WO2021133302A1 - Encapsulated enzymes and the usage thereof in textile applications - Google Patents

Encapsulated enzymes and the usage thereof in textile applications Download PDF

Info

Publication number
WO2021133302A1
WO2021133302A1 PCT/TR2020/051109 TR2020051109W WO2021133302A1 WO 2021133302 A1 WO2021133302 A1 WO 2021133302A1 TR 2020051109 W TR2020051109 W TR 2020051109W WO 2021133302 A1 WO2021133302 A1 WO 2021133302A1
Authority
WO
WIPO (PCT)
Prior art keywords
enzyme
amylase
catalase
alginate
weight
Prior art date
Application number
PCT/TR2020/051109
Other languages
French (fr)
Inventor
Derya AYDIN
Semih Durmus
Original Assignee
Ak-Kim Kimya Sanayi Ve Ticaret Anonim Sirketi
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Ak-Kim Kimya Sanayi Ve Ticaret Anonim Sirketi filed Critical Ak-Kim Kimya Sanayi Ve Ticaret Anonim Sirketi
Priority to EP20906374.2A priority Critical patent/EP4081680A4/en
Publication of WO2021133302A1 publication Critical patent/WO2021133302A1/en

Links

Classifications

    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
    • D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
    • B01J13/00—Colloid chemistry, e.g. the production of colloidal materials or their solutions, not otherwise provided for; Making microcapsules or microballoons
    • B01J13/02—Making microcapsules or microballoons
    • B01J13/04—Making microcapsules or microballoons by physical processes, e.g. drying, spraying
    • B01J13/046—Making microcapsules or microballoons by physical processes, e.g. drying, spraying combined with gelification or coagulation
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
    • B01J13/00—Colloid chemistry, e.g. the production of colloidal materials or their solutions, not otherwise provided for; Making microcapsules or microballoons
    • B01J13/02—Making microcapsules or microballoons
    • B01J13/06—Making microcapsules or microballoons by phase separation
    • B01J13/14—Polymerisation; cross-linking
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
    • C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
    • C12N11/04—Enzymes or microbial cells immobilised on or in an organic carrier entrapped within the carrier, e.g. gel or hollow fibres
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0065—Oxidoreductases (1.) acting on hydrogen peroxide as acceptor (1.11)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411—Amylases
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
    • C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
    • D06L1/00—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods
    • D06L1/12—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods using aqueous solvents
    • D06L1/14—De-sizing
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M23/00—Treatment of fibres, threads, yarns, fabrics or fibrous goods made from such materials, characterised by the process
    • D06M23/12—Processes in which the treating agent is incorporated in microcapsules
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
    • D06M15/00—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment
    • D06M15/01—Treating fibres, threads, yarns, fabrics, or fibrous goods made from such materials, with macromolecular compounds; Such treatment combined with mechanical treatment with natural macromolecular compounds or derivatives thereof
    • D06M15/03—Polysaccharides or derivatives thereof

