Support For Immobilization Of Lipase Research Articles

Fabrication and characterization of epoxylated zwitterionic copolymer-grafted silica nanoparticle as a new support for lipase immobilization

Abstract Our previous work proved that the thermal stability of Candida rugosa lipase (CRL) immobilized on zwitterionic polymer (poly(carboxybetaine methacrylate)) grafted silica nanoparticle (SNP) was much higher than that on poly(glycidyl methecrylate) (pGMA) grafted SNP, while the latter showed significantly increased activity. Inspired by the research, we have herein proposed to synthesize copolymers of zwitterionic sulfobetaine methacrylate (SBMA) and GMA for CRL immobilization. The copolymers were grafted onto SNP surface at three GMA/SBMA (G/S) molar ratios (G100/S0, G50/S50, G10/S90), followed by the covalent coupling of CRL to the surface copolymers. The immobilized CRLs on the corresponding supports were denoted as p(G100-S0)-CRL, p(G50-S50)-CRL and p(G10-S90)-CRL. The enzyme loading increased with the increase of GMA content in the copolymer, while the activity varied with the grafted copolymer composition. Kinetic study proved the improvement of enzyme-substrate affinity after immobilization. In comparison to p(G100-S0)-CRL, p(G50-S50)-CRL and p(G10-S90)-CRL presented remarkably enhanced thermal stability and pH tolerance, and p(G10-S90)-CRL showed the highest stability. These results suggest that the copolymer design is promising for development as a versatile platform for enzyme immobilization.

Immobilization on octyl‐agarose beads and some catalytic features of commercial preparations of lipase a from Candida antarctica (Novocor ADL): Comparison with immobilized lipase B from Candida antarctica

Lipase A from Candida antarctica (CALA, commercialized as Novocor ADL) was immobilized on octyl-agarose, which is a very useful support for lipase immobilization, and coated with polyethylenimine to improve the stability. The performance was compared to that of the form B of the enzyme (CALB) immobilized on the same support, as both enzymes are among the most popular ones used in biocatalysis. CALA immobilization produced a significant increase in enzyme activity vs. p-nitrophenyl butyrate (pNPB) (by a factor of seven), and the coating with PEI did not have a significant effect on enzyme activity. CALB reduced its activity slightly after enzyme immobilization. Octyl-CALA was less stable than octyl-CALB at pH 9 and more stable at pH 5 and, more clearly, at pH 7. PEI coating only increased octyl-CALA stability at pH 9. In organic solvents, CALB had much better stability in methanol and was similarly stable in acetonitrile or dioxane. In these systems, the PEI coating of octyl-CALA permitted some stabilization. While octyl-CALA was more active vs. pNPB, octyl-CALB was much more active vs. mandelic esters or triacetin. Thus, depending on the specific reaction and the conditions, CALA or CALB may offer different advantages and drawbacks. © 2018 American Institute of Chemical Engineers Biotechnol. Prog., 35: e2735, 2019.

Design and characterization of immobilized biocatalyst with lipase activity onto magnetic magnesium spinel nanoparticles: A novel platform for biocatalysis.

Lipases (EC 3.1.1.3) are very used industrial enzymes but presents drawbacks such as lack of stability, and poor recyclability. Most of these obstacles can be solved by lipase immobilization. The objective of this work was evaluated to magnetic magnesium spinel nanoparticles as support for lipase immobilization by covalent bound. The techniques used for nanoparticles synthesis presented advantages in the size selection of the nanoparticles obtained (60-100 nm). The immobilization of Candida rugosa lipase (CRL) was optimized. The optimal conditions were determined to be pH 3.7, enzyme concentration of 1.1 mg/mL at 4 °C and an ionic strength of 100 mM. The CRL@MgFe2O4 activity obtained was 3.2 times over the starting conditions (4.03 U/mL). The immobilization of the lipase on Fe3O4 was evaluated and compared. The activity of the CRL@MgFe2O4 was 61% higher than CRL@Fe3O4 and 22% higher than free enzyme. CRL@MgFe2O4 improved the lipase stability at alkaline pH, hydrophilic solvent and high temperatures. The thermogravimetric analysis showed that this new biocatalyst was more stable compared to the free enzyme. Additionally, the immobilized lipase was recycled by magnetic force and used in ten catalysis cycles. The performance of the recycle was improved using butanol or Triton X 100 during washing. Finally, CRL@FeMg2O4 showed hydrolysis and synthesis activity. Thus, CRL@FeMg2O4 as a novel biocatalyst generation presents interesting properties for industrial applications.

