Review
Enzyme Treatment at Different Stages of Textile Processing:
A Review
Stefane Vieira Besegatto,1 Flávia Nunes Costa,1
Mayra Stéphanie Pascoal Damas,1 Bruna Lyra Colombi,1
Andressa Cristina De Rossi,1 Catia Rosana Lange de Aguiar,2
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and Ana Paula Serafini Immich2
1 moval of fibrils and hairiness from fabrics or cotton garments, a
Department of Chemical Engineering and Food Engineering,
Federal University of Santa Catarina, Florianópolis, Brazil
2
Department of Engineering, Federal University of Santa Catarina,
Blumenau, Brazil
Abstract
Increased environmental awareness and regulations are mak-
ing enzymes a good alternative to replace conventional che-
mical processes, especially those using large amounts of toxic
chemicals and energy. The advantages of enzymatic processes
include proven efficiency—even for soft processing conditions,
which reduces energy consumption—and products that are
biodegradable. Enzymes, as biocatalysts, have been widely
accepted in several industries due to substrate specificity and
an increased emphasis on green chemistry. The use of enzymes
is especially recognized in textile processing for its ability to
replace harsh conventional chemicals, reduce water and en-
ergy consumption, and improve aesthetic quality. This work
presents a brief review of enzymatic applications in different
stages of textile processing, desizing, biopreparation, and
biofinishing, as well as its use in wastewater treatments as a
green alternative to conventional treatments.
Keywords: Enzymes, desizing, biopreparation, biofinishing,
effluent treatment
Introduction
T
he use of enzymes by humans emerged naturally
among primitive groups, mainly for food and beverage
production, but also for tanning hides for clothing.1 In
the textile industry, the first biotechnological applica-
tion was related to flax retting. Over 2,000 years ago, microor-
ganisms were used to separate fibers from stems. In 1919,
amylases were introduced that were able to transform starch into
water-soluble components.2 Amylases are still applied for re-
moving the starch solution from fabrics after weaving.3 In the
1960’s, biological detergents emerged, and proteases became part
of the chemical composition, specifically to extract organic stains
caused by proteins (e.g., eggs, blood) from clothes.
298 INDUSTRIAL BIOTECHNOLOGY ª M A R Y A N N L I E B E R T , I N C .  V O L . 1 4 N O . 6  D E C E M B E R 2 0 1 8
In the late 1970s, it was discovered that cellulose increases
detergency in fabric washing and removes fibrillation in mul-
tiple washes. Cellulases are currently present in many powder
detergents, especially those active in the alkaline range. There
are other applications for cellulases, including enzymatic re-
process known as biopolishing. Other applications were iden-
tified for these enzymes in the finishing process, including
giving a vintage look to denim articles and other clothes.3
The global market for industrial enzymes is extremely com-
petitive, with Novozymes, DSM, and Dupont being the largest
producers. North America and Europe are considered to the
largest consumers of industrial enzymes, although Asia-Pacific
(namely China, Japan, and India) are consuming increasing
amounts as their economies grow.4 According to Dewan, the
market for enzymes for industrial application in 2014 reached
approximately US$4.6 billion and by 2015 had grown to US$
4.9 billion.5 It is estimated that by 2021 market value will reach
about US$6.3 billion.5 This can be attributed to a better under-
standing of biochemical production, fermentation processes,
and recovery methods, which has made it possible to increase
the number of accessible enzymes and their applications into
products and industrial processes. The number of commercial
enzymes has risen due to the number of transformations they can
catalyze and the fact that they can be adapted to different process
conditions, promoting their industrial use.6,7 Currently, enzymes
are being applied in different markets, including textiles, paper
and cellulose, leather, detergents, pharmaceuticals, chemicals,
food and beverages, biofuels, animal feed, and personal care,
among others.
Around four thousand enzymes are known, and two hundred
are used by industry.8 Enzymes, as biocatalysts, were accepted by
many sectors due to substrate specificity and a push for green
chemistry. The use of enzymes, especially for textile processing,
is considered an effective way to replace conventional, harsh
chemical products, conserve water and energy, and notably re-
duce environmental impact and damage to fibers.9 Growing
concern for the environment has led to many studies that focus on
applying enzymes to different steps of textile finishing.
Enzymatic processes are applied in almost all textile-
production stages. Enzymes contribute to process-time effi-
ciencies, desizing, biopreparation, and biofinishing. They
enable the textile industry to reduce harsh conditions from
processes, reduce costs, and increase the quality of textiles.
Enzymes are also non-toxic, which is favorable to the environ-
ment and energy conservation, as well as in line with environ-
mental regulations.2,10
DOI: 10.1089/ind.2018.0018

The objective of this paper is to explain the most important
textile processes that use enzymes as a substitute for traditional
chemical processes, including their effluent treatments. This
paper analyzes each step of the process, looking at the involved
mechanisms and advantages of enzymes in the textile industry.
Desizing
In weaving, yarns are subjected to significant stresses, in-
cluding tension, bending, and friction with parts of the power
loom. This tends to lift fibers from the surface of the spun yarns
until they rupture, causing a degradation of fabric quality and a
reduction in mechanical properties. To protect the yarns and
prevent breakage during weaving, yarns go through a process
called sizing, where yarns are covered with textile-sizing che-
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micals (TSC) to bind fibers or filaments and prevent damage
from contact between yarns and power loom parts. At the end of
the weaving process, TSC needs to be removed to reobtain the
initial physical characteristics of the yarn and not interfere with
the next process, dyeing.
The TSC removal process is known as desizing. Desizing can
be done chemically, physically, or with a combination of both
techniques. Conventional processes use many chemicals, spe-
cific to each TSC used, and require enormous energy and time.
Desizing has been performed by organic decomposition, alka-
line dissolution, acid hydrolysis, and oxidizing agents. To re-
duce environmental damage enzymatic desizing has been
investigated.11
Cotton is among the fibers that most use the sizing process to
strengthen its fibers and allow them to remain intact until the end
of the weaving process. In general, starch and its derivatives are
the most-used gelling agents, corresponding to about 75% of
gelling agents use, due to their low cost and high availability.
Starch has to be removed from the cotton fibers to be digested.12
The traditional method, called kier, consists of boiling the
washing liquor containing sodium hydroxide (2% concentra-
tion) and detergent. The process is performed in a kier boiler and
aims to remove natural impurities such as waxes, wood chips,
and oil stains. After the process, the fiber requires a hot water
rinse to remove all residues for the liquor. This traditional pro-
cess, however, is expensive and generates many toxic effluents.
For that reason, enzymatic processes have been implemented.