Definitions

  • the invention relates to the encapsulated enzymes and the usage thereof in the textile applications.
  • the invention particularly relates to the amylase, catalase and cellulase enzymes encapsulated by alginate, agar and cyclodextrin and the usage thereof in the textile applications.
  • Enzymes have various applications from textile to food, from pharmaceuticals, to detergents and biofuels, and in industry and biotechnology fields. Enzymes are molecules in protein structure and are designed so as to work in biological environments in the nature. Amino acid chains determine the three-dimensional shape, conformation and function of the enzymes. The high temperature, oxidizing agents, high acidity and alkalinity that the enzymes are exposed to in the industrial applications cause their denaturation due to disruption of their three dimensional structures and decrease in their activities. This circumstance prevents efficient and long term usage of the enzymes. For this reason, continuing the enzyme activity by maintaining the stability of the enzymes is one of the most important aspects in the enzyme applications.
  • amylase Among the enzymes widely used in the textile field, we can list amylase, cellulase, catalase, protease, peroxidase, lipase and laccase. Among these enzymes, amylase, catalase and cellulase are the most commercially produced enzymes.
  • Amylase enzyme is used as a desizing enzyme and provides the removal of the sizing by decomposing the starch and its derivatives in cotton products into water-soluble dextrin form.
  • the catalase enzyme removes the hydrogen peroxide residues that may be harmful before the dyeing process by decomposing the hydrogen peroxide in the environment.
  • Cellulase enzyme is used to remove the feather of cellulosic fabrics and blends such as cotton, viscose, linen, etc. and to positively affect the touching in the completion processes.
  • These enzymes are prepared in a solution in the conventional textile products and applied to the fabric by exhaust, bleaching and foulard method according to the aim of use. These applications are performed at temperatures between 30 and 95C° and at different pH values. The high temperatures where the applications can reach cause the structures of the enzymes to deteriorate and denature and to lose their activity.
  • Enzymes are produced in the form of formulations containing sorbitol, glycerol, sugar, salt and various wetting agents that are prepared in aqueous medium in the available commercial products.
  • the enzyme cannot remain stable sufficiently in these products, their activities decrease during storage and textile applications. For this reason, the shelf life of textile products containing enzymes can vary between 3 and 6 months and can be 1 year at maximum.
  • Kumar R Entrapment of a-amylase in alginate beads: Single step protocol for purification and thermal stabilization; it is disclosed that a-amylase is encapsulated by alginate and its thermal stability is increased.
  • the present invention relates to processes that fulfill the abovementioned requirements and bring some additional advantages for encapsulation of an enzyme selected from amylase, cellulase and catalase with one selected from alginate, agar and cyclodextrin and relates to the use of encapsulated amylase, encapsulated cellulase and encapsulated catalase obtained from these processes in the textile applications.
  • the main aim of the invention is to provide processes that increase enzyme performance for use in textile applications.
  • the main aim of the invention is to provide processes that increase enzyme activity for use in textile applications.
  • Another aim of the invention is to provide processes for increasing enzyme stability and shelf life for use in textile applications.
  • the present invention provides a process for producing alginate beads by encapsulation with alginate of an enzyme selected from amylase, cellulase and catalase.
  • said process comprises a step of adding at least one of said enzymes to the aqueous sodium alginate solution.
  • concentration of said sodium alginate solution is in the range of 0.25-2.00% by weight.
  • concentration of said sodium alginate solution is 1 ,0 % by weight.
  • said process comprises the step of dropping an aqueous sodium alginate solution containing enzyme into a solution containing calcium chloride so as to obtain calcium alginate beads.
  • molarity of calcium chloride in said calcium chloride solution is 0,1-1 ,0 M.
  • molarity of calcium chloride in said calcium chloride solution is 0,2M.
  • said enzyme is amylase.
  • the concentration of amylase in sodium alginate solution is 3-20% by weight.
  • the concentration of amylase in sodium alginate solution is 5-8% by weight.
  • said enzyme is catalase.
  • the concentration of catalase in sodium alginate solution is 1-5% by weight.
  • the concentration of catalase in sodium alginate solution is 1-2% by weight.
  • said enzyme is cellulase.
  • the concentration of cellulase in sodium alginate solution is 5-20% by weight.
  • the concentration of cellulase in sodium alginate solution is 10-15% by weight.
  • the present invention provides the use of an enzyme encapsulated with alginate in textile applications, and said enzyme is selected from a-amylase, cellulase and catalase.
  • said enzyme is amylase and said textile application is desizing application.
  • said enzyme is catalase and said textile application is antiperoxide enzyme application.
  • said enzyme is cellulase and said textile application is anti-pilling application.
  • Amylase enzyme is used as a desizing enzyme and provides the removal of the sizing by decomposing the starch and its derivatives in cotton products into water-soluble dextrin form.
  • the catalase enzyme removes the hydrogen peroxide residues that may be harmful before the dyeing process by decomposing the hydrogen peroxide in the environment.
  • Cellulase enzyme is used to remove the feather of cellulosic fabrics and blends such as cotton, viscose, linen, etc. and to positively affect the touching in the completion processes.
  • the performances of the amylase, catalase and cellulase enzymes are higher than the conventional solution systems in the above mentioned textile applications. More effective results can be obtained with the present invention by using enzyme with less concentration, and the enzyme is more stable at higher temperatures. Moreover, it is found out that shelf life of the enzyme systems that are prepared by the encapsulation method is longer than the products containing enzyme in free form.
  • Alginate that is obtained from brown algae grown in cold water areas is a linear polysaccharide and consists of b-D-manuronic acid (M) and 1-4 bonds of a-L-gyluronic acid (G). Its composition and sequence along the chain vary. (Zhang and Zhao 2007; Lertsutthiwong et al. 2008). Said polysaccharide is used for the continuous release of agrochemicals after gelation using metal ions. (Fernandez-Perez 2007; Singh et al. 2013; Wlodarczyk and Siwek 2013)The chemical structure of alginate is shown by Formula 1 .
  • Cyclodextrins are complex polysaccharides consisting of glucose units (a-D- glucopyranose) that are combined with a- (1 ,4) bonds. Cyclodextrins that have specific physicochemical properties depending on the extraverted positioning and conical structure of the hydroxyl groups may carry the hydrophobic compounds in the space therein and also may dissolve in aqueous medium (Britto et al. 2004). Cyclodextrins are widely used due to their capacity to form inclusion complexes with a large number of molecules (PerezMartinez et al. 1999; De Carvalho and de Alves Pinto 2012; Morin-Crini and Crini 2013; Higueras et al. 2013; Fernandes et al. 2014; Garrido et al. 2014). The chemical structure of cyclodextrin is shown by Formula 2.
  • Agar is a hydrophilic colloid consisting of agarose and agaropectin mixture.
  • the agarose in the agar constitutes approximately 70% of the agar.
  • Agarose can be used as a matrix to encapsulate the cells.
  • Agarose comprises thermally cross linkable repeating 1 ,3-linked-d- galactose and 1 ,4-linked-3,6-anhydro-a-l-galactopyranose units. (Normand et al., 2000).
  • Agarose can be used for cell encapsulation since it constitutes a double helix structure that is aggregated in the form of thick aggregates after large-diameter intracellular hydrogen bonds are formed (Xiong et al., 2005).
  • agar can be able to form gel in a reversible manner by means of cooling a hot aqueous solution.
  • Agar gel can be melted by heating and can be returned to its original condition by cooling the same.
  • General gel temperature for 1.5% solution of agar is 35-45 C and thus it can form very rigid gels at very low concentrations.
  • the chemical structure of agarose is shown by Formula 3.
  • Enzymes can be encapsulated by encapsulating the same within cyclodextrin, agar, and alginate. Enzymes with different concentrations are added into cyclodextrin; agar and alginate solutions prepared in different concentrations and are encapsulated in the matrix obtained from these molecules by different chemical and physical mechanisms.
  • the present invention provides processes for encapsulation of an enzyme selected from amylase, cellulase and catalase with one selected from alginate, agar and cyclodextrin.