Extraction of nanosilica from oil palm leaves and its application as support for lipase immobilization

The study reports the preparation of a composite consisting of magnetite coated with nanosilica extracted from oil palm leaves (OPL) ash as nanosupports for immobilization of Candida rugosa lipase (CRL) and its application for the synthesis of butyl butyrate. Results of immobilization parameters showed that ∼ 80% of CRL (84.5 mg) initially offered was immobilized onto the surface of the nanosupports to yield a maximum protein loading and specific activity of 67.5 ± 0.72 mg/g and 320.8 ± 0.42 U/g of support, respectively. Surface topography, morphology as well as information on surface composition obtained by Raman spectroscopy, atomic force microscopy, field emission scanning electron microscopy and transmission electron microscopy showed that CRL was successfully immobilized onto the nanosupports, affirming its biocompatibility. Under optimal conditions (3.5 mg/mL protein loading, at 45 ℃, 3 h and molar ratio 2:1 (1-butanol:n-butyric acid) the CRL/Gl-A-SiO2-MNPs gave a maximum yield of 94 ± 0.24% butyl butyrate as compared to 84 ± 0.32% in the lyophilized CRL. CRL/Gl-A-SiO2-MNPs showed an extended operational stability, retaining 50% of its initial activity after 17 consecutive esterification cycles. The results indicated that OPL derived nanosilica coated on magnetite can potentially be employed as carrier for lipase immobilization in replacement of the non-renewable conventionalsilica sources.

Highly stable adsorptive and covalent immobilization of Thermomyces lanuginosus lipase on tailor-made porous carbon material

Hierarchically structured, porous carbon materials (PCM) were synthesized by sucrose infiltration into template material and subsequent carbonization. Three porous carbon materials were prepared using porous concrete (PCM-01) or silica gel (PCM-02 and 03) as template. Carbon particles from 125 to 200 μm were generated. Surface carboxylic group density was determined with 1.1 mmol/g dry material for each variant. Firstly, tailor-made PCM was evaluated as suitable support for lipase immobilization. Recombinant produced lipase of Thermomyces lanuginosus (TLL) was used as model enzyme. Two independent crude immobilization strategies were applied. Residual activities of up to 8.6 U/g and 31 U/g dry material for adsorptive and covalent immobilization (linkage via EDC) were achieved, respectively. Additionally, TLL was immobilized on commercially available polymethacrylate support showing similar residual lipase activities. Secondly, covalent immobilization was optimized to generate reproducible, highly stable and active immobilizates. Optimized covalent immobilizates showed residual activities of up to 10 U∙g−1 dry carbon material using p-nitrophenyl-palmitate assay and protein loads of up to 45 mg g−1 dry carbon material. Covalent bound TLL-PCM showed storage stability for 12 months, remaining 100% of the initial activity. Operational stability resulted in stable and 100% active immobilizates over five consecutive cycles of use. Experiments showed that tailor-made porous carbon material is a promising support for lipase immobilization, which is adaptable in shape and dimension.

