Self-Assembly Properties and Aggregation Behavior of Amphiphilic Water-Dispersed Polyester with Different Contents of Sulfonate Groups in an Aqueous Solution.

Amphiphilic polymer water-dispersed polyester (WPET) has an important application value in the textile field. However, due to the potential interactions among water-dispersed polyester (WPET) molecules, the stability of their solution is susceptible to external factors. This paper focused on the self-assembly properties and aggregation behavior of amphiphilic water-dispersed polyester with different contents of sulfonate groups. In addition, the effects of WPET concentration, temperature, and Na+, Mg2+, or Ca2+ on WPET aggregation behavior were systematically investigated. The results show that compared with the low sulfonate group content of WPET, the high sulfonate group content of the WPET dispersion has higher stability with or without a high electrolyte concentration. In contrast, dispersions with low sulfonate group content are very sensitive to electrolytes and aggregate immediately at low ionic strength. WPET concentration, temperature, and electrolyte play important and complex roles in controlling the self-assembly properties and aggregation behavior of the WPET. The increase in WPET concentration can promote the self-assembly of WPET molecules. With the increase in temperature, the self-assembly properties for water-dispersed WPET are significantly reduced, resulting in enhanced stability. In addition, the electrolytes Na+, Mg2+, and Ca2+ in the solution can significantly accelerate the aggregation of WPET. This fundamental research on the self-assembly properties and aggregation behavior of WPETs can be used to effectively control and improve the stability of WPET solutions and provide guidance for the prediction of stability for WPET molecules not yet synthesized.

Plasticizer phthalate esters degradation with a laccase from Trametes versicolor: effects of TEMPO used as a mediator and estrogenic activity removal.

Phthalate esters (PAEs) are toxic and persistent chemicals that are ubiquitous in the environment and have attracted worldwide attention due to their threats to the environment and human health. Dimethyl phthalate (DMP) is a relatively simple structure and one of the most observed PAEs in the environment. This study investigated the degradation of the DMP using Trametes versicolor laccase and its laccase-mediator systems. The degradation effect of laccase alone on DMP was poor, while the laccase-mediator systems can effectively enhance the degradation efficiency. Within 24 h, 45% of DMP (25 mg/L) was degraded in the presence of 0.8 U/mL laccase and 0.053 mM 2, 2, 6, 6-tetramethylpiperidine-1-oxyl (TEMPO). A certain concentration (1 mM) of metal ions Al3+, Cu2+ or Ca2+ can positively promote DMP degradation with the laccase-TEMPO system. Moreover, the structure of PAEs also had a great influence on the degradation efficiency. Higher degradation efficiencies were observed when incubating PAEs with short alkyl side chains by the laccase-TEMPO system compared to that with long alkyl side chains. Additionally, the branched-chain PAEs had a better degradation effect than the straight-chain. The estrogenic activity of the DMP solution after reaction was much smaller than that of the original solution. Finally, transformation products ortho-hydroxylated DMP and phthalic acid were identified by GC-MS and the possible degradation pathway was proposed. This study verifies the feasibility of the laccase-TEMPO system to degrade PAEs and provides a reference for exploring more potential value of laccase.

A novel "trifunctional protease" with reducibility, hydrolysis, and localization used for wool anti-felting treatment.

Proteases can cause unacceptable fiber damage when they are singly applied to wool anti-felting treatment which can make wool textiles machine-washable. Even if protease is attached by synthetic polymers, the modified protease plays a limited role in the degradation of keratin with dense structure consisting of disulfide bonds in the scales. Here, to obtain "machine-washable" wool textiles, a novel "trifunctional protease" with reducibility, hydrolysis, and localization is developed by means of covalent bonding of protease molecules with poly (ethylene glycol) bis (carboxymethyl) ether (HOOC-PEG-COOH) and L-cysteine using carbodiimide/N-hydroxysuccinimide (EDC/NHS) coupling, aiming at selectively degrading the scales on the surface of wool. The formation of polymer is confirmed with size exclusion chromatography (SEC) and Fourier transform infrared spectroscopy (FT-IR). Ellman's test and fluorescence microscopy reveal that the modified protease can reduce disulfide bonds and restrict hydrolysis of peptide bonds on the wool scales. Furthermore, when applied to wool fabrics, the modified protease reach better treatment effects considering dimensional stability to felting (6.12%), strength loss (11.7%) and scale dislodgement proved by scanning electron microscopy (SEM), alkali solubility, wettability, and dyeability. This multifunctional enzyme is well-designed according to the requirement of the modification of wool surface, showing great potential for eco-friendly functionalization of keratin fibers rich in disulfide linkage.