  • Encapsulation with alginate is carried out by ionic crosslinking.
  • Encapsulation with agar is performed physically (melting, setting, freezing) by method of networking.
  • the system has a hydrogel structure in the alginate and agar encapsulation, and the enzyme is made by means of releasing the same through the pores.
  • Encapsulation with cyclodextrin can be performed by loading therein.
  • the present invention provides the use of an enzyme encapsulated with alginate, agar or cyclodextrin in textile applications, the enzyme mentioned here is selected from a- amylase, cellulase and catalase.
  • the enzyme is amylase then said textile application may be desizing application.
  • the enzyme is cellulase then said textile application may be antipilling enzyme application.
  • the enzyme is catalase then said textile application may be antiperoxide.
  • the statement “textile applications” refers to the processes carried out by using enzymes in the textile field.
  • “desizing application” statement refers to the processes in the textile field that are carried out so as to remove the sizing by decomposing the starch and its derivatives in cotton products into water-soluble dextrin form by using amylase enzyme.
  • antiperoxide enzyme application refers to the processes performed in the textile field by using catalase enzyme to remove hydrogen peroxide residues that may be harmful in fabric production before the dyeing process by decomposing the hydrogen peroxide.
  • anti-pilling application refers to the processes that are carried out so as to reduce pilling formation namely to allow the fabric to gain anti-pilling characteristic that is one of important parameters affecting the quality in knit fabric production by means of using cellulase enzyme in the textile field.
  • the present invention provides a process for producing alginate beads by encapsulation with alginate of an enzyme selected from amylase, cellulase and catalase and provides the use of the alginate beads obtained in textile applications.
  • sodium alginate solution containing enzyme is prepared by adding at least one of the enzymes selected from amylase, cellulase or catalase into the sodium alginate solution; and calcium alginate beads containing enzyme or enzymes are obtained by dropping the enzyme-containing sodium alginate solution into a calcium chloride solution.
  • encapsulation with alginate is provided by ionic cross-linking of sodium alginate solution in a medium containing Ca 2+ .
  • said enzyme is amylase.
  • amylase concentration increases, the amylase/alginate ratio in the system also increases and thus the alginate ratio decreases. This causes to obtain softer gel beads with larger pores. Therefore, for example, alginate beads having an amylase concentration of 10% by weight are not as stable as alginate beads with an amylase concentration of 7% by weight, it has a weaker amylase barrier and thus it can protect its amylase activity less.
  • Another important factor is that above a certain concentration of the amylase enzyme, the alginate gel structure can be weakened by partially degrading the same.
  • said enzyme is catalase.
  • concentration of catalase in aqueous sodium alginate solution is 1 -5% by weight with the present invention, it was found that obtained alginate beads exhibited the highest performance in peroxide enzyme application on fabric.
  • concentration of catalase in aqueous sodium alginate solution is 1 -2% by weight.
  • the gel structure in the alginate beads that are obtained with this ratio is not affected. Moreover, this ratio is preferred in terms of its cost.
  • said enzyme is cellulase.
  • concentration of cellulase in aqueous sodium alginate solution is 5-20% by weight with the present invention, it was found that obtained alginate beads exhibited the highest performance in pilling application on fabric.
  • concentration of cellulase in aqueous sodium alginate solution is 10-15% by weight. The gel structure in the alginate beads that are obtained with this ratio is not affected. Moreover, this ratio is preferred in terms of its cost.
  • the concentrations of sodium alginate solution and calcium chloride solution that are used in the inventive process substantially affect the obtained alginate beads.
  • the concentration of said sodium alginate solution is in the range of 0.25-2.0% by weight, preferably 1.0% by weight so as to provide capsules that have proper spherical structure and size distribution and do not adhere to each other.
  • Molarity of calcium chloride in said calcium chloride solution is in the range between 0,1 -1 ,0 M, preferably 0,2 M. Both smooth spherical and equal sized capsules were obtained at these concentrations, and more controlled enzyme release and performance was provided with the obtained gel structure having optimum hardness.
  • Alginate solutions containing enzymes are prepared by adding enzyme with different concentrations according to the enzyme used into the sodium alginate aqueous solutions of 0.25%, 0.5, 1 .0, 1 .5 and 2.0 by weight.
  • the calcium alginate beads were obtained by dropping these solutions into 0,1 , 0,2, 0,3, 0,4, 0,5 and 1 ,0 M of calcium chloride solutions.
  • alginate solutions containing amylase were prepared by adding 7% and 10% of amylase enzyme by weight into 1.0% of sodium alginate aqueous solution by weight.
  • the calcium alginate beads were obtained by dropping these solutions into 0.2 M calcium chloride solutions.
  • Sodium alginate solutions containing amylase enzyme and calcium alginate bead samples were exposed to desizing application at 60C° for 30 minutes so as to test their performances in practice. The obtained results are given in Table 1. Enzyme performances were measured with the TEGEWA test. TEGEWA value changes in direct proportion to enzyme performance. Table 1
  • alginate beads with an enzyme concentration of 7 % by weight according to these results. Therefore, it has been discovered that although alginate beads contain less enzyme, they have an enzyme concentration of 7% by weight, and they achieve better results in the application of desizing.
  • aqueous solutions containing 7% and 10% amylase enzyme were prepared.
  • the aqueous solution containing amylase enzyme was exposed to desizing application at 60C° for 30 minutes so as to test its performance in practice.
  • the obtained results are given in Table 2.
  • Enzyme performances were measured with the TEGEWA test. TEGEWA value changes in direct proportion to enzyme performance.
  • catalase containing alginate solutions were prepared by adding 1.5% and 1.8% of catalase enzyme by weight into 1.0% of sodium alginate aqueous solution by weight.
  • the calcium alginate beads were obtained by dropping these solutions into 0.2 M calcium chloride solutions.
  • Alginate solution containing antiperoxide enzyme and calcium alginate bead samples were subjected to antiperoxide enzyme application so as to test the performance in the application.
  • a bath containing 8 g/lt NaOFI (45%) and 10 g/lt FI2O2 (50%) was prepared, after bleaching was carried out at 98C° for 45 minutes between pH 11-12, the bath was cooled to 45C° and pH was adjusted to 5-5,5. In the next step, it was kept in a bath of 0.35 g/lt for 20 minutes at 45C°.
  • the enzyme activity was determined by measuring the amount of peroxide remaining in the environment at the end of certain periods. The obtained results are given in Table 3.
  • Example 4- Catalase solution Aqueous catalase solutions of 1.8% by weight were prepared for the antiperoxide enzyme application. Aqueous catalase solutions were subjected to antiperoxide enzyme test application so as to test their performances in practice. For this purpose, a bath containing 8 g/lt NaOH (45%) and 10 g/lt H2O2 (50%) was prepared, after bleaching was carried out at 98C° for 45 minutes between pH 11-12, the bath was cooled to 45C° and pH was adjusted to 5-5,5. In the next step, it was kept in a bath of 0.35 g/lt for 20 minutes at 45C°. The catalase activity was determined by measuring the amount of peroxide remaining in the environment at the end of certain periods. The obtained results are given in Table 4.
  • Example 5 Cellulase encapsulated with alginate
  • alginate solutions containing cellulase were prepared by adding 10% and 13.3% cellulase enzyme by weight into 1% sodium alginate solution.
  • the calcium alginate beads were obtained by dropping these solutions into 0.2 M calcium chloride solutions.
  • the pilling test was carried out at 2000 cycles.
  • the pilling values are on a scale ranging from 1 -5. When the antipilling performance increases, fewer beads are formed on the fabric after application and the pilling value increases. 5 is the highest anti-pilling performance and 1 is the lowest anti pilling performance. The obtained results are given in Table 5.
  • Example 6- Cellulase solution An aqueous cellulase enzyme solution of 10% and 13,3 % was prepared for anti-pilling enzyme application. After the application is made in the bath for 60 minutes at 55C° at pH 5 so as to test its performance in the application, the pilling test was carried out at 2,000 cycles. The obtained results are given in Table 6.

