Silk fibre Technology

Introduction
Most historians agree that silk and sericulture, the cultivation of silkworms, had their origin in China nearly
2500 BC when the Empress Si-Ling-Chi, a queen of the famous Emperor Huang-Ti, learned how to rear the
silkworms and unwind their cocoons to produce fine filament fibres. After finding this knowledge, China
kept it as a secret and held a monopoly in the silk industry for nearly 4,000 years. After this period,
sericulture spread to Korea and Japan and it also spread around the world.

Silk, called the 'Queen of fibres', is a continuous protein fibre produced by the silkworm so as to form its
cocoon. The silk fibre is also produced by some spiders belonging to the Arachnida family. Unlike the
silkworms' fibre, the spiders' fibre cannot be commercially produced, and therefore, the silk fibre referred to
present days is the best fibre coming from the silkworm.

There are two main types of the silkworms: mulberry silk (Bombyx mori), also called 'cultivated silk', and
'wild silk' of which Tussah silk is the most important representative. Mulberry silk is produced by silkworm
larvae cultivated in provided habitats and fed with fleshy picked mulberry leaves.
Cultivated silk is different from Tussah silk. Cultivated silks are fine, almost white (when degummed) and
soft filaments with lustre. Nearly 80-85 % of the world silk production consists of cultivated silks.
 Silk fibre Technology

Mulberry silkworms
Mulberry silkworms can be divided into three groups:
1. Univoltine (one generation per year)
Univoltine breed is usually found in Europe. Because of the cold climate, the eggs are dormant in
winter and they are hatched only in spring. Therefore, they generate the silkworms once a year.
2. Bivoltine (two generations per year)
Bivoltine breed is normally found in Japan, Chain and Korea. The life cycle of the breed starts twice
within the same year because the climate is suitable for developing two life cycles per year.
3. Polyvoltine (up to eight generations per year)
Polyvoltine breed is customarily found in tropical zone. After eggs are laid by female butterflies, the
eggs will be hatched after between nine and twelve days.
The major groups of silkworms are univoltine and bivoltine breeds. The hybrid silkworm is a cross between
two or more pure breeds. The progeny will be a new breed of silkworm combining the good characteristics of
the parents and generating a strong silkworm because of the hybrid vigour. The hybrid silkworm tends to grow
up very fast and gives better filament quality than its parents.

In entomology, silk is grouped in the phylum Arthropoda which has a complete metamorphosis. Generally,
Bombyx mori is represented an entomological classification of mulberry silkworms.
 Silk fibre Technology

Life cycle of the silkworm

Metamorphosis of silkworm has four stages as follows:
1. Stage I (eggs), which develop into caterpillars or silkworms.
2. Stage II (larvae), which spin the filament fibre to make their cocoons for
protection and metamorphosis into the pupae.
3. Stage III (pupae), which emerge from the cocoons as moths (butterflies).
4. Stage IV (moths), of which the male and female moths breed and the female
moth lays eggs and the eggs will continue the next life cycle (Figure).
 Silk fibre Technology
Life cycle of the
silkworm
Metamorphosis of
silkworm has four
stages as follows:
1. Stage I (eggs),
which develop into
caterpillars or
silkworms.
2. Stage II (larvae),
which spin the
filament fibre to
make their cocoons
for protection and
metamorphosis into
the pupae.
3. Stage III (pupae),
which emerge from
the cocoons as moths
(butterflies).
4. Stage IV (moths),
of which the male Figure: Life cycle of the silkworm
Sericulture
 Silk fibre Technology
Structure of the silk fibre
The mature silkworm builds its cocoon by extruding a viscous fluid from two
large glands in the body of the silkworm. This solution is extruded through
two ducts in the head of the silkworm into a common spinneret. The viscous
part (fibroin) is covered by another secretion (sericin) which flows from two
other symmetrically placed glands. These two components are cemented
together by emerging into the air, coagulating and producing a firm
continuous filament.
As a consequence of this spinning process, the fibre has two main parts called
sericin and fibroin. Sericin, called silk gum, is a minor component of the
fibre (i.e. 25 % of the weight of raw silk) and it also has some impurities such
as waxes, fats and pigments. Sericin is a yellow, brittle and inelastic
substance. It acts as an adhesive for the twin fibroin filaments and conceals
the unique lustre of fibroin. Sericin is known as an amorphous structure and it
is dissolved in a hot soap solution. Sericin may be separated into sericin I, II,
III, and IV by using their different solubilities in hot water and assessing the
degree of solubility by UV adsorption. The greatest sericin content is present
in the outer layer of a cocoon whereas the least sericin proportion is present in
the innermost layer of a cocoon.

