Bio-Polishing Concept:

Bio-polishing is a biological process in which the cellulase acts on the surface of the yarn. This enzyme  is a protein with a specific catalytic action upon the 1,4-b-glucosidic bonds of cellulose. The enzyme molecule is more

than a thousand times larger than a water molecule and is therefore too large to penetrate the interior of a cotton

fiber. Thus only 1,4-b-glucosidic bonds which are on or near the surface of the cellulosic fiber are affected. In the reaction, small fibrils protruding from the cotton fiber surface are weakened. They then easily break off from the surface, making it much smoother than before.

The smoothing effect has several benefits: The fiber will have a lesser predisposition towards forming pills and

will consequently have a clearer surface structure containing less fuzz. Handling, drapability and water absorbency

will also be improved. Furthermore, these changes in the fabric’s appearance are long lasting because the Cellulase treatment actually modifies the fiber itself, rather than just coating the surface. Since it is a cellulase, it will function on

all cotton substrates such as viscose, flax and ramie, as well as parts of mixed fibers and yarns.

Tri-Cellulase BP-99

Description: Tri-cellulase BP-99 is a cellulase produced by submerged fermentation of a Trichoderma microorganism.

Application: Tri-cellulase BP-99 is used for Bio-Polishing. Bio-Polishing is a novel enzymatic process for finishing of cellulosic fabrics in which the enzyme performs a controlled hydrolysis of the cellulosic fibers in order to modify  the  fabric  surface. Bio-Polishing has a lasting effect on knitted as well as woven fabrics, giving improved resistance to pilling, a clearer, lint-free and fuzzless surface structure, and improved drapability and softness.

Pigment Dyed Fabric

Bio -Polished with Tri-Cellulase BP-99

Bio-Polishing Procedure:

using

Tri-Cellulase BP-99

· Set the bath at 135°F

· Add 0.25 % (owg)  Tissuwet P-100

· Circulate for 5 minutes

· Add  1 g/l. Jean buffer AC-50 conc.

(pH 5)

· Circulate for 5 minutes

Add 2.0 % (owg) Tri-Cellulase BP-99 Run for 20 - 30 minutes

Drop

Fill and set the temperature to 120°F Add 0.5 % (owg) Soda Ash

Heat to  180°F

Run for 5 minutes

Drop

Fill / Rinse

Drop

Related posts:

What is Enzyme Wash:

Enzyme washing is a laundering processes which uses enzymes to clean clothing or to finish fabric, especially in the case of jeans and other garments with a worn-in look. Various enzymatic cleaners are available from stores which specialize in laundry supplies, and can also be special ordered. For regular cleaning, enzymes carry numerous economic and environmental benefits. On an industrial scale, enzyme washing has replaced laborious laundering techniques such as stonewashing, saving money and environmental impact for companies.

What Is Enzyme:

Enzymes are proteins produced by living organisms. All organisms produce a wide range of enzymes to accomplish necessary biological tasks. Some enzymes can also be replicated in the lab, or engineered to perform in a particular way. One of the reasons that enzyme washing is so ecologically friendly is the natural origins of enzymes, which biodegrade, rather than lingering in the water supply. Enzyme washing products are also much more potent than other laundry products, requiring people to use far less, in terms of volume.

Different types of enzymes are suitable for different stains. In all cases, the enzyme washing process breaks the stain down into smaller molecules which can be removed with water or conventional soap. Amylases will remove starch based laundry stains, while proteases break down protein chains, making them suitable for protein stains. Lipases work very well on grease and oil, and cellulases are excellent general cleaners. Enzyme washing also yields a softer, more supple garment.

For delicate garments, enzyme washing can be an excellent way to get clothing fresh and clean. Enzymes also work at very low temperatures, making them suitable for cold wash only things ranging from silk to wet suits. Many natural detergent products mix enzymes into their formulas, to ensure that they are effective at all temperatures and on all stains.

Published on : Aug, 3,2010

Distributors needed for a reputed company, Refnol Resins & chemicals Ltd. Manufacture of textile sizing chemicals, fabric processing chemicals, laundry chemicals & cleaning chemicals is looking for distributors, channel partner.

TEXTILE ENZYMES PRODUCT DESCRIPTION RENZYME SP 20* Highly concentrated Acid Cellulase Powder Enzyme for Denim Garment finishing ECOZYME AP* Acid Cellulase Powder Enzyme for Denim Garment Finishing RENZYME 400 NP* Neutral Cellulase Powder Enzyme for finishing of Denim and other cotton Garments. ECOZYME NP* Neutral Cellulase Powder Enzyme for finishing of Denim and other cotton

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Office Tel no. 28054400Website : http://www.refnol.com

Enzymes for Detergent

For most people, the most popular known application of enzymes is in the manufacture of enzymatic washing agents (detergents). Since last 40 years, the use of enzymes in detergents has been the largest of all enzyme applications. Consumers of detergents are actual users of an enzymatic product. In majority of other applications, enzymes are used as auxiliary agents at

some point in the manufacturing process and are not, as a rule, present in the finished product - not at any rate in an active form.