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Health & Medical Sciences (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Genetics & Genomics (AREA)
  • Biochemistry (AREA)
  • Microbiology (AREA)
  • General Engineering & Computer Science (AREA)
  • Biotechnology (AREA)
  • Biomedical Technology (AREA)
  • General Health & Medical Sciences (AREA)
  • Molecular Biology (AREA)
  • Medicinal Chemistry (AREA)
  • Dispersion Chemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Textile Engineering (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Or Physical Treatment Of Fibers (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Immobilizing And Processing Of Enzymes And Microorganisms (AREA)

Abstract

The present invention relates to the use of enzymes in textile applications by encapsulating the same with macromolecules so as to increase their performance. The present invention discloses the usage of an enzyme in the textile field selected from amylase, cellulase and catalase encapsulated with a molecule selected from alginate, agar or cyclodextrin.

Description

ENCAPSULATED ENZYMES AND THE USAGE THEREOF IN TEXTILE
APPLICATIONS
TECHNICAL FIELD
The invention relates to the encapsulated enzymes and the usage thereof in the textile applications.
The invention particularly relates to the amylase, catalase and cellulase enzymes encapsulated by alginate, agar and cyclodextrin and the usage thereof in the textile applications.
STATE OF THE ART
Enzymes have various applications from textile to food, from pharmaceuticals, to detergents and biofuels, and in industry and biotechnology fields. Enzymes are molecules in protein structure and are designed so as to work in biological environments in the nature. Amino acid chains determine the three-dimensional shape, conformation and function of the enzymes. The high temperature, oxidizing agents, high acidity and alkalinity that the enzymes are exposed to in the industrial applications cause their denaturation due to disruption of their three dimensional structures and decrease in their activities. This circumstance prevents efficient and long term usage of the enzymes. For this reason, continuing the enzyme activity by maintaining the stability of the enzymes is one of the most important aspects in the enzyme applications.
Among the enzymes widely used in the textile field, we can list amylase, cellulase, catalase, protease, peroxidase, lipase and laccase. Among these enzymes, amylase, catalase and cellulase are the most commercially produced enzymes.
Amylase enzyme is used as a desizing enzyme and provides the removal of the sizing by decomposing the starch and its derivatives in cotton products into water-soluble dextrin form.
The catalase enzyme removes the hydrogen peroxide residues that may be harmful before the dyeing process by decomposing the hydrogen peroxide in the environment. Cellulase enzyme is used to remove the feather of cellulosic fabrics and blends such as cotton, viscose, linen, etc. and to positively affect the touching in the completion processes.
These enzymes are prepared in a solution in the conventional textile products and applied to the fabric by exhaust, bleaching and foulard method according to the aim of use. These applications are performed at temperatures between 30 and 95C° and at different pH values. The high temperatures where the applications can reach cause the structures of the enzymes to deteriorate and denature and to lose their activity.
Enzymes are produced in the form of formulations containing sorbitol, glycerol, sugar, salt and various wetting agents that are prepared in aqueous medium in the available commercial products. The enzyme cannot remain stable sufficiently in these products, their activities decrease during storage and textile applications. For this reason, the shelf life of textile products containing enzymes can vary between 3 and 6 months and can be 1 year at maximum.
In the state of the art, there are various methods applied to increase the stability and shelf life of enzymes. One of these is forming the composite materials wherein the enzyme is found encapsulated by a large molecule.
In the patent application numbered EP2698434A1 , it is mentioned that enzymes can be protected by means of encapsulation.
In the article, Kumar R, Entrapment of a-amylase in alginate beads: Single step protocol for purification and thermal stabilization; it is disclosed that a-amylase is encapsulated by alginate and its thermal stability is increased.
It is still required to stabilize certain enzymes by protecting the activity and the performance of the same so as to provide the conditions required in the textile applications. Moreover, providing products with a longer shelf life compared to the enzyme in free form is among the problems aimed to be solved in the textile applications.
As a result, due to the insufficiency of the current solutions regarding the subject matter, a development is required to be made in the relevant technical field.
BRIEF DESCRIPTION OF THE INVENTION The present invention relates to processes that fulfill the abovementioned requirements and bring some additional advantages for encapsulation of an enzyme selected from amylase, cellulase and catalase with one selected from alginate, agar and cyclodextrin and relates to the use of encapsulated amylase, encapsulated cellulase and encapsulated catalase obtained from these processes in the textile applications.
The main aim of the invention is to provide processes that increase enzyme performance for use in textile applications.
The main aim of the invention is to provide processes that increase enzyme activity for use in textile applications.
Another aim of the invention is to provide processes for increasing enzyme stability and shelf life for use in textile applications.
In order to fulfill all above mentioned aim and aims obtained from the following detailed description, the present invention provides a process for producing alginate beads by encapsulation with alginate of an enzyme selected from amylase, cellulase and catalase.
In a preferred embodiment of the invention, said process comprises a step of adding at least one of said enzymes to the aqueous sodium alginate solution.
In a preferred embodiment of the invention, concentration of said sodium alginate solution is in the range of 0.25-2.00% by weight.
In a preferred embodiment of the invention, concentration of said sodium alginate solution is 1 ,0 % by weight.
In a preferred embodiment of the invention, said process comprises the step of dropping an aqueous sodium alginate solution containing enzyme into a solution containing calcium chloride so as to obtain calcium alginate beads.
In another preferred embodiment of the invention, molarity of calcium chloride in said calcium chloride solution is 0,1-1 ,0 M.
In another preferred embodiment of the invention, molarity of calcium chloride in said calcium chloride solution is 0,2M.
In another preferred embodiment of the invention, said enzyme is amylase. In another preferred embodiment of the invention, the concentration of amylase in sodium alginate solution is 3-20% by weight.
In another preferred embodiment of the invention, the concentration of amylase in sodium alginate solution is 5-8% by weight.
In another preferred embodiment of the invention, said enzyme is catalase.
In another preferred embodiment of the invention, the concentration of catalase in sodium alginate solution is 1-5% by weight.
In another preferred embodiment of the invention, the concentration of catalase in sodium alginate solution is 1-2% by weight.
In another preferred embodiment of the invention, said enzyme is cellulase.
In another preferred embodiment of the invention, the concentration of cellulase in sodium alginate solution is 5-20% by weight.
In another preferred embodiment of the invention, the concentration of cellulase in sodium alginate solution is 10-15% by weight.
In order to fulfill all above mentioned aims and aims obtained from the following detailed description, the present invention provides the use of an enzyme encapsulated with alginate in textile applications, and said enzyme is selected from a-amylase, cellulase and catalase.