Enzymes require mild temperature and pressure conditions, do
not require the use of toxic chemicals, and can be adapted to any
type of equipment already present in the industry.11
Enzyme methods have been gaining ground since 1919, when
an enzyme called Rapidase, which is able to liquefy the starch in
dextrin, was introduced to the market. Today, enzymes are di-
vided into two classes, alpha and beta. a-Amylase hydrolyzes
starch at random by decomposing it into soluble sugars. b-
Amylase hydrolyzes starch into maltose so that its carbon chain
is gradually reduced. The rate of desizing can be altered by the
presence of a mixture of alpha and beta amylases. In the pres-
ence of a-amylase, the viscosity of the solution drops rapidly,
and the opposite is observed for the presence of b-amylase.
Thus, the chosen ratio between beta and alpha amylase defines
the tissue desizing time. Amylases do not cause a structural
modification in the carbohydrate chains of cotton, and the en-
zymatic process is simple and easy to perform. The tissue is
ª M A R Y A N N L I E B E R T , I N C .  VOL. 14
ENZYME TREATMENT FOR TEXTILE PROCESSING
heated in a bath containing enzymes with controlled temperature
and pH. The digestion period is influenced by the amount of
starch present as well as by the amount of amylase used. One
way to increase the efficiency of hydrolysis is with the associ-
ation of proteases and lipases. After hydrolysis, the tissue is
washed with hot water, with or without cleaning agents (mixture
composed by anionic and non-ionic surfactants), to remove
excess enzyme excess and alkaline pH-regulating products.11
However, some natural fibers present their own TSC and do
not need any additional synthetic process, including silk and
ramie, although, for an effective spinning process, their re-
moval is also necessary. Silk is a natural fiber made from the
excretion of silkworms. It consists of fibroin (70–75%), the
structural center of silk, and a group of proteins composed
mainly by sericin (25–35%). The TSC covers the fibroin,
binding them to each other and contributing to the cocoon’s
structure. The process of making silk can be divided into six
steps: baking, unwinding, desizing, dyeing, weaving, and fin-
ishing. Of these steps, desizing is for the fabric’s finishing.
Desizing focuses on the complete removal of sericin, giving
fabrics a smooth and glossy appearance and increasing dye
uptake.13
Conventional sericin removal processes consist of alkaline
baths containing surfactants, and parameters such as pH, tem-
perature, alkalinity, and time should be precisely controlled for a
complete removal. As the process requires the use of aggressive
chemicals, fiber degradation in form of mass loss occurs,
compromising the fabric’s final appearance, including superfi-
cial fibrillation, weak handling, decreased traction, and irregular
absorption of dyes.14
The use of enzymes for silk desizing is an environmentally
friendly alternative that may reduce defects that conventional
processes may cause in the final garment. Protease is the most
common class of enzymes used due to its specificity for proteins.
Although better results were obtained using alkaline proteases,
these can be acidic or neutral. Protease combined with lipase
was investigated, and it leads to an increase in fabric wettability.
Silk fabrics treated by enzymatic processes featured higher
whiteness, greater shear, and flexural stiffness, but also lower
fullness and softness.14
Vaithanomsat and Kitpreechavanich15 treated sericin recov-
ered from traditional processing by membrane ultrafiltration
associated with enzymatic hydrolysis. They demonstrated the
recovery of a large percentage of the proteins and also facilitated
the treatment of wastewater. Later, Suwannaphan et. al.13 used
extracellular serine protease of Bacillus sp. (C4 SS-2013),
which, due to its high affinity to sericin and other glue proteins
and low affinity to fibrous proteins, showed good performance
in the desizing of the silk and aided in the fiber’s bleaching.
The association of ultrasound and enzymes is extensively
studied in all stages of textile processing. Ultrasonic cavitation
changes the conformation of the protein, which will alter en-
zymatic activity. The degrees of tolerance and ultrasonic sen-
sitivity of different enzymes are conditioned to the intensity of
the treatment used. Low intensity and short duration is the best
option to increase enzymatic activity and prevent the progres-
sive loss of stability and enzyme activity. The same result can
also be observed for immobilized enzymes. Ultrasound can also
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 BESEGATTO ET AL.
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Fig. 1. Different ways of using ultrasonic treatment in enzymatic reactions. Color images available temperatures has many downsides,
online at www.liebertpub.com/ind
be used in pretreatment of substrates as a way of destroying its
molecular aggregation and acts to remove the indigestible cu-
ticle, making the substrate more vulnerable to enzymatic at-
tack.16 Figure 1 shows how ultrasound can influence the activity
of the enzyme in immobilized enzymes and in the substrate.
Enzymes such as alcalases and savinase, which are of the
protease class, and their association have been tested in con-
junction with ultrasound in the modification of an environ-
17
mentally friendly silk structure. At desizing, the reaction rate
between starch and amylase enzyme was significantly acceler-
ated by ultrasound. However, ultrasound could have negative
effects on enzymatic reactivity due to inadequate control of
parameters. The technique proved to be effective for heteroge-
neous mixtures, facilitating the mixing of the pectin, cellulose,
and starch by pectinase, cellulase and amylase, respectively.18
Even with the reduction of energy expenditure and the use of
chemical products, which would reduce environmental pollu-
tion, the low efficiency of enzymatic desizing—such as long
process periods and high costs of commercial enzymes—still
make the overall process on an industrial-scale unfeasible.
This is a study field that stills gathers great interest for further
research.
Biopreparation
Chemically, the cotton fiber contains cellulose and between 4
and 12% of natural impurities (Fig. 2), which provide both
hydrophobic protection and a lubricated surface for proces-
sing.19,20 Thus, before the wet dyeing process, the natural non-
cellulosic materials must be removed. Raw cotton must be
300 INDUSTRIAL BIOTECHNOLOGY D E C E M B E R 2 0 1 8
cleaned and converted into hydro-
philic cotton to achieve excellent
absorbency and color uniformity.
The classical industrial process of
preparation comprises an alkaline
scouring with sodium hydroxide
(NaOH) at high temperatures, ac-
companied by voluminous wash-
ing and bleaching with chemical
agents.21
The alkaline scouring allows the
removal of fats, waxes, pectins, and
proteins from the cotton fabric, in-
creasing their degree of white, ab-
sorbent capacity and wettability.21
Bleaching, on the other hand,
eliminates the natural pigments
(flavonoids) that remain in the cel-
lulosic fiber, through oxidizing
agents (hydrogen peroxide, sodium
peroxide, peracetic acid, sodium
hypochlorite, and sodium chlorite)
or reducing agents (sulfur dioxide,
sodium hydrosulfite and sodium
bisulfite).21,22 Undeniably, the use
of various chemicals and high
including the formation of toxic
gases, corrosive actions, large en-
ergy consumption, cellulose depolymerization, reduction of fab-
ric tensile strength, and ecosystem pollution.22
By introducing enzymatic treatments called bioscouring and
biobleaching, a more sustainable textile processing can be provided,
with clean technology and environmental gains. In bioscouring,
pectinases can be employed for removal of pectin, proteases for
proteins, lipases for oils and fats, xylanases for hemicellulose, etc, in
a pure or associated way.23 Catalase, glucose oxidase, and laccase
are examples of promising enzymes for biobleaching.21 The se-
lection of enzymatic lines is based on the pH, temperature, required
time, and end-product quality required.24
Usluoglu and Arabaci25 combined the purging and bleaching
bioprocesses of cotton/polyamide (CO/PA) fabrics in a single bath
with enzymes (lipase, protease, cellulase, or pectinase) and per-
acetic acid. They discovered that treatment at 60C for 45 min at
pH 7.5 provided the fabric with high-quality humidification,
outstanding whiteness, and higher tensile strength in a shorter
period, lower temperature (from 98 to 60C), and smaller alkali
consumption than the usual. The reaction was adjusted to 20 g/L of
tetra acetyl ethylene diamine (TAED), 12 g/L of sodium perborate,
2 g/L of enzymes, and 1 g/L of nonionic wetting auxiliary.25
Pušić, Tarbuk, and Dekanić26 stated that acid pectinases (pH
5) and neutral (pH 7) can also be used in the cotton bioscouring.