Figure: Structure of the raw silk fibre

 Silk fibre Technology
Structure of the silk fibre
Fibroin is the principal water insoluble protein (i.e. 78 % of the
weight of raw silk). Fibroin has a highly oriented and crystalline
structure.
Microfibrils are packed together to form the fibril bundle and several
fibril bundles produce a single strand.
Fibroin has high proportions of alanine, glycine and serine. A small
amount of cysteine residues gives a very small amount of sulphur in
the fibre. Fibroin contains only a small amount of amino acids which
have acid side chains. The amount of basic side groups in fibroin is
relatively low. Because of this, the amounts of acid and alkali that can
be absorbed by silk are relatively lower than those absorbed by wool
(ca. 0.2 equivalent per kg of silk). The isoelectric point of silk fibre is
around pH 5. There is a low proportion of amino acid residues with
large side chains in silk. Hydrogen bonding is important in fibroin. X-
ray structural analyses of the crystalline domains of fibroin show that
the peptide chains pack in fully extended forms.

Figure: Structure of the raw silk fibre

Structure of the silk fibre

Figure : Microscopic images of a silk fibre showing the two filaments of fibroin and their sericin coating
Silk – Fibroin and
Sericin

Figure 8 – Microscopic images of a silk fibre showing the two filaments of fibroin and their sericin coating

[Link]
 Silk fibre Technology
Structure of the silk fibre

Figure: Crystalline structure of the polypeptide chains in silk fibroin .

(Where ---- represents hydrogen bonding)
 Silk fibre Technology
Structure of the silk fibre