Proteases

Proteases are the most widely used enzymes in the detergent industry. They remove protein stains such as grass, blood, egg and human sweat.

These organic stains have a tendency to adhere strongly to textile fibres. The proteins act as glues, preventing the waterborne detergent systems from removing some of the other components of the soiling, such as pigments and street dirt.

The inefficiency of nonenzymatic detergents at removing proteins can result in permanent stains due to oxidation and denaturing caused by bleaching and drying. Blood, for example, will leave a rustcoloured spot unless it is removed before bleaching.

Proteases hydrolyse proteins and break them down into more soluble polypeptides or free amino acids. As a result of the combined effect of surfactants and enzymes, stubborn stains can be removed from fibres.

Lipases

Though enzymes can easily digest protein stains, oily and fatty stains have always been troublesome to remove. The trend towards lower washing temperatures has made the removal of grease spots an even bigger problem. This applies particularly to materials made up of a blend of cotton and polyester. The lipase is capable of removing fatty stains such as fats, butter, salad oil, sauces and the tough stains on collars and cuffs.

Amylases

Amylases are used to remove residues of starch-based foods like potatoes, spaghetti, custards, gravies and chocolate. This type of enzyme can be used in laundry detergents as well as in dishwashing detergents.

Cellulases

The development of detergent enzymes has mainly focused on enzymes capable of removing stains. However, a cellulase enzyme has properties enabling it to modify the structure of cellulose fibre on cotton and cotton blends. When it is added to a detergent, it results into the following effects:

Colour brightening-When garments made of cotton or cotton blends have been washed several times, they tend to get a 'fluffy' look and the colours become duller. This effect is due to the formation of microfibrils that become partly detached from the main fibres. The light falling on the garment is reflected back to a greater extent giving the impression that the colour is duller. These fibrils, however, can be degraded by the cellulase enzyme, restoring a smooth surface to the fibre and restoring the garment to its original colour.

Softening-The enzyme also has a significant softening effect on the fabric, probably due to the removal of the microfibrils.

Soil removal-Some dirt particles are trapped in the network of microfibrils and are released when the microfibrils are removed by the cellulase enzyme.

Maps offers a range of protease and lipase for various detergent applications.

Palkogent Alkaline protease for removal of protein stains, which works in alkaline pH conditions

PalkolipaseAlkaline lipase for removal of fatty and oil stains, which works in alkaline pH conditions

At Maps, a project is already underway to develop an alkaline cellulase for the detergent application.

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. 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 recognised and enzymes have been used throughout history, it was quite recently that their importance were realised. 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 gelatinised 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'.

What are Enzymes?

Enzymes are proteins and biocatalyst

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, trypsin 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.

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 specialised part(s) of the enzyme will catalyse 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, oxidising and reducing, synthesising, transferring, lytic and isomerising. 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.

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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 fertiliser.

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Enzymes and industrial applications:

Maps produces industrial enzymes 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 fertiliser. The enzymes are then, used for various industrial applications.

Enzymes for Textile:

At Maps, we continuously develop our product line in order to have innovative enzymes with unique performance 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.

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 (desizing) 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.

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

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Bio-Polishing

Cotton and other natural fibres based on cellulose can be improved by an enzymatic treatment known as BioPolishing. This treatment gives the fabric a smoother and glossier appearance. The treatment is used to remove 'fuzz' - the tiny strands of fibre that protrude from the surface of yarn. A ball of fuzz is called a 'pill' in the textile trade. After BioPolishing, the fuzz and pilling are reduced. The other benefits of removing fuzz are a softer and smoother handle, and superior colour brightness.

Maps offers a range of cellulases for bio-polishing which work on depending on fibre, fabric type and equipments.

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

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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.

Palkowash Cellulase for bio-stonewashing denims used in garment wet-processing

Palkostone Cellulase for bio-stonewashing denims used in garment wet-processing

Palkocel Cellulase for bio-stonewashing denims used in garment wet-processing

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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 cleanup 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.

PalkoperoxCatalase for bleach clean-up i.e. removal residual hydrogen peroxide after the bleaching of cotton.

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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 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.

Proteinaceous inhibitors of endo-beta-glucanases.

William S York, Qiang Qin, Jocelyn K C Rose

Department of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, 220 Riverbend Road, Athens, GA 30602-4712, USA.