In a preferred embodiment of the invention, said enzyme is amylase and said textile application is desizing application.
In a preferred embodiment of the invention, said enzyme is catalase and said textile application is antiperoxide enzyme application.
In a preferred embodiment of the invention, said enzyme is cellulase and said textile application is anti-pilling application.
The structural and characteristic features of the present invention will be understood clearly by the following detailed description and therefore the evaluation shall be made by taking the detailed description into consideration.
DETAILED DESCRIPTION OF THE INVENTION Amylase enzyme is used as a desizing enzyme and provides the removal of the sizing by decomposing the starch and its derivatives in cotton products into water-soluble dextrin form.
The catalase enzyme removes the hydrogen peroxide residues that may be harmful before the dyeing process by decomposing the hydrogen peroxide in the environment.
Cellulase enzyme is used to remove the feather of cellulosic fabrics and blends such as cotton, viscose, linen, etc. and to positively affect the touching in the completion processes.
It is found in the present invention that the performances of the amylase, catalase and cellulase enzymes are higher than the conventional solution systems in the above mentioned textile applications. More effective results can be obtained with the present invention by using enzyme with less concentration, and the enzyme is more stable at higher temperatures. Moreover, it is found out that shelf life of the enzyme systems that are prepared by the encapsulation method is longer than the products containing enzyme in free form.
Alginate that is obtained from brown algae grown in cold water areas is a linear polysaccharide and consists of b-D-manuronic acid (M) and 1-4 bonds of a-L-gyluronic acid (G). Its composition and sequence along the chain vary. (Zhang and Zhao 2007; Lertsutthiwong et al. 2008). Said polysaccharide is used for the continuous release of agrochemicals after gelation using metal ions. (Fernandez-Perez 2007; Singh et al. 2013; Wlodarczyk and Siwek 2013)The chemical structure of alginate is shown by Formula 1 .
Figure imgf000006_0001
Formula 1
Cyclodextrins are complex polysaccharides consisting of glucose units (a-D- glucopyranose) that are combined with a- (1 ,4) bonds. Cyclodextrins that have specific physicochemical properties depending on the extraverted positioning and conical structure of the hydroxyl groups may carry the hydrophobic compounds in the space therein and also may dissolve in aqueous medium (Britto et al. 2004). Cyclodextrins are widely used due to their capacity to form inclusion complexes with a large number of molecules (PerezMartinez et al. 1999; De Carvalho and de Alves Pinto 2012; Morin-Crini and Crini 2013; Higueras et al. 2013; Fernandes et al. 2014; Garrido et al. 2014). The chemical structure of cyclodextrin is shown by Formula 2.
Figure imgf000007_0001
Formula 2
Agar is a hydrophilic colloid consisting of agarose and agaropectin mixture. The agarose in the agar constitutes approximately 70% of the agar. Agarose can be used as a matrix to encapsulate the cells. Agarose comprises thermally cross linkable repeating 1 ,3-linked-d- galactose and 1 ,4-linked-3,6-anhydro-a-l-galactopyranose units. (Normand et al., 2000). Agarose can be used for cell encapsulation since it constitutes a double helix structure that is aggregated in the form of thick aggregates after large-diameter intracellular hydrogen bonds are formed (Xiong et al., 2005). It forms hydrogels with time dependent mechanical properties with said hydrogen bonds. Thus, agar can be able to form gel in a reversible manner by means of cooling a hot aqueous solution. Agar gel can be melted by heating and can be returned to its original condition by cooling the same. General gel temperature for 1.5% solution of agar is 35-45 C and thus it can form very rigid gels at very low concentrations. The chemical structure of agarose is shown by Formula 3.
Figure imgf000008_0001
Formula 3
Enzymes can be encapsulated by encapsulating the same within cyclodextrin, agar, and alginate. Enzymes with different concentrations are added into cyclodextrin; agar and alginate solutions prepared in different concentrations and are encapsulated in the matrix obtained from these molecules by different chemical and physical mechanisms.
The present invention provides processes for encapsulation of an enzyme selected from amylase, cellulase and catalase with one selected from alginate, agar and cyclodextrin. Encapsulation with alginate is carried out by ionic crosslinking. Encapsulation with agar is performed physically (melting, setting, freezing) by method of networking. The system has a hydrogel structure in the alginate and agar encapsulation, and the enzyme is made by means of releasing the same through the pores. Encapsulation with cyclodextrin can be performed by loading therein.
The present invention provides the use of an enzyme encapsulated with alginate, agar or cyclodextrin in textile applications, the enzyme mentioned here is selected from a- amylase, cellulase and catalase. When the enzyme is amylase then said textile application may be desizing application. When the enzyme is cellulase then said textile application may be antipilling enzyme application. When the enzyme is catalase then said textile application may be antiperoxide. In the present application, the statement "textile applications" refers to the processes carried out by using enzymes in the textile field. In the present application “desizing application” statement refers to the processes in the textile field that are carried out so as to remove the sizing by decomposing the starch and its derivatives in cotton products into water-soluble dextrin form by using amylase enzyme.
In the present application, "antiperoxide enzyme application" refers to the processes performed in the textile field by using catalase enzyme to remove hydrogen peroxide residues that may be harmful in fabric production before the dyeing process by decomposing the hydrogen peroxide.
In the present application, “anti-pilling application” refers to the processes that are carried out so as to reduce pilling formation namely to allow the fabric to gain anti-pilling characteristic that is one of important parameters affecting the quality in knit fabric production by means of using cellulase enzyme in the textile field.
Encapsulation with alginate
The present invention provides a process for producing alginate beads by encapsulation with alginate of an enzyme selected from amylase, cellulase and catalase and provides the use of the alginate beads obtained in textile applications.
In the inventive process, sodium alginate solution containing enzyme is prepared by adding at least one of the enzymes selected from amylase, cellulase or catalase into the sodium alginate solution; and calcium alginate beads containing enzyme or enzymes are obtained by dropping the enzyme-containing sodium alginate solution into a calcium chloride solution. Thus, encapsulation with alginate is provided by ionic cross-linking of sodium alginate solution in a medium containing Ca2+.
In a preferred embodiment of the invention, said enzyme is amylase. When the amylase concentration increases, the amylase/alginate ratio in the system also increases and thus the alginate ratio decreases. This causes to obtain softer gel beads with larger pores. Therefore, for example, alginate beads having an amylase concentration of 10% by weight are not as stable as alginate beads with an amylase concentration of 7% by weight, it has a weaker amylase barrier and thus it can protect its amylase activity less. Another important factor is that above a certain concentration of the amylase enzyme, the alginate gel structure can be weakened by partially degrading the same. When the concentration of amylase in aqueous sodium alginate solution is 3-20% by weight with the present invention, it was found that obtained alginate beads are effective in desizing application and when the concentration of amylase in aqueous sodium alginate solution is 5-8% by weight, obtained alginate beads exhibited the highest performance in desizing application.