From an ecological point of view, the action of the neutral en-
zyme is more beneficial because there is no need for neutrali-
zation of its wastewater. According to Niaz et al.,20 pectinases
decrease the percentage of non-cellulosic constituents, and give
higher tenacity, better hydrophilicity, and acceptable whiteness
for cotton yarns.

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Fig. 2. Schematic representation of the cotton structure, showing the distribution of cellulose and used for five cycles. Therefore, the
other non-cellulosic materials in the various fiber layers.21
Easson et al.27 studied bioscouring Greek cotton with pectinase
along with ultrasonic radiation to increase stability and enzymatic
activity. The optimized route employed 100% ultrasound power at
220 kHz frequency for 60 min and with 31 mg/mL of pectinase.
Pectin decomposition was higher than 98% compared to the
common NaOH technique, and the performance was greater than
37% when compared to the enzyme method without ultrasound.27
According to Karaboğa et al.,28 the introduction of ultrasonic en-
ergy during the enzymatic processing of cotton significantly im-
proves the enzymes’ efficiency, mass transfer, and yield without
affecting the strength of the fabric.
In 2015, Nerurkar, Joshi, and Adivarekar highlighted the
effectiveness of cotton bioscouring (60C, pH 9, and 120 min)
with lipase (8%) extracted from marine bacterial species
Bacillus sonorensis. This lipase was able to remove a sub-
stantial portion of waxy impurities and hydrolyze it into fatty
acids, ensuring adequate absorption and minimal damage to
the fabric. Infrared spectroscopy and scanning electron mi-
croscopy experiments revealed that, unlike bioscouring, the
alkaline scouring caused roughness on the surface of the
cellulosic fiber as a result of the damage caused by chemical
compounds.29
For biobleaching of raw cotton, Spina et al.30 applied laccases
(1 U/mL) produced by the fungus Trametes pubescens, in sy-
nergy with the conventional hydrogen peroxide (H2O2) meth-
od. The experiment was conducted at 50C for 60 min, followed
by an additional bath in H2O2 (4 mL/L) and NaOH (1,33 mL/L)
at 98C for another 30 min. The coupling of those two treat-
ments not only reduced the actual consumption of water and
chemicals but also increased the whiteness yield by up to 4.34
times.30
Silva et al.31 evaluated the effect of a commercial enzymatic
association (3.580 U/g of cellulase, 0.236 U/g of lipase, and
0.868 U/g of pectinase) on 100% cotton fabric bioscouring. The
ª M A R Y A N N L I E B E R T , I N C .  VOL. 14
ENZYME TREATMENT FOR TEXTILE PROCESSING
articulation of these three enzymes
provided excellent results in terms
of white degree (25 – 0.7 Berger),
pectin removal (87 – 9%) and hy-
drophilicity (14 – 2 s). The meth-
odology proposed by Silva et al.32
achieved equivalent and at times
improved quality, as well as less
water, time (40 min), and energy
(55C) at neutral pH (6.5) and with
less environmental impact.
Immobilization of a recombinant
pectate lyase on magnetic nano-
particles for bioscouring of cotton
fabric was studied by Chakraborty,
Rao, and Goyal.32 The immobilized
enzyme showed enhanced thermo-
stability and activity compared with
free enzyme, and it could also be
easily recovered from the mixture
with the help of a magnet and re-
immobilization of alkaline pecti-
nase can provide an economical and
environmentally friendly alternative to chemical scouring.32
Synthetic fibers also form an important part of the textile
industry but have the disadvantage of low hydrophilicity.
Polyester fibers are particularly hydrophobic. Improved hydro-
philicity can be achieved by modifying the substrate surface
with enzymes. A relevant example of an applicable enzyme is
cutinase, which displays significant hydrolytic activity and in-
creases the hydrophilicity of polyesters by hydrolysis of the ester
bonds.33
In summary, bioscouring and biobleaching processes mini-
mize fiber damage under mild pressure, pH, and temperature
conditions and are ecologically favorable by reducing the
amount of chemicals, energy, and byproducts.19,34 Bioprocesses
provide support and innovation to the textile industry, improv-
ing the quality of its products, the safety of working conditions,
and compliance with environmental regulations.2 Although they
offer many advantages, there are some shortcomings, such as the
high cost and slower reaction rates.23,29
Biofinishing
The use of enzymes in the textile industry has been an envi-
ronmentally sustainable approach, leading to high-quality prod-
ucts and cost savings. In addition, enzymes provide permanent
effects to textiles.35 The best-known applications in the biofin-
ishing of textile products are the aging, cleaning, and renovation
of fabric surfaces.36 In this context, cellulases are the main en-
zymes used as natural catalysts for the modification of cellulosic
materials.37
The use of enzymes in textile finishing began in 1980 with the
processes of biostoning of jeans.38 In this technique, the cellu-
lases confer the aged or faded look to cotton fabrics under wet
conditions, controlled temperature, and pH.39 Basically, cellu-
lases weaken the surface fibers and, in conjunction with the
mechanical actions applied during the treatment, remove the
NO. 6  DECEMBER 2018 INDUSTRIAL BIOTECHNOLOGY 301
 BESEGATTO ET AL.