Improving properties of silk sericin membranes via enzymatic oxidation with laccase and TEMPO.

Silk sericin has excellent features of antioxidant ability and good cytocompatibility; however, high water solubility and poor mechanical properties have restricted its application in biomedical fields. In this study, aimed at improving the mechanical properties of a regenerated silk sericin, the primary hydroxy groups in silk sericin were enzymatically oxidized by using laccase and 2,2',6,6'-tetramethylpiperidine-N-oxyl (TEMPO), and the generated reactive groups then reacted further with the amino groups in the sericin chains. The efficacy of the enzymatic cross-linking was evaluated by means of determination of amino groups, SDS polyacrylamide gel electrophoresis, Fourier transform infrared (FTIR) spectroscopy, and size exclusion chromatography. The results indicated that either laccase/TEMPO incubation or laccase treatment alone incurred a noticeable increase in the molecular weight of the sericin. FTIR analysis revealed that there was small change in the structure of the silk sericin after laccase/TEMPO treatment, and the obtained air-dried sericin membrane exhibited remarkably improved mechanical properties relative to those of the uncross-linked sericin membrane. In addition, the biocompatibility of the sericin membrane was at an acceptable level according to the cell viability of NIH/3T3 cells. The present work provides a novel method for the preparation of sericin-based biomaterials.

HRP-mediated graft polymerization of acrylic acid onto silk fibroins and in situ biomimetic mineralization.

Silk fibroin (SF) can be extensively utilized in biomedical areas owing to its appreciable bioactivity. In this study, biocompatible composites of SF and hydroxyapatite (HAp) were fabricated through in situ biomimetic mineralization process. Graft copolymerization of acrylic acid (AA) onto SF was conducted by using the catalytic system of acetylacetone (ACAC), hydrogen peroxide (H2O2) and horseradish peroxidase (HRP), for enhancing the deposition of apatite onto the fibroin chains. Subsequently, biomimetic mineralization of the prepared fibroin-based membrane was performed in Ca/P solutions to synthesize the organized SF/HAp composites. The efficacies of graft copolymerization and biomimetic mineralization were evaluated by means of ATR-FTIR, GPC, EDS-Mapping, XRD and others. The results denoted that AA was successfully graft-copolymerized with fibroin and formed the copolymer of silk fibroin-graft-polyacrylic acid (SF-g-PAA), and the grafting percentage (GP) and grafting efficiency (GE) under the optimal condition reached to 23.2% and 29.4%, respectively. More mineral phases were detected on the surface of SF-g-PAA membrane after mineralization process when compared to that of the untreated fibroin membrane, companying with an improved mechanical property. According to MG-63 cell viability and fluorescent adhesion assays, the mineralized SF-g-PAA composite showed satisfactory biocompatibility and exceptional adhesive effects as well. The synthetized composite of SF-g-PAA/HAp can be potentially applied in the fields of bone tissue engineering.

Enhancement of antioxidant ability of Bombyx mori silk fibroins by enzymatic coupling of catechin.

Enzymatic modification of Bombyx mori silk fibroin was carried out by using (+)-catechin, aiming at improving the antioxidant ability of the fibroin-based materials.The actions of tyrosinase on catechin were evaluated by using spectrophotometry, LC-MS, and Fourier transform infrared spectroscopy (FTIR). ε-Polylysine (ε-PLL) was used to investigate the possibility of the covalent reaction between catechin and the primary amine compound. The properties of the fibroin membranes before and after grafting of catechin were compared. The results revealed that catechin was oxidized into reactive o-quinones and subsequently formed catechin derivatives.Meanwhile, catechin could be efficiently grafted onto ε-PLL and led to a decrease in the amount of primary amine groups. 1H-NMR analysis verified the occurrence of the tyrosinase-catalyzed coupling of catechin onto the surface of silk fibroins. Improved antioxidant activity and better durability were obtained for the silk fibroin membrane based on catechin/tyrosinase treatment. Thermal behavior and biocompatibility for the catechin-grafted fibroin membranes did not noticeably change as compared to that of the untreated sample. The present work provided a novel method for preparation of the fibroin-based materials for biomedical applications.

