Different kinds of enzyme on textile substrates

MD.AZMERI LATIF BEG MSc Engr(Textile)
THE PROJECT & THESIS
ON
APPLICATION OF DIFFERENT KINDS OF ENZYME
ON TEXTILE SUBSTRATES.
MD.AZMERI LATIF BEG
M. Sc in Textile Engineering
Specialized in Apparel Manufacturing,
Processing and Designing
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INDEX
Sl No. Topics Page no.
01 Table of content 03
02 Acknowledgement 05
03 Abstract 06
04 Chapter 01- Introductory part of the project & thesis 07
05
1.1. Introduction
1.2. 08
06 1.2 Objectives 10
07 1.3 Typical applications of enzymes 10
08 Chapter 02- Literature review 11
09 2.1 What are enzymes ? 12
10 2.1.1 Enzymes are proteins and biocatalyst 12
11 2.1.2 Enzymes are specific and work in mild conditions 13
12 2.1.3 Enzymes are part of a sustainable environment 14
13 2.1.4 Enzymes and industrial applications 14
14 2.2 History of Enzymes 14
15 2.3 Nature of Enzymes 15
16 2.3.1 Enzymes are miracles of nature 16
17 2.4 How is Enzymes made ? 16
18 2.5 Enzymes for textiles 17
19 2.5.1 Desizing 18
20 2.5.2 Bio-polishing 19
21 2.5.3 Denim finishing 19
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22 2.5.4 Bleach clean-up 20
23 2.5.5 Bio-scouring 20
24 2.6 Enzymes composition 21
25 2.7 Enzyme classification 22
26 2.8 How Enzyme work? 23
27 2.8.1 Amino acid, Proteins and Bio-chemistry 23
28 2.8.2 Catalysts 23
29 2.9 Industrial application 24
30 2.10 Enzyme characteristics 2
31 2.11 Conditions for Enzyme activity 25
32
2.12 Some representative enzymes, there sources and reaction
specificities
26
33 2.13 Factors affecting enzyme activity 27
34 2.13.1 Enzyme concentration 27
35 2.13.2 Substrate concentration 29
36 2.13.3 Effects of inhibitors on enzyme activity 31
37 2.13.4 Temperature effects 34
38 2.13.5 Effects of Ph 35
39 Chapter- 03: Methodology 37
40 3.1 Materials 38
41 3.2 Method 39
42 Chapter- 04: Results & discussion 48
43 4.1 Result 49
44 4.2 Discussion 52
45 Chapter- 05: Conclusion 54
46 Chapter- 06: Reference 56
47 Appendix 58
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ABSTRACT
Enzymes are proteins with highly specialized catalytic functions, produced by all
living organisms. Enzymes are responsible for many essential biochemical reactions
in microorganisms, plants, animals, and human beings. Enzymes are essential for all
metabolic processes, but are not alive. Although like all other proteins, enzymes are
composed of amino acids, they differ in function in that they have the unique ability
to facilitate biochemical reactions without undergoing change themselves. This
catalytic capability is what makes enzymes unique. Enzymes are natural protein
molecules that act as highly efficient catalysts in biochemical reactions, that is, they
help a chemical reaction take place quickly and efficiently. Enzymes not only work
efficiently and rapidly, they are also biodegradable. Enzymes are highly efficient in
increasing the reaction rate of biochemical processes that otherwise proceed very
slowly, or in some cases, not at all.
The textile industry has used enzymes to remove hairiness of fabric. The textile
industry has become familiar with the use of celluloses for stone-washing blue jeans,
and more recently for finishing of fabrics and garments made on cotton, linen and
other cellulose fibers. In the modern textile technology finishing process, employing
environmentally friendly, fully biodegradable enzymes can replace a number of
mechanical and chemical operations which have hitherto been applied to improve the
comfort and quality of textile materials.
Application of enzymes is getting higher in practical use in textile sector day by
day.We have to observe the overall use of enzymes in defferent sectors.thus it
importance will be more visible to the technical person and for the bettermeet of the
sector aas well.
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Chapter: 1
INTRODUCTORY PART OF THE PROJECT

Chapter-1
1.1 INTRODUCTION:
The textile industry has used enzymes to remove hairiness of fabric. The textile
industry has become familiar with the use of celluloses for stone-washing blue jeans,
and more recently for finishing of fabrics and garments made on cotton, linen and
other cellulose fibers. In the modern textile technology finishing process, employing
environmentally friendly, fully biodegradable enzymes can replace a number of
mechanical and chemical operations which have hitherto been applied to improve the
comfort and quality of textile materials. The expected technical advantages resulting
from the utilization of specified enzymes for fabric finishing are as follows:
 A cleaner fabric surface with less fuzz.
 A more even fabric surface appearance.
 A reduced tendency to pill formation.
 An improved hand.
 Unique softness when combined with traditional softeners.
 A more environmentally responsible means of treating textiles.
Enzymatic treatment of cotton fabric is a nontoxic, environmentally benign process,
which has gained wide recognition for various textile-processing applications such as
de-sizing, bleach cleanup, bio-stoning, and bio-polishing. Enzymes are specialized
biopolymers (proteins) composed of many different amino acids that have complex
three-dimensional structures held in place by a variety of bonding forces. Enzymes act
as catalysts to speed up complex chemical reactions such as the hydrolysis of
cellulose, starches, and triglyceride based compounds in fats and oils. Because they
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act as catalysts, relatively small concentrations of enzymes are required. If the
conditions are favorable to the specific enzyme, the catalytic action (hydrolysis) will
be repeated many times in the same system. The application of enzymes in the textile
industry is becoming increasingly popular because of the mild conditions of
temperature and pH that are required and the capability of enzymes of replacing harsh
organic chemicals. The typical temperatures of processing during enzymatic treatment
are from about 40 to 50 °C, which offers a significant decrease in energy consumption
compared with the normal processing temperatures. Also important is that wastewater
from enzymatic treatments is readily biodegradable and, accordingly, does not pose
any environmental hazard. In addition to numerous advantages provided by the use of
enzymes for textile finishing, there are several shortcomings of enzymatic treatment
of cotton fabric, such as more expensive processing costs and a significant decrease in
fabric strength properties. Enzymatic treatments of the cotton fabrics, like any wet
processing of textiles, involve the transfer of mass from the processing liquid medium
(enzyme solution) across the surface of the textile substrate. As with all chemical
processes, these transport processes are time and temperature dependent, and
compromising either could affect productivity and/or product quality. Many of the
latest development studies on textile enzyme producers have been focused on
improving the characteristics of cellulose textile materials with cellulose preparations.
New enzyme products are still being developed for the finishing process of cellulose
materials based on cotton, linen, viscose, lyocel and their mixtures and blends with
synthetic fibers. The target of bio-finishing is to remove all impurities and individual
loose fiber ends that protrude from the fabric surface simultaneously in order to retain
the strength of fabric at an acceptable level.
At Maps, we continuously develop our product line in order to have innovative
enzymes with unique features for existing and new applications within the textile
industry. Our R&D aims to provide innovative products for fabric treatment reducing
process time, chemical consumption and energy costs in compliance with sustainable
development.
We provide a range of enzymes like amylases, cellulases, catalase, pectinase and
protease for various textile wet-processing applications like desizing, bio-polishing,
denim finishing, bleach clean-up, bio-scouring and de-wooling.
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1.2 OBJECTIVE
The major objective of this research is to establish a fundamental scheme for enzyme
process of knitted goods and other enzyme processes. This investigation was done
mainly-
1) To acquire knowledge about different enzymes.
2) To know the different application of enzymes.
3) To differentiate between enzyme application and other physical and
Chemical applications in same wet process.
4) To study the results obtained before and after enzyme treatment.
5) To know how to remove hairy fibers and fuzz from knit fabric surface.
6) To know effective use of enzyme.
1.3TYPICAL APPLICATIONS OF ENZYMES
 De-sizing.
: Removal of starch/size with amylases.
 Scouring.
: Dissolution/Dispersion of waxes.
 Bleach cleanup.
:Removal of residual hydrogen peroxide with catalases.
 Bio-polishing.
:Improvement of the appearance of cotton fabrics by removal of fuzz
fibers and pills from the surface with cellulases.
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 Bio-stoning : “Stone washing” of denim fabrics to produce the
fashionable aged appearance with celluloses.
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Chapter: 2
LITERATURE REVIEW