However, one of the problems during

enzymatic treatment is dye redeposition or
designated backstaining. This unwanted
property promotes a partial abrasion effect
and can cause blue spots on white parts,
such as pockets and lining.39,53 The use of
acid cellulases, such as cellulases produced
by Trichoderma, in biostoning is limited by
the backstaining and weakening of the tis-
sues, and anti-redeposition chemicals or
bleaching agents are used to prevent this
during washing steps.45 However, neutral
cellulases have shown a less aggressive ef-
fect.40 The ability to smear dye denim fab-
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rics to lighter shades without causing

significant changes in tissue weight and
strength has also been reported with the use
of fungal laccase.54,55 The use of im-
mobilized enzymes has been explored to
reduce the effect of backstaining and in-
creased abrasive activity.56,57
Biopolishing is another very widespread
application of the use of enzymes in the
finishing of textile products (cotton and
other cellulose-based fibers).58 This process
consists of the elimination of microfibers
from the tissue surfaces through the action
of the enzyme cellulase. It improves ap-
Fig. 3. Cellulases’ action mechanism on denim fabric. Color images available online at pearance, color brightness, feel to touch,
www.liebertpub.com/ind and the water-absorbing property of fibers,
while strongly reducing the tendency for the
weakened fibers containing the indigo dye. Since the indigo dye formation of pills and providing a cleaner surface structure.11,40
is on the surface of the fabric, removal of the surface fibers by Different effects can be obtained with different enzymatic
cellulases reveals the white string.40 The possible mechanism of compositions. In general, endoglucanase or endoglucanase-rich
biofinishing on denim garment is shown in Fig. 3. preparations are better for fiber surface aging and defibrillation,
The weakening of the fibers occurs through enzymatic hy-
drolysis, in which the cellulases catalyze the breakdown of
cellulose to smaller oligosaccharides and, finally, to glucose.41 Table 1. Cellulases Used in Textile Finishing
Cellulase activity refers to a multicomponent enzyme system
consisting of three types of cellulases: (i) endoglucanases (EG); SOURCE CELLULASE PH REFERENCE
(ii) cellobiohydrolases (CBH), also called exoglucanases; and Acremonium sp. EG 7 Schülein et al.
(iii) b-glucosidases (GC).42,43 (1996)47
Cellulases are produced through the metabolism of different
Humicola Insolens EGI, V, EGI + V 6-7 Schülein et al.
microorganisms, as can be seen in Table 1.40,44,47–52 Most of the (1998)48
related studies are of bacterial origin, although fungal and ac-
tinomycetes have also been reported.44 Trichoderma reesei and Chrysosporium Whole celulase, EG 5 Sinitsyn et al.
Humicola insolens are widely used in the textile industry to treat Lucknowense (2001)49
45
materials containing cotton denim. One reason for the wide- Melanocarpus EG, EG: CBH 5-7 Miettinen-Oinonen
spread use of T. reesei cellulases is its low cost. The cellulases Albomyces et al. (2004)40
are traditionally classified by the optimum pH of the enzyme:
Trichoderma Reesei EGIII+ EG e CBH 4,5-5,5 Fowler et al. (2001)50
neutral cellulases operate in the range of pH 6–8 and acidic
41,46
cellulases in the range of pH 4.5–6. EGII purified Heikinheimo and
Tissue stoning via biological treatment, when compared to the Buchert (2001)51
stone abrasion method, has several advantages. The application
1-4-GC Ibrahim et al.
of enzymes minimizes the amount of water, material (stones), (2011)52
and labor and allows the garment load to be increased, since it is
not necessary to add stones to the washing machine. The lack of Adapted from Miettinen-Oinonen (2007).44
stones also prevents damage to the machinery and clothing.41

302 INDUSTRIAL BIOTECHNOLOGY D E C E M B E R 2 0 1 8


while complete cellulase systems are better for cleaning and
purification purposes.38
Biopolishing can be performed before or after bleaching,
dyeing, or stamping steps. The treatment can also be performed
in conjunction with dyeing, in which case the pH values for both
processes must be compatible. However, whether the dye in-
hibits enzyme activity should be checked.39 Studies have shown
that treatment with cellulase before dyeing facilitates the sub-
sequent dyeing process.52,59
The enzymes may also be employed in the finishing of syn-
thetic fibers, such as polyester, polyamide, blends, etc. Ibrahim
et al.52 developed a new approach for the biofinishing of
cellulose-containing fabrics (bleached cotton, mercerized cot-
ton, and cotton/polyester blend fabric (50/50)) through the use of
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acid cellulases (Cellusoft L), followed by a washing cycle with
a high level of mechanical agitation to terminate the enzyme and
remove weakened fibers. Experimental results revealed that in-
creasing the enzyme dosage (20 g/L) resulted in an increase in
weight loss and a decrease in tissue rigidity coupled to an im-
provement in elasticity, regardless of the substrate used. The
lowest weight loss was obtained in the cotton/polyester blend,
followed by the bleached and mercerized cotton. Greater weight
loss is associated with greater accessibility of the enzyme to the
substrate, which is associated with the larger fibers’ surface area.
In terms of the increase of the capacity of enzyme-substrate at-
tack, the best-presented conditions were processing time 18 h,
temperature 50C, and mechanical agitation of 28 rpm.
Noreen et al.38 studied the optimization of biopolishing with
cellulase produced by Aspergillus niger in blends of polyester
and cotton fibers (52/48). Increasing cell concentration (0–5 mg/L)
resulted in an increased weight loss due to higher rates of
hydrolysis. A similar effect is obtained with the resistance to
pilling, while the tensile strength of the fabric decreased. All
fabrics are made of staple fibers prone to pilling. Thus, an op-
timum concentration of enzyme, in addition to pH and tem-
perature of the medium, should be selected to obtain the desired
degree of biopolymerization of the tissue with low weight loss.
As the purpose of the biopolishing is not to cause excess fiber
loss and resistance, it is recommended that the enzymes termi-
nate or immobilized enzymes be used.
To achieve the latest trends in fashion and improvements in
production efficiency, recent research has focused on preparing
a new generation of cellulosic enzymes that have been modified
through genetic engineering and biotechnology to offer greater
contrast of abrasion, better waxing, reduction of coloration, and
improved operating conditions (pH and temperature). Samanta
et al.60 reported that loss of strength and weight is mainly caused
by endoglucanase and exoglucanases, whereas enhancement of
biostoning and biopolishing can be achieved using endo-
glucanase II. To produce recombinant EG II without the pres-
ence of other enzymatic components, it was possible to obtain
the heterologous expression of the T. reesei gene in P. pastoris
with characteristics close to the EG II enzymes found com-
mercially—including increased thermal stability, a very im-
portant feature sought by the textile industry.
Biotechnology is the key to sustainable textile industry de-
velopment. The use of enzymes in the finishing stage proved to
be a useful tool for making textile processing environmentally
ª M A R Y A N N L I E B E R T , I N C .  VOL. 14
ENZYME TREATMENT FOR TEXTILE PROCESSING
friendly, reducing energy demand and water consumption, as
well as adding attractive characteristics to textile products.