Both plants and filamentous phytopathogens secrete proteins that inhibit endo-beta-glucanases. The first endo-beta-glucanase inhibitor proteins to be discovered are XEGIP, a tomato protein that inhibits fungal xyloglucan-specific endo-beta-1,4-glucanases, and GIP1, an oomycete protein that inhibits endo-beta-1,3-glucanases produced by the plant host. These inhibitor proteins act by forming high-affinity complexes with their endoglucanase ligands. A family of XEGIP-like proteins has been identified. At least one member of this family (extracellular dermal glycoprotein, EDGP) has been shown to have

endoglucanase-inhibitor activity, while other members have sequence similarity to a xylanase inhibitor from wheat (TAXI-1). The oomycete inhibitor GIP1 is a catalytically inactive serine protease homolog (SPH) whose structure is unrelated to XEGIP. Both types of inhibitor proteins are likely to affect the interactions of plants with filamentous phytopathogens, and a basic model describing their roles in pathogenesis is proposed.

Most cited papers:

Gene. 1989 Sep 1;81 (1):83-95 2806912 Cit: 115

Cellulase families revealed by hydrophobic cluster analysis.

B Henrissat, M Claeyssens, P Tomme, L Lemesle, J P Mornon

Centre de Recherches sur les Macromolécules Végétales, CNRS, Grenoble, France.

The amino acid sequences of 21 beta-glycanases have been compared by hydrophobic cluster analysis. Six families of cellulases have been identified on the basis of primary structure homology:(A) endoglucanases B, C and E of Clostridium thermocellum; endoglucanases of Erwinia chrysanthemi and Bacillus sp.; endoglucanase III of Trichoderma reesei; endoglucanase I of Schizophyllum commune;(B) cellobiohydrolase II of T. reesei; endoglucanases of Cellulomonas fimi and Streptomyces sp;(C) cellobiohydrolases I of T. reesei and of Phanerochaete chrysosporium; endoglucanase I of T. reesei;(D) endoglucanase A of C. thermocellum and an endoglucanase from Ce. uda;(E) endoglucanase D of C. thermocellum and an endoglucanase from Pseudomonas fluorescens;(F) xylanases of C. thermocellum and of Cryptococcus albidus and the cellobio-hydrolase of Ce. fimi. For each family, conserved potentially catalytic residues have have been listed and previous allocations of the active-site residues are evaluated in the light of the alignment of the amino acid sequences. A strong homology is also reported for the putative cellulose-binding domains of cellulases of Ce. fimi and of P. fluorescens.

Microbiol Rev. 1991 Jun ;55 (2):303-15 1886523 Cit: 103

Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families.

N R Gilkes, B Henrissat, D G Kilburn, R C Miller Jr, R A Warren

Department of Microbiology, University of British Columbia, Vancouver, Canada.

Several types of domain occur in beta-1, 4-glycanases. The best characterized of these are the catalytic domains and the cellulose-binding domains. The domains may be joined by linker sequences rich in proline or hydroxyamino acids or both. Some of the enzymes contain repeated sequences up to 150 amino acids in length. The enzymes can be grouped into families on the basis of sequence similarities

between the catalytic domains. There are sequence similarities between the cellulose-binding domains, of which two types have been identified, and also between some domains of unknown function. The beta-1, 4-glycanases appear to have arisen by the shuffling of a relatively small number of progenitor sequences.

FEMS Microbiol Rev. 1994 Jan ;13 (1):25-58 8117466 Cit: 35

The biological degradation of cellulose.

P Béguin, J P Aubert

Unité de Physiologie Cellulaire, Département des Biotechnologies, Institut Pasteur, Paris, France.

Cellulolytic microorganisms play an important role in the biosphere by recycling cellulose, the most abundant carbohydrate produced by plants. Cellulose is a simple polymer, but it forms insoluble, crystalline microfibrils, which are highly resistant to enzymatic hydrolysis. All organisms known to degrade cellulose efficiently produce a battery of enzymes with different specificities, which act together in synergism. The study of cellulolytic enzymes at the molecular level has revealed some of the features that contribute to their activity. In spite of a considerable diversity, sequence comparisons show that the catalytic cores of cellulases belong to a restricted number of families. Within each family, available data suggest that the various enzymes share a common folding pattern, the same catalytic residues, and the same reaction mechanism, i.e. either single substitution with inversion of configuration or double substitution resulting in retention of the beta-configuration at the anomeric carbon. An increasing number of three-dimensional structures is becoming available for cellulases and xylanases belonging to different families, which will provide paradigms for molecular modeling of related enzymes. In addition to catalytic domains, many cellulolytic enzymes contain domains not involved in catalysis, but participating in substrate binding, multi-enzyme complex formation, or possibly attachment to the cell surface. Presumably, these domains assist in the degradation of crystalline cellulose by preventing the enzymes from being washed off from the surface of the substrate, by focusing hydrolysis on restricted areas in which the substrate is synergistically destabilized by multiple cutting events, and by facilitating recovery of the soluble degradation products by the cellulolytic organism. In most cellulolytic organisms, cellulase synthesis is repressed in the presence of easily metabolized, soluble carbon sources and induced in the presence of cellulose. Induction of cellulases appears to be effected by soluble products generated from cellulose by cellulolytic enzymes synthesized constitutively at a low level. These products are presumably converted into true inducers by transglycosylation reactions. Several applications of cellulases or hemicellulases are being developed for textile, food, and paper pulp processing. These applications are based on the modification of cellulose and hemicellulose by partial hydrolysis. Total hydrolysis of cellulose into glucose, which could be fermented into ethanol, isopropanol or butanol, is not yet economically feasible. However, the need to reduce emissions of greenhouse gases provides an added incentive for the development of processes generating fuels from cellulose, a major renewable carbon source.