Chapter-2: Literature Review
2.1 WHAT ARE ENZYMES?
2.1.1 Enzymes are proteins and biocatalyst
Enzymes are proteins that participate in cellular metabolic processes with the ability
to enhance the rate of reaction between bio-molecules. Some enzymes can even
reverse a reaction from the direction it would normally take, by reducing the
activation energy (Ea) to the extent that the reaction favors’ the reverse direction.
Similarly, enzymes can catalyze reactions that might not otherwise occur, by lowering
the Ea to a more "affordable" level for the cell. Enzymes can be isolated using various
protein purification methods. The purity of an enzyme preparation is measured by
determining its specific activity. Enzymes, like other proteins, consist of long chains
of amino acids held together by peptide bonds. They are present in all living cells,
where they perform a vital function by controlling the metabolic processes, whereby
nutrients are converted into energy and new cells. Moreover, enzymes take part in the
breakdown of food materials into simpler compounds. As commonly known, enzymes
are found in the digestive tract where pepsin, trysin and peptidases break down
proteins into amino acids, lipases split fats into glycerol and fatty acids, and amylases
break down starch into simple sugars. Enzymes are biocatalyst, and by their mere
presence, and without being consumed in the process, enzymes can speed up chemical
processes that would otherwise run very slowly. After the reaction is complete, the
enzyme is released again, ready to start another reaction. In principle, this could go on
forever, but in practically most catalysts have a limited stability, and over a period of
time they lose, their activity and are not usable again. Generally, most enzymes are
used only once and discarded after; they have done their job. [1]
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Figure: schematic diagram of enzymes
2.1.2 Enzymes are specific and work in mild conditions
Enzymes are very specific in comparison to inorganic catalysts such as acids, bases,
metals and metal oxides. Enzyme can break down particular compounds. In some
cases, their action is limited to specific bonds in the compounds with which, they
react. The molecule(s) that an enzyme acts on is known as its substrate(s), which is
converted into a product or products. A part of large enzyme molecule will reversibly
bind to the substrate(s) and then a specialized part(s) of the enzyme will catalyze the
specific change necessary to change the substrate into a product. For each type of
reaction in a cell there is a different enzyme and they are classified into six broad
categories namely hydrolytic, oxidizing and reducing, synthesizing, transferring, lyric
and isomer sing. During industrial process, the specific action of enzymes allows high
yields to be obtained with a minimum of unwanted by-products. Enzymes can work at
atmospheric pressure and in mild conditions with respect to temperature and acidity
(pH). Most enzymes function optimally at a temperature of 30? C-70?C and at pH
values, which are near the neutral point (pH 7). Now-a-days, special enzymes have
been developed that work at higher temperatures for specific applications. Enzyme
processes are potentially energy saving and save investing in special equipment
resistant to heat, pressure or corrosion. Enzymes, due to their efficiency, specific
action, the mild conditions in which they work and their high biodegradability, they
are very well suited for a wide range of industrial applications. [1]
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2.1.3 Enzymes are part of a sustainable environment
As mentioned earlier, enzymes are present in all biological systems. They come from
natural systems, and when they are degraded the amino acids of which they are made
can be readily absorbed back into nature. Enzymes work only on renewable raw
materials. Fruit, cereals, milk, fats, meat, cotton, leather and wood are some typical
candidates for enzymatic conversion in industry. Both the usable products and the
waste of most enzymatic reactions are non-toxic and readily broken down. Finally,
industrial enzymes can be produced in an ecologically sound way where the waste
sludge is recycled as fertilizer. [1]
2.1.4 Enzymes and industrial applications
Industrial enzymes are originating from microorganisms in the soil. Microorganisms
are usually bacteria, fungi or yeast. One microorganism contains over 1,000 different
enzymes. A long period of trial and error in the laboratory is needed to isolate the best
microorganism for producing a particular type of enzyme. When the right
microorganism has been found, it has to be modified so that it is capable of producing
the desired enzyme at high yields. Then the microorganism is 'grown' in trays or huge
fermentation tanks where it produces the desired enzyme. With the latest
technological advancements of fermenting microorganisms, it possible to produce
enzymes economically and in virtually unlimited quantities. The end product of
fermentation is a broth from which the enzymes are extracted. After this, the
remaining fermentation broth is centrifuged or filtered to remove all solid particles.
The resulting biomass, or sludge in everyday language, contains the residues of
microorganisms and raw materials, which can be a very good natural fertilizer. The
enzymes are then, used for various industrial applications. [1]
2.2 HISTORY OF ENZYMES
The history of modern enzyme technology really began in 1874 when the Danish
chemist Christian Hansen produced the first specimen of rennet by extracting dried
calves' stomachs with saline solution. Apparently this was the first enzyme
preparation of relatively high purity used for industrial purposes. This significant
event had been preceded by a lengthy evolution.
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Enzymes have been used by man throughout the ages, either in the form of vegetables
rich in enzymes, or in the form of microorganisms used for a variety of purposes, for
instance in brewing processes, in baking, and in the production of alcohol. It is
generally known that enzymes were already used in the production of cheese since old
times. Even though the action of enzymes has been recognized and enzymes have
been used throughout history, it was quite recently that their importance was realized.
Enzymatic processes, particularly fermentation, were the focus of numerous studies in
the 19th century and many valuable discoveries in this field were made. A particularly
important experiment was the isolation of the enzyme complex from malt by Payen
and Persoz in 1833. This extract, like malt itself, converts gelatinized starch into
sugars, primarily into maltose, and was termed 'diastase'. Development progressed
during the following decades, particularly in the field of fermentation where the
achievements by Schwann, Liebig, Pasteur and Kuhne were of the greatest
importance. The dispute between Liebig and Pasteur concerning the fermentation
process caused much heated debate. Liebig claimed that fermentation resulted from
chemical process and that yeast was a nonviable substance continuously in the process
of breaking down. Pasteur, on the other hand, argued that fermentation did not occur
unless viable organisms were present. The dispute was finally settled in 1897, after
the death of both adversaries, when the Buchner brothers demonstrated that cell free
yeast extract could convert glucose into ethanol and carbon dioxide just like viable
yeast cells. In other words, the conversion was not ascribable to yeast cells as such,
but to their nonviable enzymes.In 1876, William Kuhne proposed that the name
'enzyme' be used as the new term to denote phenomena previously known as
'unorganised ferments', that is, ferments isolated from the viable organisms in which
they were formed. The word itself means 'in yeast' and is derived from the Greek 'en'
meaning 'in', and 'zyme' meaning 'yeast' or 'leaven'. [2]
2.3 NATURE OF ENZYMES
2.3.1 Enzymes are miracles of nature
Enzymes are large protein molecules, and like other proteins, they are made up of
long chains of amino acids. Enzymes are present in all living things, where they
perform the essential functions of converting food to energy and new cell material.
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Enzymes are bio-catalyst and can be used to speed up chemical processes or to make
reactions take place that otherwise would not.
Enzymes do this by binding to the starting material (substrate), catalysing the