Textile Effluent Treatments
Industrialization is fundamental in every country’s develop-
ment, but wastewater and the management of solid waste and
natural resources are major impediments to growth.61
In Brazil, the textile industry is an essential sector with great
economic importance. However, the activity poses a serious
threat to the country’s ecosystem, as it generates a large volume
of highly variable effluent generally containing a significant
amount of unfixed dye (8–20%), dyeing auxiliaries, inorganic
salts, and other chemicals that improve fiber adhesion.62
These highly colored effluents, when discharged into the
environment without treatment, lead to contamination of water
due to the presence of coadjuvants and many synthetic dyes,
which are lost in part during dyeing and finishing. Untreated
effluents affect not only aquatic life but also human health,
either by causing less light penetration or toxicity.61,63
Due to their complex aromatic chemical structure, most of
these dyes are extremely stable and resistant to primary treat-
ment methods, as well as physicochemical procedures, that
generally involve high operating costs and only transfer the
pollutants from one phase to another, causing secondary pollu-
tion problems.62,63 Thus, treatment of effluents is an important
step for the conservation of aquatic resources and the use of
enzymes as an alternative and more ecological method for the
treatment of such recalcitrant pollutants.64
Enzymatic treatment has proved its potential compared to
conventional methods, due to its highly selective nature, sim-
plicity, and high process efficiency, catalyzing reactions at rel-
atively low temperatures and in short time. Enzymes are also
biodegradable.65–67 Nevertheless, the treatment efficiency de-
pends on the influence of several parameters such as defined
temperature and pH ranges (optimal temperature and pH) and
enzyme and substrate concentration—factors that can directly
affect the reaction rate.65
Several studies have sought to develop enzymatic processes
using ligninolytic enzymes (such as manganese peroxidase
(MnP), lignin peroxidase (LiP) and laccase) for the treatment of
textile wastewater.65 White-rot fungi (WRF), including the ge-
nus Phanerochaete, Pleurotus, Trametes and Coriolus, have the
capacity to produce single extracellular enzymes or a lig-
ninolytic complex.61,68,69
Laccase (EC 1.10.3.2), an enzyme produced by many plants
and fungi, is an oxidoreductase that catalyzes the oxidation of
phenolic compounds and aromatic amines, increasing the
number of substrates with the use of mediators with a con-
comitant reduction of molecular oxygen to water.70–72 These
characteristics caused laccase to gain prominence in the degra-
dation of recalcitrant aromatic compounds.68
The ability of laccase to act on chromophore compounds,
such as azo, anthraquinone, triarylmethane, and indigoid dyes,
indicates the possibility of their application in processes that
discolor of textile waste water.65,73
Khlifi et al.74 investigated the discoloration and detoxification
of textile effluent by crude laccase from Trametes trogii in the
presence and absence of different mediators and observed that
NO. 6  DECEMBER 2018 INDUSTRIAL BIOTECHNOLOGY 303
 BESEGATTO ET AL.
the enzyme alone was not able to discolor the effluent. There-
fore, most of the mediators improved the discoloration of the
effluent, with 1-hydroxybenzotriazol (HBT) being the most
effective. Thus, the optimal conditions of discoloration (with
65% removal) of the defined laccase-HBT system were: 20%
effluent, pH 5.0, 50C temperature, and enzyme concentration
of 5 U/mL in the presence of 1 mM of HBT. However, the
authors concluded that only the discoloration of textile efflu-
ents does not necessarily result in their detoxification since the
byproducts of using the synthetic mediator HBT are still toxic.
The use of a natural mediator is a possible solution to such a
problem.
The use of mediators has overcome the laccase limitation of not
directly oxidizing non-phenolic substrates with high redox potential
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(above 1.3 V), due to the relatively low redox potential (0.5–0.8 V),
acting as electron carriers between the enzyme and other sub-
strates.75–77 Some synthetic mediators, such as 2,2¢-azino-bis
(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), violuric acid,
1-hydroxybenzotriazole (HBT), N-hydroxyphthalimide (HPI), and
N-hydroxyacetanilide (NHA), have been used.77 However, many
researchers have been searching for alternative mediators of natural
origin. Which should be environmentally friendly and available
economically.77,78
Khouni et al.71 studied the optimization of commercial lac-
case treatment (DeniLite IIS) in the discoloration of two re-
active textile dyes (black novacron R and blue bezaktiv S-GLD
150) in reconstituted effluent (textile dye and auxiliary com-
ponents) with a concentration of 40 mg/L and obtained maxi-
mum removal of approximately 99% for both, with optimal
values of 43C and 41.44C, pH 6.0 and 6.29, and enzyme
concentration of 222 and 226.43 U/L, respectively, after 24-h
processing period. It is important to note that the enzymatic
concentration depends on the type of dye and the composition of
the effluent.
Recently, several studies have focused on the immobilization
of this enzyme to obtain better performance. Bilal et al.68 dis-
cussed immobilization as a possibility of obtaining biocatalysts.
Immobilization also offers greater stability in the presence of
salts, solvents, heavy metals, and other denaturants and enables
biocatalyst recovery and reuse, which is of paramount impor-
tance for its commercial viability.
Zheng et al.79 immobilized purified laccase from Trametes
pubescens on glutaraldehyde crosslinked chitosan beads and
obtained considerable improvements, compared to free, in
temperature resistance, pH changes, storage time, and also
recovery. After six continuous cycles, the immobilized en-
zyme maintained 60% of its relative activity. When tested
for discoloration, it achieved better results with dye acid
black 172 (68.84% removal), 1.22 times better than with free
laccase. Increases in thermal, storage, and operation stabili-
ties of the immobilized laccase were also reported by other
authors.80,81
The peroxidases (EC 1.11.1.7), also of the oxidoreductase
class, are a group of enzymes that catalyze the oxidation of a
variety of organic and inorganic substrates in the presence of
hydrogen peroxide (or other organic peroxides as electron ac-
ceptors), being extensively distributed in plants, animal tissues
and microorganisms.82,83
304 INDUSTRIAL BIOTECHNOLOGY D E C E M B E R 2 0 1 8
Ulson de Souza84 evaluated the use of commercial HRP
(Horseradish Peroxidase) for dye removal from textile effluent.
They achieved a discoloration of 59% and 94% for the tested
dyes remazol turquoise blue G 133% and lanaset blue 2R, re-
spectively. For the textile effluent, the discoloration was 52%.
As reactions were performed at pH 4.0, 29.85 U/mL enzyme,
2x10-3 mmol/L H2O2, at 25C and stirring at 100 rpm. Toxicity
tests were performed after the treatment, and they concluded
that the effluent can be detoxified by the degradation of the HRP
enzyme.
According to Karim et al.,67 the use of peroxidases in the
detoxification and biotransformation of several aromatic
pollutants in wastewater has been reported. HRP is one of the
most studied enzymes for historical reasons; its relatively
easy availability, extraction, and purification; and the in-
creasing number of applications.85 As in laccase studies, the
researchers focused on the immobilization of peroxidase as a
strategy to obtain process improvements and reuse, which is
the main objective of most current researches.