Preparation of antibacterial silk fibroin membranes via tyrosinase-catalyzed coupling of ε-polylysine.

Silk fibroins have good biocompatibility and could be used to form a variety of regenerated functional biomaterials. In this study, enzymatic oxidization of silk fibroins with tyrosinase (TYR) was carried out, followed by coupling of ε-polylysine (ε-PLL) for improving antibacterial ability of the fibroin-based biomaterial. Trinitrobenzene sulfonic acid (TNBS) was selectively used to incubate with silk fibroins prior to TYR treatment, aiming at preventing the self-crosslinking of silk fibroins during enzymatic oxidation. The results indicated that tyrosine residues in silk fibroins could be converted to reactive dioxyphenylalanine and o-quinone residues TYR successively. TNBS pretreatment inhibited the self-crosslinks of silk fibroins and promoted the successive coupling of ε-PLL to fibroin proteins with high graft yield. The combined use of TNBS, TYR, and ε-PLL treatments endowed fibroin membrane with satisfactory antibacterial ability against Staphylococcus aureus, and the obtained durability was also acceptable. The changes in surface potential and amine acid composition for the fibroin membranes verified the favorable actions of the combined treatment. The present method could be potentially utilized for enzymatic functionalization of various fibroin-based biomaterials.

Noncovalent immobilization of cellulases using the reversibly soluble polymers for biopolishing of cotton fabric.

The hydrolytic reaction of cellulases can occur in the interior of cellulosic fibers, causing tensile strength loss of the fabrics. Cellulase immobilization is an approach to solve this problem, because enlarging the molecule size of cellulases will limit the hydrolysis to the surfaces of the fibers. In this study, commercial cellulases were noncovalently immobilized onto the reversibly soluble polymers (Eudragit S-100 and Eudragit L-100). The characteristics of cellulase-Eudragit S-100 (CES) and cellulase-Eudragit L-100 (CEL) were evaluated using Fourier transform infrared spectra, circular dichroism spectra, and fluorescence spectra. The CES showed higher stability than CEL and free cellulase, especially at higher pH and temperature. CES and CEL retained 51% and 42% of their original activities after three cycles of repeated uses, respectively. In addition, the effects of cellulase treatment on the cotton yarn and fabric have been investigated. The bending stiffness results showed that the cotton fabric samples treated with the free and immobilized cellulases were softer than untreated samples. However, less fiber damage in terms of weight loss and tensile strength of treated cotton was observed.

Fabrication of reversible bacteria-killing and bacteria-releasing cotton fabrics with anti-bacteria adhesion capacity for potential application in reusable medical materials.

Nowadays, more and more smart antibacterial materials have been prepared to meet some specific application area, and most of these materials have complex fabrication processes or incompatible biocompatibility. In this paper, a smart monomer that can switch between the form of quaternary ammonium salt and zwitterionic betaine was prepared and grafted onto cotton fabric. This finished cotton was smart too, it had nice antibacterial performance (99.89 % for E. coli and 99.97 % for S. aureus) in the form of quaternary ammonium salt, and it could release most of the attached bacteria when transferred to the form of zwitterionic betaine in PBS, and the form of zwitterionic betaine could converse back to the state of quaternary ammonium salt in HAC. Simultaneously, it was biocompatible in the form of zwitterionic betaine form. Furthermore, this smart material had nice function reproducibility after repeated transformations. In general, the smart antibacterial cotton could switch between bacteria-killing and bacteria-releasing reversibly, and had good biocompatibility and nice reproducibility, showing a potential application in reusable medical protective materials.

Effect of emulsified lipid and saponified lipid on the enzyme desizing of starch and its mechanism.