reactions, and then releasing themselves from the products so that they can react
again. Although the enzyme is not consumed in the reaction, it does lose its activity
over time and so eventually needs to be replenished. Compared with other ways of
controlling chemical reactions enzymes are more specific, more efficient and work
under milder conditions. When enzymes are used in an industrial process, these
characteristics can often be used to achieve higher purity and better yields while
saving on energy.
Enzymes can be classified by the types of substrates they work on. Proteases works
on proteins, carbohydrates (amylases) work on carbohydrates, celluloses work on
cellulose and lipases work on lipids. They can also be classified by the types of
reactions they catalyzed. Hydrolases split molecules, synthetases join them and
tranferases move groups of atoms from one molecule to another. Over two thousand
different enzymes have been identified, and several hundreds are available
commercially, but so far only 25 are produced on an industrial scale. Some enzymes
are still derived from plants and animals, including papain from papayas and rennet
from calf stomachs. But the last 100 years, and especially since mid 1960s,
microorganisms have become the most important source of enzymes. Microorganisms
can be selected to produce almost any kind of enzyme in almost any quantity. [1]
2.4 HOW ARE ENZYMES MADE?
The starting point for enzyme production is a vial of a selected strain of
microorganisms. They will be nurtured and fed until they multiply many thousand
times. Then the desired end-product is recovered from the fermentation broth and sold
as a standardised product. A single bacteria or fungus is able to produce only a very
small portion of the enzyme, but billions microorganisms, however, can produce large
amounts of enzyme. The process of multiplying microorganisms by millions is called
fermentation. Fermentation to produce industrial enzymes starts with a vial of dried or
frozen microorganisms called a production strain. One very important aspect of
fermentation is sterilisation. In order to cultivate a particular production strain, it is
first necessary to eliminate all the native microorganisms present in the raw materials
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and equipment. If proper sterilisation is not done, other wild organisms will quickly
outnumber the production strain and no production will occur. The production strain
is first cultivated in a small flask containing nutrients. The flask is placed in an
incubator, which provides the optimal temperature for the microorganism cells to
germinate. Once the flask is ready, the cells are transferred to a seed fermenter, which
is a large tank containing previously sterilised raw materials and water known as the
medium. Seed fermentation allows the cells to reproduce and adapt to the
environment and nutrients that will be encountered later on.
After the seed fermentation, the cells are transferred to a larger tank, the main
fermenter, where fermentation time, temperature, pH and air are controlled to
optimise growth. When this fermentation is complete, the mixture of cells, nutrients
and enzymes, called the broth, is ready for filtration and purification. Filtration and
purification termed as downstream processing is done after enzyme fermentation. The
enzymes are extracted from the fermentation broth by various chemical treatments to
ensure efficient extraction, followed by removal of the broth using either
centrifugation or filtration. Followed by a series of other filtration processes, the
enzymes are finally separated from the water using an evaporation process.After this
the enzymes are formulated and standardised in form of powder, liquid or granules. [2]
2.5 ENZYMES FOR TEXTILE
Enzymes are used to provide innovative products for fabric treatment reducing
process time, chemical consumption and energy costs in compliance with sustainable
development. Enzymes like amylases, cellulases, catalase, pectinase and protease are
used for various textile wet-processing applications like desizing, bio-polishing,
denim finishing, bleach clean-up, bio-scouring and de-wooling. [3]
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2.5.1 Desizing
For fabrics made from cotton or blends, the warp threads are coated with an adhesive
substance know as 'size‘; to prevent the threads breaking during weaving. Although
many different compounds have been used to size fabrics, starch and its derivatives
have been the most common sizing agent. After weaving, the size must be removed
again in order to prepare the fabric for dyeing and finishing.
This process (de-sizing) must be carried out by treating the fabric with chemicals such
as acids, alkali or oxidising agents. However starchbreaking enzymes (amylases) are
preferred for desizing due to their high efficiency and specific action. Amylases bring
about complete removal of the size without any harmful effects on the fabric. Another
benefit of enzymes compared to strong chemicals mentioned above is that enzymes
are environment friendly.Maps offers a range of amylases for desizing which work at
different temperatures and for different equipments. [3]
Palkozyme Alpha amylase for low-medium temperature conventional
desizing.
Palkozyme Ultra Alpha amylase for low-medium temperature desizing
Palkozyme Plus Alpha amylase for high temperature desizing
Palkozyme HT Heat-stable alpha amylase for high temperature desizing
Palkozyme CLX Alpha amylase for low temperature desizing
2.5.2 Bio-Polishing
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Cotton and other natural fibers based on cellulose can be improved by an enzymatic
treatment known as Bio-Polishing. This treatment gives the fabric a smoother and
glossier appearance. The treatment is used to remove 'fuzz' - the tiny strands of fiber
that protrude from the surface of yarn. A ball of fuzz is called a 'pill' in the textile
trade. After Bio-Polishing, the fuzz and pilling are reduced. The other benefits of
removing fuzz are a softer and smoother handle, and superior color brightness. A
range of celluloses for bio-polishing which work on depending on fiber, fabric type
and equipments. [3]
Palkofeel Cellulase for bio-polishing cotton and blended fabric and garment
Palkofeel C Cellulase for bio-polishing cotton fabric and garments
Palkosoft Cellulase for bio-polishing cotton and blended fabric and garment
2.5.3 Denim Finishing
Many garments are subjected to a wash treatment to give them a slightly worn look;
example is the stonewashing of denim jeans. In the traditional stonewashing process,
the blue denim was faded by the abrasive action of pumice stones on the garment
surface. Nowadays, denim finishers are using a special cellulase. Cellulase works by
loosening the indigo dye on the denim in a process know as 'Bio-Stonewashing'. A
small dose of enzyme can replace several kilograms of pumice stones. The use of less
pumice stones results in less damage to garment, machine and less pumice dust in the
laundry environment. BioStonewashing has opened up new possibilities in denim
finishing by increasing the variety of finishes available. For example, it is now
possible to fade denim to a greater degree without running the risk of damaging the
garment. Productivity can also be increased because laundry machines contain fewer
stones or no stones and more garments. Maps offers a range of cellulases for denim
finishing, each with its own special properties. These can be used either alone or in
combination with pumice stones in order to obtain a specific look. [3]
Palkowash Cellulase for bio-stonewashing denims used in garment wet-processing
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Palkostone Cellulase for bio-stonewashing denims used in garment wet-processing
Palkocel Cellulase for bio-stonewashing denims used in garment wet-processing
2.5.4 Bleach Clean-up
Natural fabrics such as cotton are normally bleached with hydrogen peroxide before
dyeing. Bleaches are highly reactive chemicals and any peroxide left on the fabric can
interfere with the dyeing process. A thorough 'Bleach Cleanup' is necessary. The
traditional method is to neutralize the bleach with a reducing agent, but the dose has
to be controlled precisely. Enzymes present a more convenient alternative because
they are easier and quicker to use. A small dose of catalase is capable of breaking
down hydrogen peroxide into water and oxygen. Compared with the traditional clean-
up methods, the enzymatic process results in cleaner waste water or reduced water