Protein Sci. 1992 Oct ;1 (10):1293-7 1303748 Cit: 28

Specificity mapping of cellulolytic enzymes: classification into families of structurally related proteins confirmed by biochemical analysis.

M Claeyssens, B Henrissat

Laboratorium voor Biochemie, Faculteit Wetenschappen, Rijksuniversiteit, Gent, Belgium.

The specificities of 15 cellulolytic enzymes have been examined using chromophoric glycosides derived from D-glucose, cellobiose, higher cellooligosaccharides, lactose, D-xylose, and beta-(1,4)-xylobiose. Coinciding with a classification based on hydrophobic cluster analysis of amino acid sequences, six families each showing a characteristic specificity pattern were observed. Furthermore, in these cases where the anomeric forms of reaction products were determined, results seem to indicate conservation of intrinsic reaction mechanism (single or double displacement) within each family. On the other hand, the low molecular weight substrates do not discriminate exo- from endocellulases. This functional differentiation is speculated to originate from the presence, in exoenzymes, of a tunnel-shaped active site formed by extra loops in their structure.

J Mol Biol. 2001 Dec 7;314 (4):797-806 11733998 Cit: 23

Recognition of cello-oligosaccharides by a family 17 carbohydrate-binding module: an X-ray crystallographic, thermodynamic and mutagenic study.

V Notenboom, A B Boraston, P Chiu, A C Freelove, D G Kilburn, D R Rose

Protein Engineering Networks of Centres of Excellence, University of British Columbia, Vancouver, Canada.

The crystal structure of the Clostridium cellulovorans carbohydrate-binding module (CBM) belonging to family 17 has been solved to 1.7 A resolution by multiple anomalous dispersion methods. CBM17 binds to non-crystalline cellulose and soluble beta-1,4-glucans, with a minimal binding requirement of cellotriose and optimal affinity for cellohexaose. The crystal structure of CBM17 complexed with cellotetraose solved at 2.0 A resolution revealed that binding occurs in a cleft on the surface of the molecule involving two tryptophan residues and several charged amino acids. Thermodynamic binding studies and alanine scanning mutagenesis in combination with the cellotetraose complex structure allowed the mapping of the CBM17 binding cleft. In contrast to the binding groove characteristic of family 4 CBMs, family 17 CBMs appear to have a very shallow binding cleft that may be more accessible to cellulose chains in non-crystalline cellulose than the deeper binding clefts of family 4 CBMs. The structural differences in these two modules may reflect non-overlapping binding niches on cellulose surfaces.

J Bacteriol. 2000 Sep ;182 (17):4915-25 10940036 Cit: 22

A scaffoldin of the Bacteroides cellulosolvens cellulosome that contains 11 type II cohesins.

S Y Ding, E A Bayer, D Steiner, Y Shoham, R Lamed

Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.

A cellulosomal scaffoldin gene, termed cipBc, was identified and sequenced from the mesophilic cellulolytic anaerobe Bacteroides cellulosolvens. The gene encodes a 2,292-residue polypeptide (excluding the signal sequence) with a calculated molecular weight of 242,437. CipBc contains an N-terminal signal peptide, 11 type II cohesin domains, an internal family III cellulose-binding domain (CBD), and a C-terminal dockerin domain. Its CBD belongs to family IIIb, like that of CipV from Acetivibrio cellulolyticus but unlike the family IIIa CBDs of other clostridial scaffoldins. In contrast to all other scaffoldins thus far described, CipBc lacks a hydrophilic domain or domain X of unknown function. The singularity of CipBc, however, lies in its numerous type II cohesin domains, all of which are very similar in sequence. One of the latter cohesin domains was expressed, and the expressed protein interacted selectively with cellulosomal enzymes, one of which was identified as a family 48 glycosyl hydrolase on the basis of partial sequence alignment. By definition, the dockerins, carried by the cellulosomal enzymes of this species, would be considered to be type II. This is the first example of authentic type II cohesins that are confirmed components of a cellulosomal scaffoldin subunit rather than a cell surface anchoring component. The results attest to the emerging diversity of cellulosomes and their component sequences in nature.