Figure: Sericin structure

Fibroin
Three crystalline phases can be identified in fibroin:
phase I: comprises 60% of the molecule and is characterized by a
highly crystalline structure made up primarily of glycine, alanine,
serine and tyrosine;
•phase II: comprises approximately 30% of the molecule and is made
up primarily of glycine, alanine, tyrosine and valine;
•phase III: comprises the amorphous part of the molecule and is
characterized primarily by amino acids with bulky or ionic side
Figure: Primary fibroin structure groups. These zones are responsible for giving silk its elasticity.
Amino acids with bulky side groups facilitate the movement of fibres.
GLYCINE (non-essential amino acid) – helps trigger the release of oxygen required for the cell-making process; important in the production of hormones responsible for a strong immune system.
ALANINE (non-essential amino acid) – is an important source of energy for muscle tissue, the brain and central nervous system; strengthens the immune system by producing antibodies; helps in the
metabolism of sugars and organic acids.
SERINE (non-essential amino acid) – stores glucose in the liver and muscles; strengthens the immune system by producing antibodies; synthesizes the fatty acid sheath that covers nerve fibres.
ASPARTIC ACID (non-essential amino acid) – helps remove harmful ammonia compounds from the body. When ammonia enters the circulatory system, it acts as a highly toxic substance that is harmful
to the central nervous system. Recent studies have demonstrated that aspartic acid can increase resistance to fatigue and enhance stamina.
GLUTAMIC ACID (non-essential amino acid) – considered to be a natural “brain food” that improves mental capacities; helps speed the healing of ulcers; reduces fatigue; helps control alcoholism,
schizophrenia and sugar cravings.
VALINE (essential amino acid) – promotes mental vigour, muscle coordination and relaxation.
PROLINE (non-essential amino acid) – is extremely important for the proper functioning of joints and tendons; helps maintain and strengthen heart muscles.
THREONINE (essential amino acid) – is an important constituent of collagen, elastin, and enamel protein; prevents fat accumulation in the liver; aids digestion and improves intestinal tract function;
assists in metabolism and assimilation.
LYSINE (essential amino acid) – ensures the adequate absorption of calcium; helps form collagen (which makes up bone cartilage and connective tissues); aids in the production of antibodies, hormones
and enzymes. Recent studies have shown that lysine may be effective against herpes by improving the balance of nutrients that reduce viral growth. A deficiency can cause tiredness, impaired
concentration, irritability, bloodshot eyes, retarded growth, hair loss, anaemia and reproductive problems.
ARGININA (non-essential amino acid) – studies have shown that it improves immune responses to bacteria, viruses and tumour cells; promotes wound healing and regeneration of the liver; causes the
release of growth hormones; considered crucial for optimal muscle growth and tissue repair.
TYROSINE (non-essential amino acid) – transmits nerve impulses to the brain; aids in recovery from depression; improves memory; increases mental alertness; promotes healthy functioning of the
thyroid, adrenal and pituitary glands.
PHENYLALANINE (essential amino acid) – used by the brain to produce noradrenaline, a chemical that transmits signals between nerve cells and the brain; keeps people awake and alert; reduces hunger
pains; functions as an antidepressant and helps improve memory.
LEUCINE AND ISO-LEUCINE (essential amino acid) – provide ingredients to produce other essential biochemical components in the body, some of which are used for energy production; stimulants for
the upper brain that enhance alertness.
METHIONINE (essential amino acid) – principle supplier of sulphur which prevents disorders of the hair, skin and nails; helps lower cholesterol levels by increasing the liver’s production of lecithin;
reduces liver fat and protects the kidneys; a natural chelating agent for heavy metals; regulates ammonia production and creates ammoniafree urine, which reduces bladder irritation; influences the
formation of hair follicles and promotes hair growth.
CYSTINE (non-essential amino acid) – functions as an antioxidant and is a potent aid in protecting the body against radiation and pollution. It can slow the aging process, deactivate free radicals,
neutralize toxins, aid in protein synthesis, and ensure cell renewal. Essential in the formation of skin, it helps in recovery from burns and surgery. Comprises 10-14% of hair and skin.
TRYPTOPHAN (essential amino acid) – a natural relaxant, it helps relieve insomnia by inducing normal sleep; reduces anxiety and depression; helps in the treatment of migraines; helps the immune
system; helps reduce the risk of arterial and cardiac spasms; together with LYSINE reduces cholesterol levels.
TAURINE (essential amino acid) – helps stabilize membrane excitability, an important factor in the control of epileptic seizures. TAURINE and SULPHUR are considered necessary factors for the control of
countless biochemical modifications that occur in the aging process; helps eliminate waste from free radicals.
HISTIDINE (non-essential amino acid) – is found abundantly in haemoglobin; used in the treatment of rheumatoid arthritis, allergenic diseases, ulcers and anaemia. A deficiency can cause hearing
problems.
Tables 1.1 and 1.2 show that there are different proportions of amino acid residues in fibroin and sericin.
 Silk fibre Technology
Physical properties of silk
Microscopy of the silk fibre Figure shows
that the cross-section of raw silk is roughly
elliptical. It shows the triangular twin
fibroin filaments, completely covered by
sericin, which normally face each other.
After the degumming process, the two
triangular fibroin filaments (brins) separate
into
individual filaments giving different fibre
geometry from the raw silk (i.e. a finer
fibre and a
more lustrous fibre).

Shape and appearance

Silk filaments are approximately 900 -
1700 metres long. The diameter of the silk
filament is from 9 to 11 microns. A raw
cultivated silk is off-white to yellow in
colour. Figure: Cross section, longitudinal view and perspective of silk filaments
Unlike cultivated silks, wild silks are
uneven, brown and slightly less lustrous
 Silk fibre Technology
Physical properties of silk
Microscopy of the silk fibre Figure shows that the cross-section of raw silk is roughly elliptical. It shows
the triangular twin fibroin filaments, completely covered by sericin, which normally face each other.
After the degumming process, the two triangular fibroin filaments (brins) separate into individual
filaments giving different fibre geometry from the raw silk (i.e. a finer fibre and a more lustrous fibre).

Shape and appearance

Silk filaments are approximately 900 - 1700 metres long. The diameter of the silkfilament is from 9 to 11
microns. A raw cultivated silk is off-white to yellow in colour. Unlike cultivated silks, wild silks are
uneven, brown and slightly less lustrous than those from cultivated silks.

Fibroin consists of non-crystalline and crystalline regions. The crystalline region tends to be oriented
along the fibre axis because the fibre is drawn as it is extruded from the spinnerets of the silkworm.