To enhance the flexibility of starch film adhesion on yarns, sizing lipids (saponified lipid or emulsified lipid) must be added during the sizing process. However, different types of sizing lipids may have diverse combinations with starch to impact enzyme desizing. Therefore, this study investigated the effects of saponified lipid and emulsified lipid commonly used in warp sizing on the hydrolysis of starch. Additionally, the desizing efficiency and chain structure of desizing residues were analyzed. Experimental results demonstrated that the existence of saponified lipid or emulsified lipid led to a reduction in the degree of hydrolysis (1.1 % and 2.6 %, respectively) compared to the original corn starch. Notably, saponified lipid exhibited a relatively strong negative impact. Furthermore, the desizing efficiency decreased after adding emulsified lipid (1.2 %) or saponified lipid (2.9 %). Starch-lipid V-type complexes and physical hindrance could inhibit the enzyme desizing, resulting in a larger wavelength of maximum absorbance for desizing residues, along with higher molecular weight, z-average radius of gyration, and an increased proportion of long chains. The presence of saponified lipid significantly negatively influenced desizing, possibly due to the smaller particle size and propensity for complex formation with starch.

Reversible bacteria-killing and bacteria-releasing cotton fabric with anti-bacteria adhesion ability for potential sustainable protective clothing applications.

Multifunctional antibacterial surfaces are playing an essential role in various areas. Smart antibacterial materials equipped with switchable "bacteria-killing" and "bacteria-releasing" abilities have been created by scientists. However, most of them are either biologically incompatible, or complex fabricating procedures, or cannot prevent themselves from being attached by bacteria. In this work, a double-layer smart antibacterial surface was created easily by simple surface initiate atom transfer radical polymerization: the upper layer PSBMA provides anti-bacteria adhesion capacity, the NCl bond can show bacteria-killing ability and the under layer PNIPAM can exhibit bacteria-releasing property. Remarkably, the NCl bond can interconvert with the NH bond easily, which allows switching between bacteria-killing and bacteria-releasing. As a result, the functional cotton fabrics can resist about 99.66 % of bacteria attaching, kill nearly 100 % of attached bacteria after 5 min contacting and release about 99.02 % of the formerly attached bacteria. Furthermore, the functional cotton fabric kept excellent anti-bacteria adhesion ability (about 99.27 %) and bacteria-releasing capacity (about 98.30 %) after 9 cycles of re-chlorination. In general, a reversible "bacteria-killing" and "bacteria-releasing" cotton fabric was fabricated with well anti-bacteria adhesion capacity in a simple way, and this smart multifunctional cotton fabric shows a great potential application in reusable protective clothing.

Study on the cross-linking process of carboxylated polyaldehyde sucrose as an anti-wrinkle finishing agent for cotton fabric.

Sucrose was oxidized in a two-step oxidation reaction catalyzed by 2,2,6,6-tetramethyl-1-piperidinyloxy (TEMPO)-laccase and sodium periodate (NaIO4). To generate carboxylated polyaldehyde sucrose (openSu) containing multiple aldehyde and carboxyl groups. The amount of TEMPO and laccase used, as well as the temperature and reaction time were optimized for the oxidation reaction. The successful combination of aldehyde and carboxyl groups of openSu with cellulose was achieved by changing the composition, ratio of the catalyst and the curing conditions. Thereafter, we analyzed the structural characteristics of openSu as well as the aldehyde and carboxyl group content using nuclear magnetic resonance carbon spectroscopy (13C NMR). We found that the optimal finishing conditions were a mixture of magnesium chloride and sodium hypophosphite at a mass concentration ratio of 16 g/L:4 g/L, and curing at 150 °C for 3 min followed by curing at 180 °C for 2 min. There was significant improvement in the anti-wrinkle performance of the openSu-finished fabric, with a wrinkle recovery angle of 258°, whiteness index of 72.1, and a tensile strength rate of more than 65%. We also studied the covalent crosslinking mechanism between openSu and the cotton fabrics.

Effects of exogenous proteins on enzyme desizing of starch and its mechanism.

Added protein to starch has abundantly applied to size the yarns. However, scarce information is available about the impact of proteins on the enzyme desizing of starch. Thus, the objective of this study was to explore the effect of corn gluten, soybean protein and bone glue on enzyme desizing and reveal the interference mechanism. The desizing efficiency of starch was detected after added proteins. The contact angle, swelling ability, protein content and structure of starch adhesion on desized yarn were measured to analyze the effect of protein on desizing. In addition, the binding forces between protein and starch were detected, and the inhibition mechanism was analyzed. Experimental results showed that desizing efficiencies of starch were decreased after adding the protein. Corn gluten had the strongest influence in hindering desizing due to the weakest promotion in the swelling of film and the stronger binding force between protein and starch, mainly through hydrophobic interaction and hydrogen bond. Improving the swelling ability of film and inhibiting the binding between starch and protein may be feasible ways to reduce the inhibition of protein on desizing.