In a preferred embodiment of the invention, said enzyme is catalase. When the concentration of catalase in aqueous sodium alginate solution is 1 -5% by weight with the present invention, it was found that obtained alginate beads exhibited the highest performance in peroxide enzyme application on fabric. In a preferred embodiment of the invention, the concentration of catalase in aqueous sodium alginate solution is 1 -2% by weight. The gel structure in the alginate beads that are obtained with this ratio is not affected. Moreover, this ratio is preferred in terms of its cost.
In a preferred embodiment of the invention, said enzyme is cellulase. When the concentration of cellulase in aqueous sodium alginate solution is 5-20% by weight with the present invention, it was found that obtained alginate beads exhibited the highest performance in pilling application on fabric. In a preferred embodiment of the invention, the concentration of cellulase in aqueous sodium alginate solution is 10-15% by weight. The gel structure in the alginate beads that are obtained with this ratio is not affected. Moreover, this ratio is preferred in terms of its cost.
The concentrations of sodium alginate solution and calcium chloride solution that are used in the inventive process substantially affect the obtained alginate beads. The concentration of said sodium alginate solution is in the range of 0.25-2.0% by weight, preferably 1.0% by weight so as to provide capsules that have proper spherical structure and size distribution and do not adhere to each other. Molarity of calcium chloride in said calcium chloride solution is in the range between 0,1 -1 ,0 M, preferably 0,2 M. Both smooth spherical and equal sized capsules were obtained at these concentrations, and more controlled enzyme release and performance was provided with the obtained gel structure having optimum hardness.
Examples
Alginate solutions containing enzymes are prepared by adding enzyme with different concentrations according to the enzyme used into the sodium alginate aqueous solutions of 0.25%, 0.5, 1 .0, 1 .5 and 2.0 by weight. The calcium alginate beads were obtained by dropping these solutions into 0,1 , 0,2, 0,3, 0,4, 0,5 and 1 ,0 M of calcium chloride solutions. Example 1 - Amylase encapsulated with alginate
For desizing enzyme application, alginate solutions containing amylase were prepared by adding 7% and 10% of amylase enzyme by weight into 1.0% of sodium alginate aqueous solution by weight. The calcium alginate beads were obtained by dropping these solutions into 0.2 M calcium chloride solutions. Sodium alginate solutions containing amylase enzyme and calcium alginate bead samples were exposed to desizing application at 60C° for 30 minutes so as to test their performances in practice. The obtained results are given in Table 1. Enzyme performances were measured with the TEGEWA test. TEGEWA value changes in direct proportion to enzyme performance.
Figure imgf000011_0001
Table 1
The best enzyme performance was registered on alginate beads with an enzyme concentration of 7 % by weight according to these results. Therefore, it has been discovered that although alginate beads contain less enzyme, they have an enzyme concentration of 7% by weight, and they achieve better results in the application of desizing.
Example 2- Amylase solution
For the desizing application, aqueous solutions containing 7% and 10% amylase enzyme were prepared. The aqueous solution containing amylase enzyme was exposed to desizing application at 60C° for 30 minutes so as to test its performance in practice. The obtained results are given in Table 2. Enzyme performances were measured with the TEGEWA test. TEGEWA value changes in direct proportion to enzyme performance.
Figure imgf000011_0002
Table 2 As a result of the experiments, when alginate beads containing amylase were present in the system, higher TEGEWA values were found compared to the amylase solutions. Flerein, gel formation of alginate by ionic cross-linking is effective in forming a more effective barrier to the enzyme. Example 3 - Catalase encapsulated with alainate
For antiperoxide enzyme application, catalase containing alginate solutions were prepared by adding 1.5% and 1.8% of catalase enzyme by weight into 1.0% of sodium alginate aqueous solution by weight. The calcium alginate beads were obtained by dropping these solutions into 0.2 M calcium chloride solutions. Alginate solution containing antiperoxide enzyme and calcium alginate bead samples were subjected to antiperoxide enzyme application so as to test the performance in the application. For this purpose, a bath containing 8 g/lt NaOFI (45%) and 10 g/lt FI2O2 (50%) was prepared, after bleaching was carried out at 98C° for 45 minutes between pH 11-12, the bath was cooled to 45C° and pH was adjusted to 5-5,5. In the next step, it was kept in a bath of 0.35 g/lt for 20 minutes at 45C°. The enzyme activity was determined by measuring the amount of peroxide remaining in the environment at the end of certain periods. The obtained results are given in Table 3.
Figure imgf000012_0001
Table 3
The best result was registered on alginate beads with an enzyme concentration of 1.8% by weight.
Example 4- Catalase solution Aqueous catalase solutions of 1.8% by weight were prepared for the antiperoxide enzyme application. Aqueous catalase solutions were subjected to antiperoxide enzyme test application so as to test their performances in practice. For this purpose, a bath containing 8 g/lt NaOH (45%) and 10 g/lt H2O2 (50%) was prepared, after bleaching was carried out at 98C° for 45 minutes between pH 11-12, the bath was cooled to 45C° and pH was adjusted to 5-5,5. In the next step, it was kept in a bath of 0.35 g/lt for 20 minutes at 45C°. The catalase activity was determined by measuring the amount of peroxide remaining in the environment at the end of certain periods. The obtained results are given in Table 4.
Figure imgf000013_0001
Table 4 As a result of the experiments, after the application in formulations containing alginate beads, less peroxide was found in the medium compared to aqueous catalase solutions. Herein, gel formation of alginate by ionic cross-linking is effective in forming a more effective barrier to the enzyme.
Example 5 - Cellulase encapsulated with alginate For antipilling enzyme application, alginate solutions containing cellulase were prepared by adding 10% and 13.3% cellulase enzyme by weight into 1% sodium alginate solution. The calcium alginate beads were obtained by dropping these solutions into 0.2 M calcium chloride solutions. After the application is made in the bath for 60 minutes at 55C° at pH 5 so as to test its performance in the application, the pilling test was carried out at 2000 cycles. The pilling values are on a scale ranging from 1 -5. When the antipilling performance increases, fewer beads are formed on the fabric after application and the pilling value increases. 5 is the highest anti-pilling performance and 1 is the lowest anti pilling performance. The obtained results are given in Table 5.
Figure imgf000013_0002
Figure imgf000014_0002
Table 5
The best result was registered on alginate beads with an enzyme concentration of 10 % by weight.
Example 6- Cellulase solution An aqueous cellulase enzyme solution of 10% and 13,3 % was prepared for anti-pilling enzyme application. After the application is made in the bath for 60 minutes at 55C° at pH 5 so as to test its performance in the application, the pilling test was carried out at 2,000 cycles. The obtained results are given in Table 6.
Figure imgf000014_0001
Table 6
As a result of the experiments, fewer beads were formed after the application in the formulations containing alginate in the system compared to aqueous cellulase solutions, a higher pilling value was found directly proportional to the antipilling performance. Herein, gel formation of alginate by ionic cross-linking is effective in forming a more effective barrier to the enzyme.