Sun et al.86 used a novel macroporous nano protein support
composed of ZnO/SiO2 to immobilize HRP so that the catalyst
showed high discoloration activity for the dyes blue acid 113
(95.4%) and black acid 10 BX (90.3%) with a concentration of
50 mg/L and a reaction time of 35 minutes. The immobilized
HRP showed even higher resistance to temperature and pH
changes than to free form. Stability to storage and reuse were
also improved through immobilization. With discoloration of
the dye Blue Acid 113, it was found that 80.4% of the initial
efficiency was maintained after incubation at 4C for 60 days,
and that 79.4% of the decolorization efficiency was retained
after 12 cycles, reused.
Bilal et al.87 studied the immobilization of crude HRP by the
CLEAs technique and tested their efficacy on a range of reactive
dyes using a packed bed reactor, where a maximum degradation
of 94.26% was achieved for methyl orange dye followed by
basic red 9 with 91.73%, indigo with 84.35%, rhodamin B with
81.47% and rhodamin 6G with 73.6%, under the same condi-
tions, and maintaining 60% of its initial activity after seven
consecutive cycles of degradation of methyl orange dye. The
method of treatment significantly reduced the toxicity of the
dyes in the tested samples.
Based on the above, it is possible to observe that there
are several advantages associated with the use of peroxi-
dases and laccases, which demonstrate their potential in the
treatment of textile wastewater by reducing or eliminating
their toxicity and sludge formation. A trend has been noted in
current studies that the development and use of immobilized
enzymes would allow their reuse and could thus reduce their
cost.
Conclusion
Enzymes have been used by man for millennia and have in-
creasingly become an integral and active part of industrial
production of various goods and services. In the textile industry,
history and scientific efforts confirm that enzymes have become
a promising option for economic and technological develop-
ment and environmental gains.

Contamination of the environment from the textile industries
is a critical issue, and bio-innovation can provide a more sus-
tainable processing and healthy ecosystem, as well as add value
and quality to the textile product. However, a major factor in the
application of enzymes on a large scale is the high commercial
cost, which should be weighed against the reduction of water,
energy, and chemicals and benefits during processing.
Future studies must still be carried out to define the best
operational conditions to ensure the complete replacement of
classical methods. The transformative potential of enzymes,
coupled with biotechnology, microbiology, and genetics, can
and should provide more research, development, and innovation
opportunities.
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Author Disclosure Statement
No competing financial interests exist.
REFERENCES
1. Lotti M, Alberghina L. Lipases: Molecular structure and functions. In: Polaina J,
MacCabe AP, ed. Industrial Enzymes: Structure, Function and Applications.
Dordrecht: Springer, 2007: 263–282.
2. Aly AS, Moustafa AB, Hebeish A. Biotechnological treatment of cellulosic
textiles. J Clean Prod 2004;12(7):697–705.
3. Gübitz GM. Uma introdução à biotecnologia e à enzimologia e suas aplicações
na indústria têxtil. Quimı́ca Têxtil 2003;73:54–71.
4. Adrio JL, Demain AL. Microbial enzymes: Tools for biotechnological processes.
Biomolecules 2014;4:117–139.
5. Dewan, SS (2014). Global Markets for Enzymes in Industrial Applications.
Research Biotecnologic Reports. BBC Research, Report ID: BIO030J. Available at:
https://bccresearch.com/market-research/biotechnology/enzymes-industrial-
applications-report-bio030j.html (Last accessed October 2018).
6. Sharma R, Chisti Y, Banerjee UC. Production, purification, characterization, and
applications of lipases. Biotechnol Adv 2001;19(19):627–662.
7. Kirk O, Borchert TV, Fuglsang CC. Industrial enzyme applications. Curr Opin
Biotechnol 2002;13(4):345–351.
8. Badgujar KC, Dhake KP, Bhanage BM. Immobilization of Candida cylindracea
lipase on poly lactic acid, polyvinyl alcohol and chitosan based ternary blend
film: Characterization, activity, stability and its application for N-acylation
reactions. Process Biochem 2013;48(9):1335–1347.
9. Binod P, Palkhiwala P, Gaikaiwari R, et al. Industrial enzymes—Present status
and future perspectives for India. J Sci Ind Res 2013;72(5):271–286.
10. Madhu A, Chakraborty JN. Developments in application of enzymes for textile
processing. J Clean Prod 2017;145:114–133.
11. Karmakar SR. Chemical Technology in The Pre-Treatment Processes of Textile.
Elsevier Ltd, 1999:1–497.
12. Kozlowski RM. Handbook of natural fibres. Elsevier Ltd, 2012:1–516.
13. Suwannaphan S, Fufeungsombut E, Promboon A, Chimanage P. A serine
protease from newly isolated Bacillus sp. for efficient silk degumming, sericin
degrading and colour bleaching activities. Int Biodeterior Biodegrad 2017;117:
141–149.
14. Freddi G, Mossotti R, Innocenti R. Degumming of silk fabric with several
proteases. J Biotechnol 2003;106(2):101–112.
15. Vaithanomsat P, Kitpreechavanich V. Sericin separation from silk degumming
wastewater. Sep Purif Technol 2008;59(2):129–133.
16. Wanga D, Yan L, Ma X, et al. Ultrasound promotes enzymatic reactions by
acting on different targets: Enzymes, substrates and enzymatic reaction
systems. Int J Biol Macromol 2018;119:453–461.
ª M A R Y A N N L I E B E R T , I N C .  VOL. 14
ENZYME TREATMENT FOR TEXTILE PROCESSING
17. Mahmoodi NM, Arami M, Mazaheri F, Rahimi S. Degradation of sericin
(degumming) of Persian silk by ultrasound and enzymes as a cleaner and
environmentally friendly process. J Clean Prod 2010;18(2):146–151.
18. Harifi T, Montazer M. A review on textile sonoprocessing. A special focus
on sonosynthesis of nanomaterials on textile substrates. Ultrason Sonochem
2015;23:1–10.
19. Agrawal PB. The performance of cutinase and pectinase in cotton scouring
[PhD thesis] University of Twente, 2004;12:679–765.
20. Niaz A, Malik QJ, Muhammad S, et al. Bioscouring of cellulosic textiles. Color
Technol 2011;127(4): 211–216.
21. Varadarajan G, Venkatachalam P. Sustainable textile dyeing processes. Environ
Chem Lett 2016;14(1):113–122.
22. Ramadan AR. Characterization of biobleaching of cotton/linen fabrics. J Tecno
Gest 2008; 6 (1): 1–12.
23. Shahid M, Mohammad F, Chen G, et al. Enzymatic processing of natural fibres:
White biotechnology for sustainable development. Green Chem 2016.
24. Hoondal G, Tiwari R, Tewari R, et al. Microbial alkaline pectinases and their
industrial applications: A review. Appl Microbiol Biotechnol 2002;59(4):409–
448.
25. Usluoglu A, Arabaci G. Bleaching of Cotton/polyamide fabrics with enzymes and
peracetic acid. Asia-Pacific J Chem Eng 2014;9(3):364–367.