J Bacteriol. 2002 Mar ;184 (5):1378-84 11844767 Cit: 21

Cel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome.

Anne Belaich, Goetz Parsiegla, Laurent Gal, Claude Villard, Richard Haser, Jean-Pierre Belaich

Laboratoire de Bioénergétique et Ingenierie des Protéines, IBSM, Centre National de la Recherche Scientifique, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. abelaich@ibsm.cnrs-mrs.fr

A new cellulosomal protein from Clostridium cellulolyticum Cel9M was characterized. The protein contains a catalytic domain belonging to family 9 and a dockerin domain. Cel9M is active on carboxymethyl cellulose, and the hydrolysis of this substrate is accompanied by a decrease in viscosity. Cel9M has a slight, albeit significant, activity on both Avicel and bacterial microcrystalline cellulose, and the main soluble sugar released is cellotetraose. Saccharification of bacterial microcrystalline cellulose by Cel9M in association with two other family 9 enzymes from C. cellulolyticum, namely, Cel9E and Cel9G, was measured, and it was found that Cel9M acts synergistically with Cel9E. Complexation of Cel9M with the mini-CipC1 containing the cellulose binding domain, the X2 domain, and the first cohesin

domain of the scaffoldin CipC of the bacterium did not significantly increase the hydrolysis of Avicel and bacterial microcrystalline cellulose.

Biochim Biophys Acta. 2000 Dec 29;1543 (2):239-252 11150609 Cit: 20

Protein engineering of cellulases.

M Schülein

Novozymes A/S, Smoermosevej 25, DK-2880, Bagsvaerd, Denmark. mas@novozymes.com

Cellulases are enzymes which hydrolyse the beta-1,4-glucosidic linkages of cellulose. They fall into 13 of the 82 glycoside hydrolase families identified by sequence analysis, but they are traditionally divided into two classes termed 'endoglucanases'(EC 3.2.1.4) and 'cellobiohydrolases'(3.2.1.91). Both types of cellulases degrade soluble cellodextrins and amorphous cellulose but, with a few notable exceptions, it is only the cellobiohydrolases which degrade crystalline cellulose efficiently. Site-directed mutagenesis has been central to the characterisation of cellulases, ranging from the identification and characterisation of putative catalytic and binding residues, the trapping of enzyme-substrate complexes by crystallography through to the construction of new and improved biocatalysts including 'glycosynthases'. Whilst studies on soluble substrates and substrate analogues have provided a wealth of information, understanding the mechanism of degradation of the natural substrate, crystalline cellulose, remains a great challenge.

Syst Appl Microbiol. 2000 Dec ;23 (4):479-86 11249017 Cit: 13

Partial sequencing of the hrpB and endoglucanase genes confirms and expands the known diversity within the Ralstonia solanacearum species complex.

S Poussier, P Prior, J Luisetti, C Hayward, M Fegan

Laboratoire de Phytopathologie, Centre de Cooperation Internationale en Recherche Agronomique pour le Developpement, Saint-Pierre, La Reunion, France.

We determined partial hrpB and endoglucanase genes sequences for 30 strains of Ralstonia solanacearum and one strain of the blood disease bacterium (BDB), a close relative of Ralstonia solanacearum. Sequence comparisons showed high levels of variability within these two regions of the genome involved in pathogenicity. Phylogenetic analysis based upon sequence comparisons of these two regions revealed three major clusters comprising all Ralstonia solanacearum isolates, the BDB strain constituted a phylogenetically distinct entity. Cluster 1 and cluster 2 corresponded to the previously defined divisions 1 and 2 of Ralstonia solanacearum. Moreover, two subclusters could be identified within cluster 2. The last cluster, designated cluster 3 in this study, included biovar 1 and N2 strains

originating from Africa. This recently described group of strains was confirmed to be clearly different from the other strains suggesting a separate evolution from those of both divisions 1 and 2.

Cell Mol Life Sci. 2002 Sep ;59 (9):1554-60 12440775 Cit: 12

Cellulase genes from the parabasalian symbiont Pseudotrichonympha grassii in the hindgut of the wood- feeding termite Coptotermes formosanus.

K I Nakashima, H Watanabe, J I Azuma

Cellulase genes of Pseudotrichonympha grassii (Hypermastigida: Eucomonymphidae), the symbiotic flagellate in the hindgut of the wood-feeding termite Coptotermes formosanus, were isolated and characterized. The nucleotide sequences of the major cellulase component in the hindgut of C. formosanus were determined based on its N-terminal amino acid sequence. The five isolated nucleotide sequences (PgCBH-homos) had an open reading frame of 1350 bp showing similarity to catalytic domains of glycoside hydrolase family (GHF) 7 members, and primary structure comparison with GHF7 members whose tertiary structures are well-characterized revealed the overall similarity between PgCBH-homo and the catalytic domain of a processive cellulase Cel7A (formerly CBHI) from the aerobic fungus Trichoderma reesei. Functional expression of PgCBH-homos in Escherichia coli, using the carboxymethylcellulose-Congo red assay, demonstrated the actual cellulolytic activity of PgCBH-homo. RT-PCR showed that PgCBH-homos were expressed, from the three flagellates in the hindgut, specifically in P. grassii.