Degradation of octylphenol polyethoxylates with a long ethoxylate chain using the laccase-mediated systems.

Alkylphenol polyethoxylates (APEOn) are the second-largest category of commercial nonionic surfactants, which are difficult to degrade naturally in the environment. This study examined the degradation of octylphenol polyethoxylate (OPEOn) by laccase and its laccase-mediated systems. The results showed that OPEOn was poorly degraded by laccase alone. 2, 2'-azino-bis [3-ethylbenzothiazoline-6-sulphonic acid] (ABTS), 1-hydroxybenzotriazole (HBT), and 2, 2, 6, 6-tetramethylpiperidine-1-oxyl (TEMPO) were selected as the redox mediators. Experimental results also indicated that 52.4% of the initial OPEOn amount was degraded by laccase in the presence of TEMPO. The degradation efficiency was analyzed using high-performance liquid chromatography. Furthermore, the structural characteristics of the degradation products were measured using matrix-assisted laser desorption/ionization-time of flight mass spectrometry and nuclear magnetic resonance spectroscopy, and it could be found that the laccase-TEMPO system could gradually shorten the ethoxylate chain by oxidizing the primary hydroxyl group of OPEOn, thereby degrading the OPEOn of the macromolecule into small molecules. The maximum of the ion peak distributions of OPEOn decreased from n = 8 finally down to 3. The novel enzymatic system introduced by this study will become a promising alternative method for high-efficiency APEOn conversion and had great potential value in wastewater treatment.

Preparation of PEG-modified wool keratin/sodium alginate porous scaffolds with elasticity recovery and good biocompatibility.

To improve mechanical properties of keratin (KR) porous scaffolds, we prepared a PEGylated keratin through thiol-ene click reaction. Several porous scaffolds were prepared by blending PEGylated keratin with sodium alginate (SA). The surface morphology, mechanical properties, and porosity of scaffolds were detailed studied at different KR/SA proportions. The results showed the content of SA had an effect on pore formation and mechanical properties. When the mass ratio of KR to SA was 2:1, the stress of yield point of the keratin porous scaffold reached 1.24 MPa, and also showed good deformation recovery ability. The PEGylated keratin porous scaffold had a high porosity and great cytocompatibility. Its' porosity is up to 81.7% and the cell viability is about 117.78%. This allows it to absorb the simulated plasma quickly (9.20 ± 0.37 g/g). In addition, the structural stability and acid-base stability of the keratin porous scaffold were also improved after PEGylation. Overall, the PEGylated keratin porous scaffold will be promising in tissue materials due to its great physical, chemical, and biological properties.

How starch-g-poly(acrylamide) molecular structure effect sizing properties.

The effect of starch-g-poly(acrylamide) (S-g-PAM) molecular structure on sizing properties has been investigated. S-g-PAMs were synthesized with the catalysis of horseradish peroxidase (HRP) and Fourier transform infrared (FT-IR) confirmed the acrylamide (AM) units had been successfully grafted on starch chains. Structural parameters, including degree of branching (DB), degree of substitution (DS) and grafting ratio (GR) were characterized by 1H nuclear magnetic resonance (1H NMR), and were correlated with sizing properties of apparent viscosity, adhesion to cotton yarns and film mechanical properties. The apparent viscosity of S-g-PAMs has no obvious correlation with DB and DS (or GR), as the amylose content of the native starch might have more influence on the viscosity of grafted starches. DS (or GR) values of grafted starches have a positive relationship with the tensile strength of sized cotton yarns and are negatively related with tensile strength of starch film. These results can provide guidance in the section of starch with improved sizing properties.

Green modification of cellulose-based natural materials by HRP-initiated controlled "graft from" polymerization.

Considerable attention has been focused on the application of natural cellulosic materials due to the cost-effectiveness, renewability, and biodegradability of cellulose. However, gaps between cellulose-based and petroleum-based materials still exist. In this study, a green, environmental modification method for cellulose by enzyme-initiated reversible addition fragmentation chain transfer (RAFT) graft polymerization was reported. First, the grafting of acryloyl chloride (AC) provided reaction sites on cellulosic fiber surfaces, followed by the enzymatic RAFT graft polymerization of acrylamide (AM). The grafting of well-controlled polyacrylamide (PAM) chains on the cellulosic material surface was verified by Fourier transform infrared spectrometer (FTIR), X-ray photoelectron spectroscopy (XPS), and the controlled grafting ratio was also estimated. The transition of wetting behaviors after the modification of AC and PAM also provided evidence for successful grafting on cellulosic materials. In addition, this method can be well applied for the preparation of various functional cellulosic materials.