Novel nanohybrid biocatalyst: application in the kinetic resolution of secondary alcohols

In this work, a nanohybrid material was developed and used for the first time to the kinetic resolution of secondary alcohols as rac-indanol, rac-1-phenylethanol (rac-1), rac-1-(3-bromophenyl)-1-ethanol (rac-2) and rac-1-(3-methylphenyl)-1-ethanol (rac-3). Chiral indanol is used as a precursor intermediate for the synthesis of enantiomeric drugs, such as (+)-Indatraline, Irindalone, Indinavir, (+)-Sertraline and Rasagiline mesylate. Chiral 1-phenylethanol is used as an ophthalmic preservative, a solvatochromic dye and an inhibitor of cholesterol absorption and as a mild floral fragrance. For this purpose, the ultrasound irradiation was used to couple APTES on the superparamagnetic nanoparticles surface. Then, the system was activated with glutaraldehyde and used as a support for immobilization of lipase from Pseudomonas fluorescens. Thermal stability analysis was performed in buffer and hexane, showing an excellent stability in buffer solution at 60 °C, holding 72% of the initial activity, even after 7 h. In hexane (40 °C), the immobilized enzyme retained 100% of activity with 693 min of half-life time at 50 °C. The high thermal stability is mainly related to the covalent bonding between enzymes and support. Immobilized lipase on magnetic support proved to be a robust biocatalyst in the kinetic resolution, leading to (S)-indanol with high selectivity (e.e. > 99%, E > 200) in 1.75 h at 50 °C, being reused five times without significant loss of the activity and selectivity. The kinetic resolution of rac-1, via acetylation reaction, catalyzed by lipase from Pseudomonas fluorescens immobilized on magnetic support, led to (R)-acetate with enantiomeric excess > 99% and to the remaining (S)-alcohol with enantiomeric excess of 94%, conversion of 49% and E > 200, after 48 h of reaction at 40 °C. Under the same reactions conditions, rac-2 and rac-3 were slightly less reactive, since the corresponding (R)-acetates were obtained with conversion values of 44%, but with high enantioselectivity (enantiomeric excesses > 99% and E values > 200). These results correspond to an important step in heterogeneous catalysis due to the ability to obtain important precursors for the synthesis of enantiomerically pure chiral drugs and other bioactive substances.

Poly(carboxybetaine methacrylate)-functionalized magnetic composite particles: A biofriendly support for lipase immobilization

In this work, poly(carboxybetaine methacrylate) as an extremely hydrophilic polymer was modified on superparamagnetic Fe3O4 nanoparticles (pCB-Fe3O4), which were employed to immobilize porcine pancreatic lipase. The properties of immobilized lipase were investigated in comparison with the free enzyme counterpart. Enzymatic stability, reusability, and activity of the immobilized lipase were found significantly superior to that of the free lipase. In particular, at an elevated temperature of 60°C, the immobilized lipase retained 50% of its initial activity after 150min, while the free enzyme displayed only one-third activity of the immobilized enzyme. Besides, the immobilized lipase retained >60% of its initial activity after 7 cycles. Furthermore, the value of Kcat/Km indicated the catalytic efficiency of the immobilized lipase was increased by 50% compared to that of the free one. The pCB-Fe3O4 particles displayed non-cytotoxicity, while the naked Fe3O4 particles caused only 50% viability of NIH 3T3 cells. These results showed that pCB-Fe3O4 composite particles had higher efficiency and improved stability for lipase immobilization, which are more promising for industrial scale up of biocatalytic systems with excellent biocompatibility.

Biochemical characterization and stability assessment of Rhizopus oryzae lipase covalently immobilized on amino-functionalized magnetic nanoparticles

Amino-functionalized magnetic nanoparticles (Fe3O4) have been investigated as a support for covalent immobilization of lipase. The nanoparticles were prepared by chemical coprecipitation method and subsequently were coated with 3-aminopropyltriethoxysilane (APTES) via silanization reaction. With glutaraldehyde, as the coupling agent, the lipase from Rhizopus oryzae was successfully immobilized onto the amino-functionalized magnetic nanoparticles. The synthesized support was characterized by transmission electron microscopy and Fourier transform infrared spectroscopy. The results showed that the load of immobilized protein could reach as high as 7mg protein g−1 support. The optimum pH for maximal catalytic activity of the immobilized enzyme was 8.0 at 40°C. The Km values were found as 0.66 and 0.57mgmL−1 for the free and immobilized enzymes, respectively. The Vmax values for the free and immobilized enzymes were calculated as 0.14 and 0.47μmolmg−1min−1, in turn, when p-nitrophenyl butyrate (pNPB) was used as the substrate. A quick separation of lipase from the reaction mixture was achieved when a magnetically active support was applied. In comparison to the free enzyme, the immobilized enzyme was thermally stable and was reusable for 10 cycles while retaining 64% of its initial activity.