Stonewash Effect:

In traditional washing process, volcanic rocks or pumice stones are added to the garments during washing as abradant. Due to ring dyeing and heavy abrasion fading is more apparent but less uniform.

The degree of colour fading depends on the garment to stone ratio, washing time, size of stones, material to liquor ratio and load of garments. Normally after desizing, stone wash process starts with pumice stone addition in rotary drum type garment washer. Process time varies from 60-120 mins.

Stone wash effect is one of the oldest but highly demanded washing effects. Stone wash process gives “used” look or “vintage” on the garments, because of varying degree of abrasion in the area such as waistband, pocket, seam and body.

There are many limitations and drawbacks associated with stone washing process, which can be overcome by using new enzyme based washing technology. This technology also helps to conserve water, time, energy and environment.

Enzyme Wash

Cellulase enzymes are natural proteins which are used in denim garment processing to get stone wash look on to the denim garments without using stones or by reducing the use of pumice stone.

Cellulase attacks primarily on the surface of the cellulose fibre, leaving the interior of the fibre as it is, by removing the indigo present in the surface layer of fibre.

Cellulase enzyme is classified into two classes:

Acid Cellulase: It works best in the pH range of 4.5-5.5 and exhibit optimum activity at 50.

Neutral cellulase: It works best at pH 6 however its activity is not adversely affected in the range of ph 6-8 and show maximum activity at 55 C.

Advantage of enzyme washing

1. Soft handle and attractive clean appearance is obtained without severe damage to the surface of yarn.

2. Inexpensive, low-grade fabric quality can be finished to a top quality product by the removal of hairiness fluff and pills, etc.

3. Simple process handling and minimum effluent problem.4. Better feel to touch and increased gloss or luster.5. Prevents tendency of pilling after relatively short period of wear.6. Can be applied on cellulose and its blend.7. Due to mild condition of treatment process is less corrosive.8. Fancy colour-flenced surface can be obtained without or a partial use of stone.9. More reproducible effect can be obtained.10. It allows more loading of the garment into machines.11. Environmental friendly treatment.12. Less damage to seam edges and badges.13. Wear and tear of equipment is minimum due to absence of stone.14. Use of softener can be avoided or minimised.15. Easy handling of floor and severs as messy sludge of stones does not interfere.16. Due to absence of stone, labour intensive operation of stone removal is not required.17. Homogenous abrasion of the garments.18. Puckering effect can also be obtained.19. Problem of pumice powder contamination on garment is not there.

Enzymatic anti-backstaining agent-protease:

The use of an engineered oxidatively stable alkaline protease that can tolerate a range of operating temperature and pH conditions offers flexible and alternative processes for backstaining clean-up, improved contrast of denim finishes, and reduced residual cellulase of fabric.

It is claimed that significant reduction in backstaining can be achieved at much lower temperature than conventional process by using small amount of protease either at the end of the cellulase washing step or during the rinsing step. By adding the protease at the end of the cellulase wash step, one rinse step is eliminated offering savings in time and energy. This process at lower temperature also claims to achieve a significant reduction of residual cellulase.

CELLULASE WASH :

Cellulase enzymes have gained acceptance in the garment wash industry as a means to achieve a washdown appearance

without the use of stones or with reduced quantities of stones. These enzymes are different from the alpha amylase enzymes

used for starch removal in that they are selective only to the cellulose and will not degrade starch. Under certain conditions,

their ability to react with cellulose (cotton) will result in surface fiber removal (weight loss). This will give the garments a

washed appearance and soft hand.

PROCEDURE 1. Load stones in machine (normally 0.5 - 2.0 part weight stones: 1 part weight garments) if applicable. 2. Load garments. 3. Desize with alpha amylase enzyme and detergent. 4. Rinse. 5. Add cellulase enzyme (amount, pH, temperature, and cycle time dependent upon type of fabric and desired effects; manufacturer's recommendations should be followed). 6. Adjust pH as recommended. 7. Tumble 30-90 minutes. 8. Drain. *9. Rinse well (70◦C). 10. Drain. 11. Rinse well (70◦C). 12. Drain. Separate garments from stones if used (garments can be transferred to another machine). 13. Apply softener. 14. Extract and unload. 15. De-stone and tumble dry. 16. Press, if required. After step 7, a chlorine bleach may be used as described in STONEWASH WITH CHLORINE.