Laccase-catalyzed polymerization of hydroquinone incorporated with chitosan oligosaccharide for enzymatic coloration of cotton.

Chitosan oligosaccharide (COS), a water-soluble carbohydrate obtained from chemical or enzymatic hydrolysis of chitosan, has similar structure and properties to non-toxic, biocompatible, and biodegradable chitosan. However, COS has many advantages over chitosan due to its low molecular weight and high water solubility. In the current work, COS was incorporated in the laccase-catalyzed polymerization of hydroquinone. The laccase-catalyzed polymerization of hydroquinone with or without COS was investigated by using simple structure of glucosamine hydrochloride as an alternative to COS to understand the mechanism of COS-incorporated polymerization of hydroquinone. Although polyhydroquinone can be regarded as the polymeric colorant with dark brown color, there is no affinity or chemical bonding between polyhydroquinone and cotton fibers. Cotton fabrics were successfully in-situ dyed into brown color through the laccase-catalyzed polymerization of hydroquinone by incorporating with COS as a template. The presence of COS enhanced the dye uptake of polyhydroquinone on cotton fibers due to high affinity of COS to cotton and covalent bonding between COS and polyhydroquinone during laccase catalysis. This novel approach not only provides a simple route for the biological coloration of cotton fabrics but also presents a significant way to prepare functional textiles with antibacterial property.

Graft modification of lignin-based cellulose via enzyme-initiated reversible addition-fragmentation chain transfer (RAFT) polymerization and free-radical coupling.

In this study, a green approach combining enzyme-initiated reversible addition-fragmentation chain transfer (RAFT) polymerization and free-radical coupling was developed for the modification of jute fiber, which is a typical lignin-based cellulose. Jute fiber surface was covered by rich amount of lignin, which offered great opportunities for further functional modification. The controlled polymerization of vinyl monomers, acrylamide (AM) or butyl acrylate (BA), was carried out by horseradish peroxidase (HRP)-initiated RAFT to form well-defined polymers with well-controlled molecular weights and structures. Enzymatic grafting by HRP occurred between the free radicals of well-defined polymers and free radicals of lignin on jute. Gel permeation chromatography (GPC) analysis indicated the alkyl chain length of polymers prepared via HRP-initiated RAFT polymerization was well-controlled. Other results of flourier transformed infrared spectroscopy (FTIR) and X-ray photoelectron spectroscopy (XPS) revealed that well-controlled alkyl chains prepared via enzymatic catalysis were grafted on the exposed lignin of jute. The study explores a new and eco-friendly modification method for lignin-based materials with the controlled graft chain structure via two different catalysis with HRP.

New strategy for grafting hydrophobization of lignocellulosic fiber materials with octadecylamine using a laccase/TEMPO system.

The enzymatic functionalization of lignocellulosic fibers using oxidoreductases was successfully achieved by targeting lignin moieties as grafting sites on the surface. In this study, a novel strategy for hydrophobization of lignocelluloses was investigated, which involved the laccase/TEMPO-mediated grafting of octadecylamine (OA) onto both lignin and cellulose components of jute fabrics. The results showed that OA monomers were successfully grafted onto jute fabric surface using the laccase/TEMPO system with the grafting percentage and efficiency values of 0.712% and 10.571%, respectively. The primary hydroxyl groups of cellulose were oxidized by laccase/TEMPO to carbonyl groups, which were then coupled with amino-contained OA monomers via Schiff base reaction. The phenolic hydroxyl groups of lignin were transformed by laccase to radicals, on which OA molecules were grafted via Michael addition reaction. Consequently, grafted jute fabrics showed a considerable increase in the surface hydrophobicity with a contact angle of 125.9° and a wetting time of at least 2 h. Furthermore, there was an acceptable decrease in the breaking strength of jute fabrics by 13.60%, and the color of fabrics turned yellowish and reddish. This eco-friendly enzymatic process provides a new strategy for grafting hydrophobization and even functionalization of lignocellulosic fiber materials using amino compounds.