consumption. Maps offer catalase for removing residual hydrogen peroxide after the
bleaching of cotton. It reduces the rinsing necessary to remove bleach or it can be
used to replace chemical treatments. [3]
Palkoperox Catalase for bleach clean-up i.e. removal residual hydrogen peroxide after the
bleaching of cotton.
2.5.5 Bio-Scouring
Cotton yarn or fabric, prior to dyeing or printing, goes through a number of processes
in a textile processing unit. A very important process is scouring. In this process, non-
cellulosic components from native cotton are completely or partially removed.
Scouring gives a fabric with a high and even wet ability so that it can be bleached and
dyed successfully. Today, highly alkaline chemicals caustic soda are used for
scouring. These chemicals not only remove the non-cellulosic impurities from the
cotton, but also attack the cellulose leading to heavy strength loss and weight loss in
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the fabric. Furthermore, using these hazardous chemicals result in high COD
(chemical oxygen demand), BOD (biological oxygen demand) and TDS, in the waste
water Recently a new enzymatic scouring process know as 'Bio-Scouring' is used in
textile wet-processing with which all non-cellulosic components from native cotton
are completely or partially removed. After this Bio-Scouring process, the cotton has
an intact cellulose structure, with lower weight loss and strength loss. The fabric gives
better wetting and penetration properties, making subsequent bleach process easy and
resultantly giving much better dye uptake. [3]
Palkoscour
Multi-component enzyme for bio-scouring i.e. complete or partial
removal of non-cellulosic components from native cotton
2.6 ENZYME COMPOSITION
Enzymes can have molecular weights ranging from about 10,000 to over 1 million. A
small number of enzymes are not proteins, but consist of small catalytic RNA
molecules. Often, enzymes are multiprotein complexes made up of a number of
individual protein subunits. Many enzymes catalyze reactions without help, but some
require an additional non-protein component called a co-factor. Co-factors may be
inorganic ions such as Fe2+, Mg2+, Mn2+, or Zn2+, or consist of organic or
metalloorganic molecules knowns as co-enzymes. [4]
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Figure: schematic diagram of enzymes composition
2.7 ENZYME CLASSIFICATIONS
Enzymes are classified according to the reactions they catalyze. The six classes are:
1. Oxidoreductases
2. Transferases
3. Hydrolysis
4. Lyases
5. Isomerases
6. Ligases
Examples:
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1. Alcohol dehydrogenase: An oxidoreductase converting alcohols to
aldehydes/ ketones.
2. Aminotransferases: Transferases catalyzing the amino acid degradation by
removing amino groups.
3. Glucose-6-phosphatase: A hydrolase that removes the phosphate group
from glucose-6-phosphate, leaving glucose and H3PO4.
4. Pyruvate decarboxylase: A lyase that removes CO2 from pyruvate.
5. Ribulose phosphate epimerase: an isomerase that catalyzes the
interconversion of ribulose-5-phosphate and xylulose-5-phosphate.
6. Hexokinase: A ligase that catalyzes the interconversion of glucose and
ATP with glucose-6-phosphate and ADP. [4]
2.8 HOW ENZYME WORKS
2.8.1 Amino Acids, Proteins, and Biochemistry
Amino acids are organic compounds made of carbon, hydrogen, oxygen, nitrogen,
and (in some cases) sulfur bonded in characteristic formations. Strings of 50 or more
amino acids are known as proteins, large molecules that serve the functions of
promoting normal growth, repairing damaged tissue, contributing to the body's
immune system, and making enzymes. The latter are a type of protein that functions
as a catalyst, a substance that speeds up a chemical reaction without participating in it.
Catalysts, of which enzymes in the bodies of plants and animals are a good example,
thus are not consumed in the reaction. [5]
2.8.2 Catalysts
In a chemical reaction, substances known as reactants interact with one another to
create new substances, called products. Energy is an important component in the
chemical reaction, because a certain threshold, termed the activation energy, must be
crossed before a reaction can occur. To increase the rate at which a reaction takes
place and to hasten the crossing of the activation energy threshold, it is necessary to
do one of three things.
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The first two options are to increase either the concentration of reactants or the
temperature at which the reaction takes place. It is not always feasible or desirable,
however, to do either of these things. Many of the processes that take place in the
human body, for instance, normally would require high temperatures—temperatures,
in fact, that are too high to sustain human life. Imagine what would happen if the only
way we had of digesting starch was to heat it to the boiling point inside our stomachs!
Fortunately, there is a third option: the introduction of a catalyst, a substance that
speeds up a reaction without participating in it either as a reactant or as a product.
Catalysts thus are not consumed in the reaction. Enzymes, which facilitate the
necessary reactions in our bodies without raising temperatures or increasing the
concentrations of substances, are a prime example of a chemical catalyst. [5]
2.9 INDUSTRIAL APPLICATIONS
There is even ongoing research into the creation of edible products from the
fermentation of petroleum. While this may seem a bit far-fetched, it is less difficult to
comprehend powering cars with an environmentally friendly product of fermentation
known as gasohol. Gasohol first started to make headlines in the 1970s, when an oil
embargo and resulting increases in gas prices, combined with growing environmental
concerns, raised the need for a type of fuel that would use less petroleum. A mixture
of about 90% gasoline and 10% alcohol, gasohol burns more cleanly that gasoline
alone and provides a promising method for using renewable resources (plant material)
to extend the availability of a nonrenewable resource (petroleum). Furthermore, the
alcohol needed for this product can be obtained from the fermentation of agricultural
and municipal wastes. The applications of fermentation span a wide spectrum, from
medicines that go into people's bodies to the cleaning of waters containing human
waste. Some antibiotics and other drugs are prepared by fermentation: for example,
cortisone, used in treating arthritis, can be made by fermenting a plant steroid known
as diosgenin. [6]
2.10 ENZYMES CHARACTERISTICS
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Enzymes can be isolated and are active outside the living cell. They are such efficient
catalysts that they accelerate chemical reactions measurably, even at concentrations so
low that they cannot be detected by most chemical tests for protein. Like other
chemical reactions, enzyme-catalyzed reactions proceed only when accompanied by a
decrease in free energy; at equilibrium the concentrations of reactants and products
are the same in the presence of an enzyme as in its absence. An enzyme can catalyze
an indefinite amount of chemical change without itself being diminished or altered by
the reaction. However, because most isolated enzymes are relatively unstable, they
often gradually lose activity under the conditions employed for their study. [6]
2.11 CONDITIONS FOR ENZYME ACTIVITY
All enzymes need the right environment for effective function, notably an optimal
acidity, which differs in accordance with the site at which a particular enzyme acts
(for example, more acidic inside cells than outside, and, for digestive enzymes, acidic
in the stomach and alkaline in the duodenum). Like any chemical reactions, the rate of
those that are catalyzed by enzymes varies with temperature. Local heat generation,
for example in exercising muscle, enhances all such reactions within it. Likewise,
whole-body metabolic rate increases in fever and decreases in hypothermia, because
of the effect on all enzyme-catalyzed reactions. Extremes of pH or temperature
irreversibly abolish enzyme activity, and so also do some substances that bind to the
active sites of particular enzymes. These include an organophosphate ‘nerve gas’ that
blocks acetyl cholinesterase (causing persistent accumulation of acetylcholine at
neuromuscular junctions, and thus uncontrollable muscle contraction). Poisoning by
cyanide is due to blocking an essential enzyme in mitochondria and so fatally
preventing all tissue respiration. [6]
Page 23 of 55