Hygroscopic nature
The conventional moisture region of silk is about 11.0 % compared with the mercerised cotton fibre
which has conventional moisture regain 10.5 %. The amount of moisture absorbed by silk is dependent
on its previous history such as whether it is raw or degummed silk, on the species of silk as well as on the
atmospheric humidity.
 Silk fibre Technology
Tensile properties
Silk fibre is extremely strong. A filament of silk is stronger than an equal diameter filament of
steel. Normally, the dry silk fibre has a tenacity varying from 2.4 to 5.1 grams per denier. The wet
strength of the fibre is about 80-85 % of the dry strength.

Elongation
Elongation at break of silk filaments is around 20-25 % under normal conditions. The extension
at break is 33 % at 100 % RH.

Specific gravity
Specific gravity of raw cultivated silk and raw tussah silk are 1.33 and 1.32 [Link] -3 respectively.
On the other hand, weighted silk has specific gravity more than 1.60 [Link] -3.

Effect of heat
Silk fibre heated at 140°C remains unaffected for a long period of time but it is decomposed very
quickly at 175 °C or more.

Effect of UV radiation
The strength and elongation of silk fibroin fibres were decreased when the fibres were exposed to
the UV radiation. The degree of the crystallinity was not affected by the radiation treatment.
 Silk fibre Technology
Chemical properties
Effect of water
Silk is not dissolved by water at room temperature but silk may lose weight in boiling water or steam at 100 °C.

Effect of acids and alkalis

Acids and alkalis cause hydrolysis of the polypeptide chains in the fibre. It has been claimed that pH values between 4
and 8 cause the least damage to the fibre. Acid hydrolysis tends to be more damaging to fibre than alkaline hydrolysis.
Acid hydrolysis occurs at nearly all the peptide linkages in the chain while alkali hydrolysis firstly attacks at the end of
the peptide chains. Concentrated sulphuric acid and hydrochloric acid will dissolve the fibre; nitric acid colours silk
yellow. Dilute acids do not attack the fibre under mild conditions. Strong hot caustic alkalis will readily dissolve the
fibre. Weak alkalis such as soap, borax and ammonia normally dissolve sericin but they also attack fibroin when the
treatment time at boiling point is prolonged.

Effect of organic solvents

The commonly used dry cleaning solvents do not dissolve the fibre.

Effect of oxidizing agents

Oxidation reactions are very complex and are considered to take place at the side chains of tyrosine, the amino terminal
residues of the main chains and at the peptide bonds. Fibroin is highly vulnerable to oxidizing agents. Therefore, care
must be taken when bleaching the fibre. Hydrogen peroxide and some peracids are normally used in the bleaching
process of raw silk. It has been found that peracetic acid causes a more destructive effect with fibroin than hydrogen
peroxide does.
 Silk fibre Technology
Chemical properties

Effect of reducing agents

It is known that fibroin resists the reducing agents such as hydrosulphite, sulphurous acid and its salts.
 Silk fibre Technology

Silk production
One of the first operations in silk production is a reeling process. Before
being reeled, the cocoons must be sorted carefully for size, quality and
defects. The cocoons are immersed into a hot water bath, which softens the
sericin holding the filaments together. The pupae in fresh cocoons are
killed at this stage. The filament ends can be found on the surface of
cocoons, unwound and twisted from several cocoons (e.g. seven to eight
cocoons) in order to make a raw silk multi filament yarn between 20 and
25 denier (the weight in g of 9000 m). Moreover, this process also gets rid
of a certain small amount of sericin in the fibre. Frequently, the filaments
are accumulated further by a process called as throwing, the process of
producing twisted silk yarn from reeled silk. Hence it produces `thrown
silk’ which is a suitable twisted yarn for producing a specific fabric by
knitting or weaving.
 Silk fibre Technology
Degumming silk
Derived from French word Degommage, degumming is at the heart of wet processing of raw silk due to the fact that
the raw silk contains the two components fibroin, and sericin which covers the filaments. Sericin contains some
impurities, for example, waxes, fats, mineral salts and pigments. Sericin has the same amino acid residues as fibroin
but the proportions contained in both components are quite different. As a result of this, the degumming process must
be carefully carried out on silk in the appropriate conditions otherwise the fibroin may be damaged. The pH range
from 4 to 8 is normally safe for fibroin. It has been found that alkaline conditions are less harmful to fibroin than acid
conditions. In contrast to fibroin, the solubility of sericin is very high at pH values between 1.5 and 2 and between
9.5 and 10.5. The main purposes of the degumming process are to remove the sericin from the fibre, to remove some
impurities (e.g. waxes, fats, mineral salts) affecting both the dyeing and printing processes, to make the fibre highly
absorbent for dyes and chemicals, and to reveal the lustre of fibroin and to improve the appearance of the fibre. The
sericin is removed from the fibre but the fibroin must not be damaged at the same time.
The degumming processes are classified into five methods as follows:

Degumming with water under pressure at 115°C

Water at room temperature does not dissolve silk but silk is highly susceptible to dissolution in boiling water. For this
reason, this process gives a risk of the fibroin being damaged when the time of treatment is prolonged. This process
needs large autoclaves to treat the fibre in the silk industry. A further disadvantage is that this process gives
incomplete degumming and sometimes soap or synthetic detergent must be added to improve the degumming effect.
Therefore, this process is very difficult to control and now it is not used in the silk industry.
Question: What do know about degumming of silk? Mention some processes for
degumming of silk. Describe anyone of them. 6
Question: Describe degumming of silk fibres with enzyme. 6
 Silk fibre Technology
Degumming with soap (ca. 98 °C )
Marseilles soap, an olive oil soap, is an outstanding soap for degumming. For example, this process may be
carried out using 10-20 g/l soap at 92-98 °C for 2-4 hours adjusted pH to 10.2-10.5 in order to react effectively
upon the sericin. As a result of the high temperature, this process tends to attack both sericin and fibroin because
of the sensitive nature of fibroin itself and the chemical similarity of fibroin and sericin. Moreover, the most
important requirement of the process is a soft water to avoid the formation of a calcium soap.

Degumming with synthetic detergent (ca. 98 °C )

Synthetic detergents play a crucial role in this process because they have some advantages over soap such as
reducing the time of treatment (e.g. 30-40 min at 98 °C ) and damaging the fibre less. Non-ionic synthetic
detergent aided the removal of sericin without affecting the tensile strength of the fibre. The degumming process
using 2.5 g/l non-ionic synthetic detergent at pH 11.5 for 30 minutes gave a most efficient degumming effect.
However, the problem of this process is that it is carried out at high temperature (e.g. at 98 °C ) and high pH (e.g.
at pH 11.5). Therefore, the temperature, the time of treatment and the amount of detergent used must be properly
controlled to avoid damage to the fibroin.

Degumming with acid (ca. 98 °C )

Some acids such as sulphuric, hydrochloric, tartaric and citric acids can be used as degumming agents. This
process has not received much attention in the silk industry because of the idea that degumming in alkaline
solution is safer for fibroin than in acid solution. It has been found that the complete degumming of silk with
strong mineral acids (e.g. sulphuric and hydrochloric acids) cannot be achieved without harm to the fibroin.
 Silk fibre Technology
Degumming with enzymes
Enzymes are proteins, catalysing a specific chemical reaction, which are known as 'bio-catalysts'. Generally,
enzymes appear in living cells. Therefore, they work at atmospheric pressure and in mild conditions (e.g. at 40
°C, pH 8.0). Different enzymes may cause hydrolysis, reduction, oxidation, coagulation and decomposition
reactions. Hydrolytic enzymes are commonly used in the textile industry: e.g. cellulase, trypsin and papain.
Some properties of enzymes are as follows :
1. enzymes are complex and high molecular weight protein molecules,
2. enzymes are susceptible to high temperatures and pH values outside their
optimum ranges because they can be denatured,
3. enzymes react at specific parts of the substrate molecule depending on their
active sites and types, and
4. enzyme reactions are reversible reactions.
e.g. A + B C

In order to react with substrate as a catalyst, enzyme has an active site and the substrate molecule fits the active
site like a key fitting into a lock forming an enzyme-substrate complex. The enzyme-substrate complex then
releases an end product and a regenerated enzyme molecule. The regenerated enzyme will then generate a new
cycle.
Degumming with enzymes

In order to react with substrate as a Enzyme reactions

catalyst, enzyme has an active site The 'Lock-key theory' simply explains enzyme reactions
and the substrate molecule fits the
active site like a key fitting into a
lock forming an enzyme-substrate
complex. The enzyme-substrate
complex then releases an end product
and a regenerated enzyme molecule.
The regenerated enzyme will then
generate a new cycle.
1. Enzyme
2. Substrate molecule
3. Enzyme-substrate complex
4. End products

