Yamada H, Fuha Y, Yuri O, Obayashi M & Arashima T, 62 Yamada H, Yamazuki K & Nozaki K, Skin moisturizing and
Collagen formation promoters containing sericin or its conditioning cosmetics containing sericin and saccharides,
hydrolyzates and antiaging cosmetics, Jpn Kokai Tokkyo Jpn Kokai Tokkyo Koho Jap 2001064148 A2 (to Seiren Co
Koho, JP 10226653 A2 (to Noevirco Ltd, Seiran co Ltd, Ltd & Teikoku Seiyaku Co Ltd) 13 March 2001, P 6; Chem
Japan) 25 August 1998, Heisei, P 8; Chem Abstr, 129(14) Abstr, 134(16) (2001) 227100.
(1998) 179985. 63 Sakamoto K & Yamakishi K, Sericin containing cleaning
56 Ogawa, A & Yamada H, Antiaging cosmetic containing composition, Jpn Kokai Tokkyo Koho Jap 2000073090 A2
sericin or hydrolysates and saccharomyces extracts, Jpn (to Seiren Co Ltd, Japan) 7 March 2000, P 4; Chem Abstr,
Kokai Tokkyo Koho Jap 11193210 A2 (to Noevier Co Ltd, 132 (2000) 196164.
Seiren Co Ltd Japan) 21 July 1999, Heisei, P 9; Chem Abstr, 64 Yamada H & Yuri O, Sericin coated powders for cosmetics,
131(7) (1999) 923508. Jpn Kokai Tokkyo Koho Jap 10226626 A2 (to Noevir Co
57 Henne W & Hoppe U, Light and screening composition, Ger Ltd, Seiren Co Ltd, Japan) 25 August 1998, Heisei, P 9;
Offen DE 3408406 A1 (to Beiersdrof A G Fed Rep Ger) 12 Chem Abstr, 129(16) (1998) 207009.
September 1985, P 14; Chem Abstr, 104(6) (1986) 39519. 65 Yoshioka M, Segawa A, Veda A & Omi S, UV absorbing
58 Padamwar M N, Daithankar A V, Pisal S S & Pawar A P, compositions containing fine capsules, Jpn Kokai Tokkyo
Evaluation of moisturizing efficiency of silk protein II: silk Koho Jap2001049233 A2 (to Seiwa Kasei K K Japan) 20
sericin, presented in sixty second World Cong of FIP, Nice February 2001, P 14; Chem Abstr, 134(14) 197870.
(France) (31st August-5th September 2002). 66 Yamada H, Yamasaki K & Zozaki K, Nail cosmetics
59 Kirikawa M, Kasaharu T, Kishida K & Akiyama D, Silk containing sericin, PCT Int Appl WO 2001015660 A1 (to
protein micropowders for coating with excellent feeling, Teikoku Seiyaku Co Ltd Seiren Co Ltd Japan) 8 March
antistaticity and moisture absorbability and releasability and 2001, P 15; Chem Abstr, 134(14) (2001) 197888.
there manufacture, Jpn Kokai Tokkyo Koho Jap 2000044598 67 Hoppe U, Koerbaecher K & Roeckl M, Hair and bath
A2 (to Daiwa Spinning Co Ltd, Nippon Ind Ltd, Japan) 15 preparations containing sericin, Ger Offen DE 3233388
February 2000, P 8; Chem Abstr, 132 (2000) 153320. A1(to Beiersdorf A G, Ger) 15 March 1984, P 15; Chem
60 Yasuda N, Yamada H & Nomura M, Sericin from silk as Abstr, 100 (1984) 215305.
dermatitis inhibitor Jpn Kokai Tokkyo Koho Jap 10245345 68 Hata O, Cosmetics containing sericin hydrolysates, Jpn
A2 (to Seiran Co Ltd, Japan) 14 September 1998, Heisei, P Kokai Tokkyo Koho Jap 62036308 A2 (to Kishu Sangyo K K
4; Chem Abst, 129(16) (1998) 207197. Japan) 17 February 1987, Showa, P 7; Chem Abstr, 106(26)
61 Miyashita T, Sweat and sebum absorbing cosmetics (1987) 219374.
containing cellulose fibres, Jpn Kokai Tokkyo Koho, Jap 69 Engel W & Hoppe U, Aqueous hair preparations containing
11152206 A2 (to Hsan Sangyo K K Japan) 8 June 1999, sericin and pelarogenic acids, Ger Offen DE 3603595 A1 (to
Heisei, P 3; Chem Abstr, 131(2) (1999) 23271. Beiersdorf A G, Ger) 13 August 1987, P 4; Chem Abstr,
108(16) (1988) 137689.

View publication stats