2.12 SOME REPRESENTATIVE ENZYMES, THEIR SOURCES, AND
REACTION SPECIFICITIES
Enzyme Some sources Reaction catalyzed
Pepsin Gastric juice Hydrolysis of proteins to
peptides and amino acids
Urease Jackbean, bacteria Hydrolysis of urea to ammonia
and carbon dioxide
Amylase Saliva, pancreatic juice Hydrolysis of starch to maltose
Phosphorylase Muscle, liver, plants Reversible phosphorolysis of
starch or glycogen to glucose-
1-phosphate
Transaminases Many animal and plant tissues Transfer of an amino group
from an amino acid to a keto
acid
Phosphohexose
isomerase
Muscle, yeast Interconversion of glucose-6-
phosphate and fructose-6-
phosphate
Pyruvic
carboxylase
Yeast, bacteria, plants Decarboxylation of pyruvate to
acetaldehyde and carbon
dioxide
Catalase Erythrocytes, liver Decomposition of hydrogen
peroxide to oxygen and water
Page 24 of 55

Alcohol
dehydrogenase
Liver Oxidation of ethanol to
acetaldehyde
Xanthine
oxidase
Milk, liver Oxidation of xanthine and
hypoxanthine to uric acid
2.13 FACTORS AFFECTING ENZYME ACTIVITY
Knowledge of basic enzyme kinetic theory is important in enzyme analysis in order
both to understand the basic enzymatic mechanism and to select a method for enzyme
analysis. The conditions selected to measure the activity of an enzyme would not be
the same as those selected to measure the concentration of its substrate. Several
factors affect the rate at which enzymatic reactions precede - temperature, pH,
enzyme concentration, substrate concentration, and the presence of any inhibitors or
activators. [7]
2.13.1 Enzyme Concentration
In order to study the effect of increasing the enzyme concentration upon the reaction
rate, the substrate must be present in an excess amount; i.e., the reaction must be
independent of the substrate concentration. Any change in the amount of product
formed over a specified period of time will be dependent upon the level of enzyme
present. Graphically this can be represented as:
Page 25 of 55