Figure Nature of an enzyme reaction

Enzymes for degumming
Trypsin, papain and bacterial enzymes are the main
types of enzymes for silk degumming. These enzymes
are called 'proteases' because they degrade proteins and
their degradation products are polypeptides, peptides
and other substances by hydrolysis of the - CO-NH-
linkage. The proteolytic enzyme action is shown in the
Figure.
Figure: Proteolytic enzyme action on protein
Trypsin
Secreted from the pancreas, trypsin is a serine protease
which is most active in the pH range between 7 and 9
at 37 °C . It reacts with peptide bonds between the
carboxylic acid group of lysine or arginine and the
amino group of the adjacent amino acid residue.
Sericin may be less crystalline than fibroin, and it has
relatively high lysine and arginine contents. Fibroin
may be less affected by trypsin due to its lower
proportion of lysine and arginine residues
Figure: Specific site of protein hydrolysis by trypsin
Papain
Papain enzyme, derived from papyrus latex, is a sulphydryl enzyme which is
most active in the range of the pH between 5.0 and 7.5 at 70-90 oC. Before the degumming
process, papain must be activated by a sulphydryl reagent. Activated papain attacks the
peptide bonds between the carboxylic acid group of lysine or arginine and the adjacent amino
acid residue. Minor cleavage occurs at the carboxylic acid group of histidine and also of
glycine, glutamic acid, glutamine, leucine and tyrosine residues [37].
Bacterial enzymes
A bacterial enzyme, alkalase, produced by Novo [50, 53], has been found to be
effective in hydrolysing sericin. This bacterial enzyme was claimed to be more effective than
trypsin and papain in that it will completely decompose sericin in 1 h at 60oC, pH 9.0 [37].
Other alkaline-stable proteases have been found suitable for silk degumming
such as degummase, esperase, proteinase and sauinase [37, 53].
Enzyme degumming has the following advantages over the conventional
degumming with alkaline soap: [53]
1. it has a specific reaction thereby it may give a minimum damage to fibroin,
2. it has a lesser risk of over degumming than alkaline soap degumming,
3. weight loss can be easily modified by adjusting the concentration of enzyme,
the reaction time and the use of optimum pH and temperature,
4. with the enzyme method, silk is treated at low temperature (e.g. at 40oC) not
only reducing energy costs but also preventing fibre weakness,
5. enzyme treatment is an environmentally friendly process because enzyme
can be readily biodegradable in nature [54], and
6. there are no soap required in enzymatic degumming process,
therefore,
uneven dyeing problem caused by metallic soap can be avoided.
Enzymatic degumming also has some economic disadvantages
as:
1. it need some pre-treatment processes, since the gum must be
swollen before
the enzyme bath [43,55], and
2. it is a very slow reaction compared to alkaline soap
degumming [43], on the
other hand, enzymatic degumming may give a better
degumming result because it can be well
controlled compared with alkaline soap degumming. Therefore,
fibroin may be intact.
9.4 Finishing
1. Weighting [72, 73]
The degumming process causes a weight loss on silk (e.g. 20-25 %).
Weighting process is sometimes used to increase the weight of silk. Silk is treated with a
suitable organic or inorganic substance in order to increase the weight. The weighting process
improves the drapability of silk, which is a highly appreciated property in the case of dress and
garment fabrics.
2. Mechanical finishing [74]
Silk fabrics can be calendered using a two-bowl calendering machine so as to
improve handle and appearance.
3. Softeners and lubricants [75]
With the presence of softeners and lubricants, silk enhances its unusual
properties. Generally, softener is used in the final stage of wet processing of silk.
4. Flame-retardants [75]
Flame-retardants are used on silk fabric to inhibit pyrolysis reactions. Some
flame-retardants are alkyl and aryl phosphates, phosphonates, poly (vinyl or vinylidene
halides) latexes, poly (halogenated acrylate) latexes, colloidal antimony pentoxide and so on.
5. Crease-recovery finishes [23, 55, 75]
Easy-care properties of silk are not high compared to synthetic fibres.
Therefore, cross-linking agents are used for this purpose. These products either react with one
another or crosslink the fibroin backbone to form water insoluble products under the action of
a suitable catalyst and heat.
6. Oil and water repellent finishes
Oil and water repellent finishes are applied together or separately on silk.
Conventional auxiliaries are waxes, metal acid salt and oxides, proteins and nitrogenous