Claims

1 . A process for producing alginate beads by encapsulation with alginate of an enzyme selected from amylase, cellulase and catalase.
2. Process according to claim 1 , characterized in that; the step comprises a step of adding at least one of said enzymes into the aqueous sodium alginate solution.
3. Process according to claim 2, characterized in that; concentration of said sodium alginate solution is in the range of 0.25-2.00% by weight.
4. Process according to claim 3, characterized in that; concentration of said sodium alginate solution is 1 ,0% by weight.
5. Process according to any of the preceding claims, characterized in that; it comprises the step of dropping an aqueous sodium alginate solution containing enzyme into a solution containing calcium chloride so as to obtain calcium alginate beads.
6. Process according to claim 5, characterized in that; molarity of calcium chloride in said calcium chloride solution is between 0,1 -1 ,0 M.
7. Process according to claim 6, characterized in that; molarity of calcium chloride in said calcium chloride solution is 0.2M.
8. Process according to any of the previous claims, characterized in that; said enzyme is amylase.
9. Process according to claim 8, characterized in that; the concentration of amylase in sodium alginate solution is 3-20% by weight.
10. Process according to claim 9, characterized in that; the concentration of amylase in sodium alginate solution is 5-8% by weight.
11. Process according to any of the claims 1-7, characterized in that; said enzyme is catalase.
12. Process according to claim 11 , characterized in that; the concentration of catalase in sodium alginate solution is 1-5% by weight.
13. Process according to claim 12, characterized in that; the concentration of catalase in sodium alginate solution is 1-2% by weight.
14. Process according to any of the claims 1 -7, characterized in that; said enzyme is cellulase.
15. Process according to claim 14, characterized in that; the concentration of cellulase in sodium alginate solution is 5-20% by weight.
16. Process according to claim 15, characterized in that; the concentration of cellulase in sodium alginate solution is 10-15% by weight.
17. Use of an enzyme encapsulated with alginate in textile applications, characterized in that; the enzyme is selected from a-amylase, cellulase and catalase.
18. Usage according to claim 17, characterized in that; said enzyme is amylase and said textile application is desizing application.
19. Usage according to claim 17, characterized in that; said enzyme is catalase and said textile application is anti-peroxide enzyme application.
20. Usage according to claim 17, characterized in that; said enzyme is cellulase and said textile application is anti-pilling application.
PCT/TR2020/051109 2019-12-26 2020-11-16 Encapsulated enzymes and the usage thereof in textile applications WO2021133302A1 (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
EP20906374.2A EP4081680A4 (en) 2019-12-26 2020-11-16 Encapsulated enzymes and the usage thereof in textile applications