These reactions are said to be "zero order" because the rates are independent of
substrate concentration, and are equal to some constant k. The formation of product
proceeds at a rate which is linear with time. The addition of more substrate does not
serve to increase the rate. In zero order kinetics, allowing the assay to run for double
time results in double the amount of product. [7]
Table I: Reaction Orders with Respect to Substrate Concentration
Order Rate Equation Comments
zero rate = k rate is independent of substrate concentration
first rate = k[S] rate is proportional to the first power of substrate
concentration
second rate = k[S][S]=k[S]2 rate is proportional to the square of the substrate
concentration
second rate = k[S1][S2] rate is proportional to the first power of each of
two reactants
Page 26 of 55

The amount of enzyme present in a reaction is measured by the activity it catalyzes.
The relationship between activity and concentration is affected by many factors such
as temperature, pH, etc. An enzyme assay must be designed so that the observed
activity is proportional to the amount of enzyme present in order that the enzyme
concentration is the only limiting factor. It is satisfied only when the reaction is zero
order. In Figure 5, activity is directly proportional to concentration in the area AB, but
not in BC. Enzyme activity is generally greatest when substrate concentration is
unlimiting.
When the concentration of the product of an enzymatic reaction is plotted against
time, a similar curve results, Figure 6. Between A and B, the curve represents a zero
order reaction; that is, one in which the rate is constant with time. As substrate is used
up, the enzyme's active sites are no longer saturated, substrate concentration becomes
rate limiting, and the reaction becomes first order between B and C. To measure
enzyme activity ideally, the measurements must be made in that portion of the curve
where the reaction is zero order. A reaction is most likely to be zero order initially
since substrate concentration is then highest. To be certain that a reaction is zero
order, multiple measurements of product (or substrate) concentration must be made.
Figure 7 illustrates three types of reactions which might be encountered in enzyme
assays and shows the problems which might be encountered if only single
measurements are made. [7]
Page 27 of 55

B is a straight line representing a zero order reaction which permits accurate
determination of enzyme activity for part or all of the reaction time. A represents the
type of reaction that was shown in Figure 6. This reaction is zero order initially and
then slows, presumably due to substrate exhaustion or product inhibition. This type of
reaction is sometimes referred to as a "leading" reaction. True "potential" activity is
represented by the dotted line. Curve C represents a reaction with an initial "lag"
phase. Again the dotted line represents the potentially measurable activity. Multiple
determinations of product concentration enable each curve to be plotted and true
activity determined. A single end point determination at E would lead to the false
conclusion that all three samples had identical enzyme concentration. [7]
2.13.2 Substrate Concentration
It has been shown experimentally that if the amount of the enzyme is kept constant
and the substrate concentration is then gradually increased, the reaction velocity will
increase until it reaches a maximum. After this point, increases in substrate
concentration will not increase the velocity (delta A/delta T). This is represented
graphically in Figure 8.
Page 28 of 55

It is theorized that when this maximum velocity had been reached, all of the available
enzyme has been converted to ES, the enzyme substrate complex. This point on the
graph is designated Vmax. Using this maximum velocity and equation (7), Michaelis
developed a set of mathematical expressions to calculate enzyme activity in terms of
reaction speed from measurable laboratory data. [7]
The Michaelis constant Km is defined as the substrate concentration at 1/2 the
maximum velocity. This is shown in Figure 8. Using this constant and the fact that
Km can also be defined as:
Km=K-1 + K2 / K+1
K+1, K-1 and K+2 being the rate constants from equation (7). Michaelis developed
the followin
Page 29 of 55

 A small Km indicates that the enzyme requires only a small amount of
substrate to become saturated. Hence, the maximum velocity is reached at
relatively low substrate concentrations.
 A large Km indicates the need for high substrate concentrations to achieve
maximum reaction velocity.
 The substrate with the lowest Km upon which the enzyme acts as a catalyst is
frequently assumed to be enzyme's natural substrate, though this is not true for
all enzymes. [7]
2.13.3 Effects of Inhibitors on Enzyme Activity
Enzyme inhibitors are substances which alter the catalytic action of the enzyme and
consequently slow down, or in some cases, stop catalysis. There are three common
types of enzyme inhibition - competitive, non-competitive and substrate inhibition.
Most theories concerning inhibition mechanisms are based on the existence of the
enzyme-substrate complex ES. As mentioned earlier, the existence of temporary ES
structures has been verified in the laboratory. Competitive inhibition occurs when the
substrate and a substance resembling the substrate are both added to the enzyme. A
theory called the "lock-key theory" of enzyme catalysts can be used to explain why
inhibition occurs.
Page 30 of 55

The lock and key theory utilizes the concept of an "active site." The concept holds
that one particular portion of the enzyme surface has a strong affinity for the
substrate. The substrate is held in such a way that its conversion to the reaction
products is more favorable. If we consider the enzyme as the lock and the substrate
the key (Figure 9) - the key is inserted in the lock, is turned, and the door is opened
and the reaction proceeds. However, when an inhibitor which resembles the substrate
is present, it will compete with the substrate for the position in the enzyme lock.
When the inhibitor wins, it gains the lock position but is unable to open the lock.
Hence, the observed reaction is slowed down because some of the available enzyme
sites are occupied by the inhibitor. If a dissimilar substance which does not fit the site
is present, the enzyme rejects it, accepts the substrate, and the reaction proceeds
normally.Non-competitive inhibitors are considered to be substances which when
added to the enzyme alter the enzyme in a way that it cannot accept the substrate.
Figure 10.
Page 31 of 55

Substrate inhibition will sometimes occur when excessive amounts of substrate are
present. Figure 11 shows the reaction velocity decreasing after the maximum velocity
has been reached.
Additional amounts of substrate added to the reaction mixture after this point actually
decrease the reaction rate. This is thought to be due to the fact that there are so many
substrate molecules competing for the active sites on the enzyme surfaces that they
block the sites (Figure 12) and prevent any other substrate molecules from occupying
them.
Page 32 of 55

This causes the reaction rate to drop since all of the enzyme present is not being used.
[7]
2.13.4 Temperature Effects
Like most chemical reactions, the rate of an enzyme-catalyzed reaction increases as
the temperature is raised. A ten degree Centigrade rise in temperature will increase the
activity of most enzymes by 50 to 100%. Variations in reaction temperature as small
Page 33 of 55

as 1 or 2 degrees may introduce changes of 10 to 20% in the results. In the case of
enzymatic reactions, this is complicated by the fact that many enzymes are adversely
affected by high temperatures. As shown in Figure 13, the reaction rate increases with
temperature to a maximum level, then abruptly declines with further increase of
temperature. Because most animal enzymes rapidly become denatured at temperatures
above 40°C, most enzyme determinations are carried out somewhat below that
temperature. Over a period of time, enzymes will be deactivated at even moderate
temperatures. Storage of enzymes at 5°C or below is generally the most suitable.
Some enzymes lose their activity when frozen. [7]
2.13.5 Effects of pH
Enzymes are affected by changes in pH. The most favorable pH value - the point
where the enzyme is most active - is known as the optimum pH. This is graphically
illustrated in Figure 14.
Extremely high or low pH values generally result in complete loss of activity for most
enzymes. pH is also a factor in the stability of enzymes. As with activity, for each
enzyme there is also a region of pH optimal stability. [7]
Page 34 of 55