26. Pušić T, Tarbuk A, Dekanić T. Bio-innovation in cotton fabric scouring—acid and
neutral pectinases. Fibres Text East Eur 2015;23(1):98–103.
27. Easson MW, Wojkowski S, Condon B, et al. Ultrasound-enhanced bioscouring of
greige cotton: Regression analysis of process factors. AATCC J Res 2015;2(1):
16–23.
28. Karaboǧa C, Körlü AE, Duran K, et al. Use of ultrasonic technology in enzymatic
pretreatment processes of cotton fabrics. Fibres Text East Eur 2007;15(4):97–
100.
29. Nerurkar M, Joshi M, Adivarekar R. Bioscouring of cotton using lipase from
marine bacteria Bacillus sonorensis. Appl Biochem Biotechnol 2015;175(1):253–
265.
30. Spina F, Junghanns C, Donelli I, et al. Stimulation of laccases from Trametes
pubescens: Use in dye decolorization and cotton bleaching. Prep Biochem
Biotechnol 2016;46 (5):639–647.
31. de Melo da Silva LG, de Oliveira D, Ulson de Souza AA, Guelli Ulson de Souza
SM. Study and application of an enzymatic pool in bioscouring of cotton knit
fabric. Can J Chem Eng 2017;95(7):1253–1260.
32. Chakraborty S, Jagan Mohan Rao T, Goyal A. Immobilization of recombinant pectate
lyase from Clostridium thermocellum ATCC-27405 on magnetic nanoparticles for
bioscouring of cotton fabric. Biotechnol Prog 2017;33(1):236–244.
33. Vertommen MAME, Nierstrasz VA, Veer M van der, Warmoeskerken MMCG.
Enzymatic surface modification of poly(ethylene terephthalate). J Biotechnol
2005;120:376–386.
34. Shrimali K, Dedhia E. Enzymatic finishing of textiles. Int J Sci Res 2013;14(5):
2319–7064.
35. Schindler WD, Hauser PJ. Chemical Finishing of Textiles. Elsevier Ltd, 2004: 1–
213.
36. Duran N, Duran M. Enzyme applications in the textile industry. Rev Prog Color
Relat Top 2000;30(1):41–44.
37. Pere J, Puolakka A, Nousiainen P, Buchert J. Action of purified Trichoderma
reesei cellulases on cotton fibers and yarn. J Biotechnol 2001;89:247–255.
38. Noreen H, Zia MA, Ali S, Hussain T. Optimization of bio-polishing of polyester/
cotton blended fabrics with cellulases prepared from Aspergillus niger. J Ind
Biotechnol 2014;13(1):108–113.
39. Galante Y, Formantici C. Enzyme applications in detergency and in
manufacturing industries. Curr Org Chem 2003;7(13):1399–1422.
40. Miettinen-oinonen A, Londesborough J, Joutsjoki V. Three cellulases from
Melanocarpus albomyces for textile treatment at neutral pH. 2004;34:332–341.
NO. 6  DECEMBER 2018 INDUSTRIAL BIOTECHNOLOGY 305
 BESEGATTO ET AL.
41. Miettinen-oinonen A. Cellulases in the textile industry. In: Polaina J, MacCabe
AP, eds. Industrial Enzymes: Structure, Function and Applications. Dordrecht:
Springer, 2007:51–63.
42. Teeri TT. Crystalline cellulose degradation: New insight into the function of
cellobiohydrolases. Trends Biotechnol 1997;15(5):160–167.
43. Juturu V, Wu JC. Microbial cellulases: Engineering, production and applications.
Renew Sustain Energy Rev 2014;33:188–203.
44. Behera BC, Sethi BK, Mishra RR, et al. Microbial cellulases—Diversity &
biotechnology with reference to mangrove environment: A review. J Genet Eng
Biotechnol 2017;15(1):197–210.
45. Cavaco-Paulo A. Mechanism of cellulase action in textile processes. Carbohydr
Polym 1998;37(3):273–277.
46. Klahorst S, Kumar A, Mullins MM. Optimizing the use of cellulase enzymes. Text
Chem Color 1994;26:13–18.
Downloaded by STOCKHOLMS UNIVERSITET from www.liebertpub.com at 01/07/19. For personal use only.
47. Sulzenbacher G, Driguez H, Henrissat B, et al. Structure of the Fusarium
oxysporum Endoglucanase I with a nonhydrolyzable substrate analogue:
Substrate distortion gives rise to the preferred axial orientation for the leaving
group. Biochemistry 1996;35(48):15280–15287.
48. Schülein M, Kauppinen MS, Lange L, et al. Characterization of Fungal Cellulases
for Fiber Modification. In: Erikson KEL, Cavaco-Paulo A, ed. Enzym Appl Fiber
Process. ACS Symposium Series,1998:66–74.
49. Sinitsyn AP, Gusakov A V, Grishutin SG, et al. Application of microassays for
investigation of cellulase abrasive activity and backstaining. J Biotechnol 2001;
89(2):233–238.
50. Fowler T, Clarkson KA, Ward M, et al (2001). Method and Compositions for
Treating Cellulose Containing Fabrics Using Truncated Cellulase Enzyme
Compositions. Google Patents. Available at: https://google.com/patents/
US6268196 (Last accessed May 2018).
51. Heikinheimo L, Buchert J. Synergistic effects of Trichoderma reesei cellulases on
the properties of knitted cotton fabric. Text Res J 2001;71(8): 672–677.
52. Ibrahim NA, El-badry K, Eid BM, et al. A new approach for biofinishing of cellulose-
containing fabrics using acid cellulases. Carbohydr Polym 2011;83(1):116–121.
53. Charon N, Ponthus J, Espinat D, et al. Multi-technique characterization of fast
pyrolysis oils. J Anal Appl Pyrolysis 2015;116:18–26.
54. Asgher M, Shahid M, Kamal S, et al. Enzymatic Recent trends and valorization
of immobilization strategies and ligninolytic enzymes by industrial
biotechnology. J Mol Catal B Enzym 2014;101:56–66.
55. Chatha SAS, Ali S, Asgher M, Bhatti HN. Investigation of the potential of
microbial stripping of dyed cotton fabric using white rot fungi. Text Res J 2011;
81(17):1762–1771.
56. Pazarlioglu NK, Sariisxik M, Telefoncu A.Treating denim fabrics with immobilized
commercial cellulases. Process Biochem 2005;40(2):767–771.
57. Yu Y, Yuan J, Wang Q, et al.Cellulase immobilization onto the reversibly soluble
methacrylate copolymer for denim washing. Carbohydr Polym 2013;95 (2):675–
680.
58. Hebeish A, Hashem M, Shaker N, et al. Effect of post- and pre-crosslinking of
cotton fabrics on the efficiency of biofinishing with cellulase enzyme.