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
TR2019/21815A TR201921815A2 (en) 2019-12-26 2019-12-26 ENCAPSULATED ENZYMES AND THEIR USE IN TEXTILE APPLICATIONS
TR2019/21815 2019-12-26

Publications (1)

Publication Number Publication Date
WO2021133302A1 true WO2021133302A1 (en) 2021-07-01

Family

ID=76574904

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/TR2020/051109 WO2021133302A1 (en) 2019-12-26 2020-11-16 Encapsulated enzymes and the usage thereof in textile applications

Country Status (3)

Country Link
EP (1) EP4081680A4 (en)
TR (1) TR201921815A2 (en)
WO (1) WO2021133302A1 (en)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN113737509A (en) * 2021-09-02 2021-12-03 珠海百康生物技术有限公司 Solid enzyme preparation and preparation method and application thereof

Non-Patent Citations (2)

* Cited by examiner, † Cited by third party
Title
SITI NORAIDA ABD RAHIM ET AL.: "Enzymes Encapsulation within Calcium Alginate-clay Beads: Characterization and Application for Cassava Slurry Saccharification", PROCEDIA ENGINEERING, vol. 68, 2013, pages 411 - 417, XP028847511, ISSN: 1877-7058, DOI: https://doi.org/10.1016/j.proeng. 2013.12.20 0 *
TALEKAR, SACHIN ET AL.: "Optimization of immobilization of alpha amylase in alginate gel and it's comparative biochemical studies with free alpha amylase", RECENT RESEARCH IN SCIENCE AND TECHNOLOGY, vol. 4, no. 02, 2012, pages 1 - 5, XP055835177 *

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN113737509A (en) * 2021-09-02 2021-12-03 珠海百康生物技术有限公司 Solid enzyme preparation and preparation method and application thereof
CN113737509B (en) * 2021-09-02 2023-09-05 珠海百康生物技术有限公司 Solid enzyme preparation and preparation method and application thereof

Also Published As

Publication number Publication date
EP4081680A1 (en) 2022-11-02
EP4081680A4 (en) 2024-07-03
TR201921815A2 (en) 2021-07-26

Similar Documents

Publication Publication Date Title
Bayazidi et al. Immobilization of lysozyme on bacterial cellulose nanofibers: Characteristics, antimicrobial activity and morphological properties
Dinçer et al. Improving the stability of cellulase by immobilization on modified polyvinyl alcohol coated chitosan beads
Klapiszewski et al. Titania/lignin hybrid materials as a novel support for α-amylase immobilization: A comprehensive study
Bayramoğlu et al. Immobilization of a thermostable α-amylase onto reactive membranes: kinetics characterization and application to continuous starch hydrolysis
Trad et al. Chitosan hydrogel‐coated cotton fabric: Antibacterial, pH‐responsiveness, and physical properties
Chan et al. Semisynthesis of a controlled stimuli-responsive alginate hydrogel
Levi et al. Limonene encapsulation in alginate/poly (vinyl alcohol)
Naguleswaran et al. Distribution of granule channels, protein, and phospholipid in triticale and corn starches as revealed by confocal laser scanning microscopy
Çini et al. Polyphosphates as inorganic polyelectrolytes interacting with oppositely charged ions, polymers and deposited on surfaces: fundamentals and applications
CN105693883B (en) Chitosan microball, preparation method and application for enzyme immobilization
EP4081680A1 (en) Encapsulated enzymes and the usage thereof in textile applications
Sharma et al. Entrapment of α‐Amylase in Agar Beads for Biocatalysis of Macromolecular Substrate
Wu et al. An optical glucose biosensor based on entrapped-glucose oxidase in silicate xerogel hybridised with hydroxyethyl carboxymethyl cellulose
Ran et al. A facile method for improving the covalent crosslinking adsorption process of catalase immobilization
Cumana et al. Immobilization of glucose 6-phosphate dehydrogenase in silica-based hydrogels: a comparative study
Kadowaki et al. Biochemical and structural insights into a thermostable cellobiohydrolase from Myceliophthora thermophila
Tien et al. Immobilization of α-amylase on a zirconium dynamic membrane
Zeng et al. Application of flower-like SnS 2 nanoparticles for direct electrochemistry of hemoglobin and its electrocatalysis
Idumah Characterization and fabrication of xerogel polymeric nanocomposites and multifunctional applications
Yang et al. Utilization of cyclodextrins and its derivative particles as nucleants for protein crystallization
Marconi et al. Properties and use of invertase entrapped in fibers
Bayramoğlu et al. Reversible immobilization of uricase on conductive polyaniline brushes grafted on polyacrylonitrile film
Araya-Hermosilla et al. Immobilization of rhodamine 6G in calcium alginate microcapsules based on aromatic–aromatic interactions with poly (sodium 4-styrenesulfonate)
Karim et al. Single step immobilization of CMCase within agarose gel matrix: kinetics and thermodynamic studies
Zhang et al. Thin-layer polymer wrapped enzymes encapsulated in hierarchically mesoporous silica with high activity and enhanced stability

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 20906374

Country of ref document: EP

Kind code of ref document: A1

NENP Non-entry into the national phase

Ref country code: DE

ENP Entry into the national phase

Ref document number: 2020906374

Country of ref document: EP

Effective date: 20220726