THE OPTIMUM PH VALUE WILL VARY GREATLY FROM ONE ENZYME
TO ANOTHER, AS TABLE II SHOWS:
Enzyme pH Optimum
Lipase (pancreas) 8.0
Lipase (stomach) 4.0 - 5.0
Lipase (castor oil) 4.7
Pepsin 1.5 - 1.6
Trypsin 7.8 - 8.7
Urease 7.0
Invertase 4.5
Maltase 6.1 - 6.8
Amylase (pancreas) 6.7 - 7.0
Amylase (malt) 4.6 - 5.2
Catalase 7.0
In addition to temperature and pH there are other factors, such as ionic strength,
which can affect the enzymatic reaction. Each of these physical and chemical
parameters must be considered and optimized in order for an enzymatic reaction to be
accurate and reproducible. [7
Page 35 of 55

Chapter-3: Methodology
Page 36 of 55
Chapter: 3
METHODOLOGY

3.1 MATERIALS
In our project work, we have taken cellulosic fabric (knit & woven) for observing the
effect of enzyme treatment. We have taken a piece of woven fabric (plain fabric) and
four piece of knitted fabric as our materials for accomplishing our project work. The
name of the sample and their construction & specification are given in below:
A. PLAIN FABREIC (100% Cotton)
B. SINGLE JERSEY
C. WOVEN FABRIC
D. DENIM FABRIC
A. PLAIN FABREIC (100% Cotton)
1. Ends per Inch (EPI) = 97
2. Picks per Inch (PPI) = 64
3. GSM = 91
4. Warp Count = 51 Ne
5. Weft Count = 42 Ne
6. Warp Twist = 32
7. Weft Twist = 36
8. Warp Twist Direction = “Z”
9. Weft Twist Direction = “Z”
B. SINGLE JERSEY
1. Wales per Inch = 38
2. Course per Inch = 54
3. Yarn Count = 32 Ne
4. G.S.M = 164
5. TPI (Twist per Inch) = 23
6. Twist Direction = “Z”
3.2 METHOD
Page 37 of 55

3.2.1 De-sizing:
Enzymatic Treatment (oxidative method):
The weight of 25gm fabric from five samples (each sample contains 5gm) have been
taken for the enzyme treatment by using the following recipe:
Recipe:
Enzyme = 1.5% owf
Wetting Agent = 1%
PH
= 4.5 – 5.5
Temp = 550
C
Time = 15 min
M: L = 1: 10
Calculation
Total liquor = 15 gm × 10 = 150 ml
Enzyme % amount respect to owf (on the weight of the fabric)
In recipe, the Enzyme % (on the weight of the fabric) amount respect to the materials .
5
Required amount Enzyme =
= (5 ×1.5 ) ÷ 1
= 7.5cc×2=15cc
Acetic acid (gm/l) and wetting agent (gm/l) amount respect to liquor
Page 38 of 55
(Materials weight × Recipe amount %)
Stock solution%

In recipe, Acetic acid (gm/l) and wetting agent (gm/l) amount respect to liquor is
calculated with the following formula;
Required amount Wetting agent =
= ( 5× 1%) ÷ 1%
= 5 cc×2=10c
Temperature = 550
C
PH
= 4.5 – 5.5 (by PH
paper)
Process Curve:
Page 39 of 55
Stock solution%
(Total Liquor (lit) × Recipe amount)

Process:
1 = Raw Water
2 = Acetic Acid
3 = PH
Check
4 = Enzyme
5 = Materials
Working Procedure:
Page 40 of 55
1 2 3 4 5
1 5min at 550
c
Cool
10 min at 800
c
Bath Drain
+
Cooling
+
Rinsing
+
Washing

1. Firstly, 5 gm of fabric from each sample has been taken for enzyme
treatment.
2. Set the bath with substrate at room temperature and add wetting agent,
acetic acid and check PH
. (PH
= 4.5-5.5)
3. After checking PH
of the dye bath, appropriate amount of enzyme is added
into the dye bath.
4. If necessary small amount of common salt or calcium chloride are added to
keep enzyme solution stable at temperature.
5. Raise the temperature up to 550
c and hold the temperature for 15 min for
proper enzymatic action.
6. Then cool and rinse for removing fiber dust from the bath.
7. After rinsing the temperature is raised up to 800
c to kill enzyme. After
completing the action the process is drained out.
3.2.2 Bio-scouring: Americos Bio-scoured XL
Enzymetic Treatment (Exhust Method);
Adventages:
• Softer febric
• Reduced water consumption
• Reduced energy consumption
• Mild application conditions
Properties:
Page 41 of 55

Apperence Viscos liquid
Chemical character Mixture of pectinase & cellulose
enzyme
Ionicity Non-ionoc
Soluability Readily soluable in water
pH(1% solution) 7±1
Application pH range 7.5-9
Application temperature range 55º-60ºc
Stability:
Hard water Good ,ca2+ & mg2+ ions increase the
efficacy of enzyme
Acids Poor
Alkalies Stable in alkaline region from pH 7 to 9
Metal ions Iron and copper ions are poisonous for
enzymes
Compatibility:
Non-ionic surfactant Generally very good
Anionic surfactant Selective, some reduce the efficacy of
enzyme
Solvent based surfactant Selective, some reduce the efficacy of
Enzyme
Organic sequestrant Generally good
Page 42 of 55

Reducing / oxidizing agent Reduce the efficacy of
Enzyme
Application Methods:
Americos Bio-scoured XL can be applied by exhaust method:
Exhaust application : (jigger ,soft-flow m/c, winch)
• Americos Bio-scoured XL 2-3 ml/l
• Americos anti-crease pro-76 A 0.5-1 g/l
• temparature 55º-60ºc
• pH 7.5-9
• time 60 min
Working Procedure:
• Add 2-3 g/l of Americos extracta XL ( emulsifying cum wetting
agent),raise the temperature to 80º-85ºc and run the machine for 30
minutes.
• Drain the above liquer at high temperature.
• Give one hot wash & one cold wash.
3.2.3 Neutral cellulase:
Americos cellucom 110 OM:
Enzymetic Treatment (Exhust Method);
Adventages:
• High contrast with low strength loss.
• Better and bigger granular effect.
• Even abrasion.
• Low back staining of indigo.
• Improves the touch of germents
• Very broad pH range (5.5-8)
Properties:
Page 43 of 55