Carbohydr Polym 2009;78(4):953–960.
59. Paul R, Teli MD. Effect of swelling and reactive dyeing on the accessibility of
cotton to cellulase enzymes. J Appl Polym Sci 2011;121(4):1946–1950.
60. Samanta S, Basu A, Halder UC, Sen SK. Characterization of Trichoderma reesei
Endoglucanase II expressed heterologously in Pichia pastoris for better
biofinishing and biostoning. J Microbiol 2012;50:518–525.
61. Holkar CR, Jadhav AJ, Pinjari DV, et al. A critical review on textile wastewater
treatments: Possible approaches. J Environ Manag 2016;182:351–366.
62. Chhabra M, Mishra S, Sreekrishnan TR. Combination of chemical and
enzymatic treatment for efficient decolorization/degradation of textile
effluent: High operational stability of the continuous process. Biochem
Eng J 2015;93:17–24.
306 INDUSTRIAL BIOTECHNOLOGY D E C E M B E R 2 0 1 8
63. Bilal M, Asgher M, Iqbal M, et al. Chitosan beads immobilized manganese
peroxidase catalytic potential for detoxification and decolorization of textile
effluent. Int J Biol Macromol 2016;89:181–189.
64. Vigneswaran C, Ananthasubramanian M, Kandhavadivu P, et al. Enzymes in
textile effluents. In: C. Vigneswaran, M. Ananthasubramanian, P. Kandhavadivu,
ed. Bioprocessing of Textiles. India: WPI 2014:251–298.
65. Khouni I, Marrot B, Moulin P, et al. Decolourization of the reconstituted
textile effluent by different process treatments: Enzymatic catalysis,
coagulation/flocculation and nanofiltration processes. Desalination 2011;
268:27–37.
66. Mohan SV, Prasad KK, Rao NC, et al. Acid azo dye degradation by free and
immobilized horseradish peroxidase (HRP) catalyzed process. Chemosphere
2005;58(8):1097–1105.
67. Karim Z, Adnan R, Husain Q. A b-cyclodextrin-chitosan complex as the
immobilization matrix for horseradish peroxidase and its application for the
removal of azo dyes from textile effluent. Int Biodeterior Biodegrad 2012;72:
10–17.
68. Bilal M, Asgher M, Parra-Saldivar R, et al. Immobilized ligninolytic
enzymes: An innovative and environmental responsive technology to
tackle dye-based industrial pollutants—A review. Sci Total Environ 2017;
576:646–659.
69. Sen SK, Raut S, Bandyopadhyay P, et al. Fungal decolouration and degradation
of azo dyes: A review. Fungal Biol Rev 2016;30:112–133.
70. Sathishkumar P, Mythili A, Hadibarata T, et al. Laccase mediated diclofenac
transformation and cytotoxicity assessment on mouse fibroblast 3T3-L1
preadipocytes. RSC Adv 2014;4(23):116–189.
71. Khouni I, Marrot B, Amar RB. Decolourization of the reconstituted dye bath
effluent by commercial laccase treatment: Optimization through response
surface methodology. Chem Eng J 2010;156 (1):121–133.
72. Wang H, Zhang W, Zhao J, et al. Rapid decolorization of phenolic azo dyes by
immobilized laccase with Fe3O4/SiO2 nanoparticles as support. Ind Eng Chem
Res 2013;52(12):4401–4407.
73. Abadulla E, Tzanov T, Costa S, et al. Decolorization and detoxification of textile
dyes with a laccase from Trametes hirsuta. Appl Environ Microbiol 2000;66(8):
3357–3362.
74. Khlifi R, Belbahri L, Woodward S, et al. Decolourization and detoxification of
textile industry wastewater by the laccase-mediator system. J Hazard Mater
2010;175(1–3):802–808.
75. Moya R, Hernández M, Garcı́a-Martı́n AB, et al. Contributions to a better
comprehension of redox-mediated decolouration and detoxification of azo dyes
by a laccase produced by Streptomyces cyaneus CECT 3335. Bioresour Technol
2010;101(7):2224–2229.
76. Andreu G, Vidal T. Effects of laccase-natural mediator systems on kenaf
pulp. Bioresour Technol 2011;102(10):5932–5937.
77. Qiu W, Zhang W, Chen H. Natural laccase mediators separated from water-
washed solution of steam exploded corn straw by nanofiltration and organic
solvent fractionation. Bioresour Technol 2014;156:368–371.
78. Cañas AI, Camarero S: Laccases and their natural mediators: Biotechnological
tools for sustainable eco-friendly processes. Biotechnol Adv 2010;28(6):694–
705.
79. Zheng F, Cui BK, Wu XJ, et al.Immobilization of laccase onto chitosan beads to
enhance its capability to degrade synthetic dyes. Int Biodeterior Biodegrad
2016;110:69–78.
80. Arica MY, Salih B, Celikbicak O, Bayramoglu G. Immobilization of laccase on
the fibrous polymer-grafted film and study of textile dye degradation by
MALDI-ToF-MS. Chem Eng Res Des 2017;128:107–119.
81. Asgher M, Noreen S, Bilal M. Enhancing catalytic functionality of Trametes
versicolor IBL-04 laccase by immobilization on chitosan microspheres.
Chem Eng Res Des 2017;119:1–11.
82. O’Brien PJ. Peroxidases. Chem Biol Interact 2000;129(1–2):113–139.
 ENZYME TREATMENT FOR TEXTILE PROCESSING

83. Torres E, Bustos-Jaimes I, Le Borgne S. Potential use of oxidative enzymes for Address correspondence to:
the detoxification of organic pollutants. Appl Catal B Environ 2003;46(1):1–15. Ana Paula Serafini Immich
84. Ulson de Souza SMAG, Forgiarini E, Ulson de Souza AA. Toxicity of textile dyes Department of Engineering
and their degradation by the enzyme horseradish peroxidase (HRP). J Hazard Federal University of Santa Catarina
Mater 2007;147(3):1073–1078.
Blumenau campus
85. Monier M, Ayad DM, Wei Y, Sarhan AA. Immobilization of horseradish 2750 João Pessoa St.
peroxidase on modified chitosan beads. Int J Biol Macromol 2010;46(3):324–
330.
Blumenau SC
89036-002
86. Sun H, Jin X, Long N, Zhang R. Improved biodegradation of synthetic azo dye by Brazil
horseradish peroxidase cross-linked on nano-composite support. Int J Biol
Macromol 2017;95:1049–1055. Phone: +5548 3721 3376
87. Bilal M, Iqbal HMN, Hu H, et al. Development of horseradish peroxidase-based
cross-linked enzyme aggregates and their environmental exploitation for
bioremediation purposes. J Environ Manage 2017;188:137–143.
E-mail: ana.immich@ufsc.br
Downloaded by STOCKHOLMS UNIVERSITET from www.liebertpub.com at 01/07/19. For personal use only.

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