* The increase in temperature serves to deactivate the cellulase. pH adjustment to 9.0-10.0 with soda ash can also be incorporated. Some operations use both the increases in pH and temperature.

The statements, recommendations and suggestions contained herein are based on experiments and information believed to

be reliable only with

regard to the products and/or processes involved at the time. No guarantee is made of their accuracy, however, and the

information is given without

warranty as to its accuracy or reproducibility either express or implied, and does not authorize use of the information for

purposes of advertisement

or product endorsement or certification. Likewise, no statement contained herein shall be construed as a permission or

recommendation for the use

of any information, product or process that may infringe any existing patents. The use of trade names does not constitute

endorsement of any

product mentioned, nor is permission granted to use the name Cotton Incorporated or any of its trademarks in conjunction

with the products

Cellulase Enzymes

BioPol – Conc.

BioPol – Conc. is a concentrated Cellulase Enzyme. The product is designed to be formulated into products that fill the needs of Fabric and Garment Processors. BioPol – Conc. is used for bio-polishing of cellulosic fabric under acidic conditions. It partially digests excess and protruding yarns, loosening them from the fabric. The resulting fuzz is then easily removed by mechanical agitation of the fabric. This not only creates a smoother fabric with resistance to pilling, but also improves softness, luster and drape. 

 

BioPol – Conc. offers the following benefits:

Specific action on protruding fibers only. Improves texture, softness and appearance of fabric. Wide variety of application processes. Eco-friendly & Biodegradable.

 

CHARACTERISTICS & PROCESSING PARAMETERS:

 

Appearance Liquid

Color Brown

Operative pH range 4.5 - 5.7

Operative Temperature range 40°C - 60°C

Solubility Soluble in water

 

 

 

 

BioFade – Conc.

BioFade – Conc. is a concentrated Cellulase Enzyme. The product is designed to be formulated in to products that fill the needs of Garment Processors.

BioFade – Conc. partially digests excess and protruding yarns, loosening them from the fabric.

The fading effect is obtained by homogenous removal of the indigo dye trapped inside the fibers by the cooperative action of enzymatic hydrolysis and mechanical agitation of the fabric. This improves softness, luster and drape.

 

BioFade – Conc. offers the following benefits:

Improves texture, softness and appearance of fabric. Excellent fading effect with clear fabric surface. No damage to strength of fabric.

Wide variety of application processes. Eco-friendly & Biodegradable.

CHARACTERISTICS:

Appearance Liquid

Color Brown

Operative pH range 4.5 - 5.5

Operative Temperature range 50°C - 55°C

Solubility Soluble in water

Payment Terms: L/C (Letter of Credit), T/T (Bank Transfer)Port of Dispatch: KolkataProduction Capacity: 10 Tons/MonthDelivery Time: Dispatch within 7-10 DaysPackaging Details: 25 KG, 50 KG

Texel BPF 18 is a fungal cellulase enzyme preparation for bio-polishing.

Characteristics

Texel BPF 18 has the following characteristics:

Characteristics Physical form LiquidAppearance Light brown colourOdour Yeast likepH 4.8-.5.2

Working Parameters

Texel BPF 18 operates best under the following parameters:

Parameters Optimal rangeOperational rangeTemperature

55°C-60°C 50°C-65°C

pH 4.55.5 4.56.0

Application

Texel BPF 18 should be used on fabric and garment finishing processes for bio-polishing. It is especially used on woven as well as knitted fabric and garment made from fibres like, cotton and its blends, flax and ramie. Texel BPF 18 gives permanent improvement in fabric quality by reducing fuzz and pilling to give soft and smooth hand feel, without damaging the fabric and garment.

Texel BPF 18 replaces the conventional use of chemicals, giving better gloss / lustre, colour brightening with improved hand feel.

Texel BPF 18 is a ready-to-use formulation of enzyme, stabiliser and surfactants for high performance bio-polishing.

Wetting agents and non-ionic detergents can be used with Texel BPF 18 to enhance penetration.

Advantages

q       Provides efficient bio-polishing for fabric and garment

q       Provides surface polishing and softening

q       Minimum weight reduction and damage to the fabric and garment

q       Reduces fuzz and pilling

q       Improves softness and smoothness

q       Improves hand feel

q       Increases gloss / lustre and colour brightening

q       Efficient and specific in action

q       Reduces process cycle time

q       Easy to dispense and disperse in the wash

q       100% Eco-friendly and bio-degradable

Usage Guidelines

There are many factors that influence bio-polishing with Texel BPF 18, such as:

q       Type and construction of fabric

q       Quality and type of cellulosic content of fabric

q       Temperature and pH of the process

q       Process cycle time

q       Efficiency of pre-treatment process

q       Type of equipment

q       Type of mechanical action

Storage

Texel BPF 18 should be stored in a cool dry place.  When stored below 30°C Texel BPF 18 will maintain its declared activity for atleast six months.