Apperence Powder
Odor Slightly fermented odor
Chemical character Cellulose (endo,1-4-8 d glucanase )
Soluability Readily soluable in water
pH(1% solution) 7±1
Application pH range 5.5-7.5
Application temperature range 50º-60ºc
Stability:
Hard water Good
Acids/ Alkalies Active and Stable in pH range 4.5 to 8.5
Metal ions Iron and copper ions are poisonous for
Enzymes
Compatibility:
Non-ionic surfactant Good
Page 44 of 55

Anionic surfactant Selective, some reduce the efficacy of
enzyme
Solvent based surfactant Selective, some reduce the efficacy of
enzyme
Organic sequestrant Generally good
Reducing / oxidizing agent Reduce the efficacy of
enzyme
Application Methods:
Americos cellucom 110 OM is applied on denim germents using rotary drum
washer with high mechanical action.
Dosage :
• Americos cellucom 110 OM 0.5-1%(owg)
• Americos anti-crease pro-76 A 0.5-1 g/l
• temparature 55º-60ºc
• pH 6-7
• time 60 min
Working Procedure:
• Add 2-3 g/l of Americos extracta XL ( emulsifying cum wetting
agent),raise the temperature to 80º-85ºc and run the machine for 30
minutes.
• Drain the above liquer at high temperature.
• Give one hot wash & one cold wash.
Page 45 of 55

Page 46 of 55
Chapter: 4
RESULTS & DISCUSSION

Chapter-4: Result & Discussion
4.1 RESULT
After completing enzyme treatment we have analyzed the fabric by different tests.
There is an important test is done in textile industry after enzyme treatment on
cellulose fabric. The test procedure and our analyzed report are given in below:
Experimental procedure:
At first 5 gm fabric from each sample were cut accurately by sample cutter their
weights were taken separately with the help of balance. Then, the samples were
prepared for enzyme treatment. After completing the enzyme treatment, the samples
were weighted again and the following data was taken.
Sample Name Wt. of Untreated
Sample
Wt. of Treated
Sample
Wt. Loss Wt. Loss %
1. Plain Fabric 5.000 gm 4.905 gm 0.095 gm 4.167
2. Single jersey 5.000 gm 4.899 gm 0.101 gm 4.367
3.Woven fabric 5.000 gm 4.901 gm 0.099 gm 4.333
4.2 Samples of Enzyme Treatment
Page 47 of 55

4.2 Discussion
Page 48 of 55

Enzymes act as catalysts to speed up complex chemical reactions such as the
hydrolysis of cellulose, starches, and triglyceride based compounds in fats and oils.
Because they act as catalysts, relatively small concentrations of enzymes are required.
If the conditions are favorable to the specific enzyme, the catalytic action (hydrolysis)
will be repeated many times in the same system.
Enzymatic treatments of the cotton fabrics, like any wet processing of textiles, involve
the transfer of mass from the processing liquid medium (enzyme solution) across the
surface of the textile substrate. As with all chemical processes, these transport
processes are time and temperature dependent, and compromising either could affect
productivity and/or product quality.
At the end of our project work, we have reached in a decision that after enzyme
treatment the weight loss % of three samples (plain, single jersey, rib) are about the
same label. But we also observed that there is a significant variation of weight loss %
in interlock fabric and pique fabric has little effect of weight loss % than other
samples. Because interlock fabric contains large number of hairy fibers and the
number of hairy fibers of pique fabric is little than other sample.
In our project work we have known that principle of bio-finishing is to remove all
impurities and individual loose fibers end that protrude from the fabric surface
simultaneously in order to retain the strength of fabric at an acceptable level.
Page 49 of 55

Page 50 of 55
Chapter: 5
CONCLUSION

5.0 Conclusion
1. Enzyme treatment is very important for textile wet processing technology.
It increases more even fabric surface appearance and improved hand. It
removes all impurities and individual loose fibers end that protrude from
the fabric surface simultaneously in order to retain the strength of fabric at
an acceptable level.
2. So we can say that cotton and other natural fiber based on cellulose can be
improved by an enzymatic treatment known as Bio-Polishing. This
treatment gives the fabric a smoother and glossier appearance. The
treatment is used to remove 'fuzz' - the tiny strands of fiber that protrude
from the surface of fabric. A ball of fuzz is called a 'pill' in the textiles.
After Bio-Polishing, the fuzz and pilling are reduced.
3. One thing is very clearly pointed out that benefits of removing fuzz are a
softer and smoother handle, and superior color brightness of fabric.
Page 51 of 55

Page 52 of 55
Chapter: 6
REFERENCE

6.1 REFERENCE
A. Webpage
1. http://www.mapsenzyme.com
2. http://www.mapsenzymes.com/History_of_Enzymes.asp
3. http://www.answers.com
4. http://biotech.about.com/mbiopage.htm
5. http://www.biology-questions-and-answers.com/biology-ebook.html
6. http://www.chemheritage.org
7. http://www.worthington.com
8. http://www.naturalnews.com/np/enzymes.html
9. http://en.wikipedia.org/wiki/Main_Page
10. http://www.2456.com/epub/eventlist/event_ata_en.html
B. Books
1. Textbook of Biochemistry by- Harrow- B and Mazur
2. Chemistry of Textile Industry by- C.M. CARR
C. Industry
1. R L YARN DYEING LTD.
Chandura, Shafipur,Gajipur,Dhaka
2. MAGPIE KNIT COMPOSITE LTD
Amtola,savar,Dhaka.
Page 53 of 55

Page 54 of 55
Chapter: 7
Appendix

7.0 Appendix
1) For more information:
USA and Canada
Danisco US Inc.
Genencor Division
200 Meridian Centre Blvd., Rochester, NY 14618 USA
Telephone: 1-800-847-5311 (USA)
Telephone: +1-585-256-5200
Telefax: +1-585-244-4544
2) Europe, Africa and Middle East
Genencor International B.V.
P.O. Box 218, 2300 AE Leiden, The Netherlands
Telephone: +31-71-5686-168
Telefax: +31-71-5686-169
Latin America
3) Danisco Argentina S.A.
Alicia Moreau de Justo 1750 Piso 2, G y H
Buenos Aires C1107AFJ
Argentina
Telephone: +54-11-5199-9550
Telefax: +54-11-5199-9559
Asia/Pacific
4) Danisco Singapore Pte Ltd.
Genencor Division
61 Science Park Road
The Galen #06-16 East Wing
Singapore Science Park III
Singapore 117525
Telephone: +65-6511-5600
Telefax: +65-6511-5666
Web Address
www.genencor.com
Page 55 of 55

Different kinds of enzyme on textile substrates

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