 

Packaging

Texel BPF 18 is available in 35 kg jerry can.

Product Name : SUKACell-L1000 Acid Cellulase for Bio-polishingItem  : 11476-467Model : Last update : 2010.04.20SUKACell-L1000

Acid Cellulase for Bio-polishing

 INTRODUCTION: Cellulose is an unbranched glucose polymer composed of anhydro-D-glucose units linked by 1, 4-b-D-glucoside bonds. These glycosidic bonds can be hydrolysed by cellulolytic enzymes. The native structure of the cellulose is composed of crystalline and less organized amorphous regions. SUKACell-L1000 is an enzyme preparation obtained from the submerged fermentation of a high cellulase-producing microbial strain. It is widely used in textile and garment stone wash industries.WORKING MECHANISM:The 1, 4-b-D-glucosidic linkages in cellulose, lichenin and cereal b-D glucans are hydrolyzed to release free glucose units through the successive action of cellulase enzymes.The less organized amorphous region at the center of the cellulose chain is initially attacked by endoglucanase by random cutting of the b-1, 4 glycosidic linkages within the chain thereby producing cello-oligosaccharides. Cellobiohydrolases I and II act on the cello-oligosaccharides from the reducing end and non-reducing end of the cello-oligosaccharides to release cellobiose. b- glucosidase act on the released cellobiose to produce b–D glucose units.PROPERTIES:SUKACell-L1000 will function from a pH of 4.5 to 6.0 with pH 4.8 as an optimum. It will function from 40℃ to 60℃。 Appearance: Medium to dark amber liquid (Note that color does not affect or reflect activity.) Odor: Slight fermentation odorpH (as is)：4.5±1.0；Density：1.05-1.20SPECIFICATION:SUKACell-L1000 (activity is 10000 U/ml)High activity product is available upon request of our customers.ENZYME ACTIVITY UNIT DEFINITION:Reducing sugar method: At a pH of 4. 8 and temperature of 50 ℃, to produce the amount of reducing sugar equivalent to 1 mg glucose, it needs l g solid enzyme (or 1mL liquid enzyme) and 1 h hydrolyze sodium carboxymethyl cellulose substrate, as 1 enzyme activity unit, state as u/g (or u/mL). CMCA – DNS for short. EXECUTION STANDARD:Light industry standard of the People's Republic of China, QB 2583 2003USAGE:Ø        SUKACell-L1000 - is a kind of acidic liquid cellulase, used for biofinishing, significantly soften 100% cotton fabrics, both woven and knits.Ø        SUKACell-L1000 – provide soft touch except used for jean leaven dye processing.Ø        SUKACell-L1000 - can obviously improve clothing surface magnitude.OPERATION & DOSAGE:

    OPERATION DOSAGE

Biofinishing Stonewashing

Desize thoroughly Desize thoroughly Desize thoroughlyDrain liquor then fill machine

to liquor ratio of1：10 (jean/ water) 1：10 (jean/ water)

Add pumice (if required), heat 40-60℃ 50-60℃

bath toAdd SUKACell-L1000

at the rate of0.25-2.0% owg 0.25-0.75% owg

Adjust pH to4.5-5.5，with pH 4.8 as an

optimum4.5-5.5，with pH 4.8 as an

optimum

Process time20-45 minutes

（depending on desired effect）30-45 minutes

（depending on desired effect）After drainage add water and softening add water and softening

NOTE: Some denim fabrics of lower quality may have severe backstaining problems that can be overcome with our ES resist.Use soda ash 1-3 grams and resist ES 1-2 grams (water ratio) to wash out ferment remaining residue, after that you can adopt our consistent lubricant/ film/ organic silicon oil. The information presented is believed to be accurate. However, said information and products are offered without warranty or guarantee. Sales commitment should pay legal responsibility. We recommend that the prospective user determine the suitability of our materials and suggestions before adopting them on a commercial scale.PACKAGING:SUKACell-L1000 is packaged in 25 kg plastic drum and 1 ton plastic drum for the liquid form.Alternative packaging is available upon request for smaller or larger volumes. STORAGE: Store in a cool, dry place and away from direct sunlight. SUKACell-L1000 maintains its activity for considerably longer time when stored at lower temperatures (below 25℃). Do not let freeze.HANDLING PRECAUTIONS:SUKACell-L1000 is non-toxic and biodegradable. However, unnecessary contact with the product should be avoided. Long term exposure to protein based products such as SUKACell-L1000 may sensitize certain individuals to the product. Wash hands with warm soapy water after handling. Keep out of reach of children.TECHNICAL SERVICE:SUKAHAN (Weifang) Bio-Technology Co., Ltd will assist customers with the use of our products in applications development.