Performance of Chitosan/Glycerol Phosphate Hydrogel as a Support for Lipase Immobilization

A biocompatible and biodegradable hybrid chitosan/glycerol phosphate hydrogel (CS-GP) was prepared and evaluated as support for enzyme immobilization. In this work a lipase sn-1,3 specific from Rhizopus oryzae was physically immobilized in CS-GP by adsorption (PA) and in CS-GP modified chemically with glutaraldehyde (CS-GP-GA) by covalent attachment (CA). The matrices (pure and chemically modified) and immobilized lipases were characterized by scanning electron microscopy (SEM), Fourier Transform Infrared Spectroscopy (FTIR) and thermogravimetric (TG) analysis. Moreover, a comparative study between free and immobilized lipase was provided in terms of pH, temperature, kinetic parameters and thermal stability. The catalytic properties of biocatalysts were assayed in olive oil hydrolysis. The maximum activities were found at 60◦C/pH 8.5 and 50◦C/pH 7.5 for lipase immobilized by PA and CA, respectively. Both immobilization process turned biocatalysts highly active, since they were stable for 120 days at low (-10◦C) temperatures and around 2-fold more stable than free lipase at 60◦C (high temperature). Thus, results revealed the potential application of chitosan/glycerol phosphate hydrogel (CS-GP) as matrix for lipase immobilization. Nevertheless, better performance was achieved when the lipase was immobilized by covalent attachment.

Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization

The main purpose of the study was to achieve effective immobilization of lipase B from Candida antarctica (CALB) onto 3D spongin-based scaffolds from Hippospongia communis marine demosponge for rapeseed oil transesterification. Successful immobilization onto the marine sponge skeleton was confirmed for the first time. Lipase B-containing biocatalytic system exhibited the highest catalytic activity retention (89%) after 60 min of immobilization at pH 7 and temperature of 4 °C. Immobilization was found to improve the thermal and chemical stability compared to free lipase, and retain over 80% of its initial catalytic activity over a wide range of temperature (30–60 °C) and pH (6–9). Additionally, immobilized lipase has good storage stability and retains over 70% of its initial activity even after catalyzing of 25 reaction cycles. The obtained product was used in a transesterification reaction of rapeseed oil with methanol and proved to be an efficient biocatalyst for biofuel production. The highest conversion value and fatty acids methyl esters (FAME) concentration were observed after a process conducted at 40 °C and pH 10. The possible mechanism of interaction between the enzyme and the spongin-based support is proposed and discussed.

Amperometric biosensor for detection of triglyceride tributyrinbased on zero point charge of activated carbon

A simple and robust single enzyme biosensor was fabricated for triglyceride (TG) detection. Graphite rods were modified with activated carbon (AC) and used as support for lipase immobilization. Chitosan (CHIT) was eventually used to create film on the bioelectrode and retain the immobilized enzyme. To extend the linear range of TG detection, AC was functionalized with carboxyl and then amine groups (AAC) to enhance the isoelectric point of AC. The constructed graphite/AAC/lipase /CHIT bioelectrode was characterized using cyclic voltammetry and field emission scanning electron microscopy (FE-SEM). The accuracy of the developed biosensor was assessed through determination of different concentrations of tributyrin (TB) in buffer solution. Linear responses were found for TB concentration in the range of 50 to 350 mg dL-1 with a detection limit of 9.9 mg dL-1. The biosensor showed good sensitivity of 0.16 μA mg-1 dL. The detected level of TG in several human serum specimens using the constructed biosensor was in good agreement with the results of an automatic biochemical analyzer. The fabricated biosensor was not affected by a number of human serum materials and showed a strong anti-interference ability. The relative standard deviation in reproducibility and repeatability tests was 3.46% and 2.94%, respectively.

New Tailor-Made Alkyl-Aldehyde Bifunctional Supports for Lipase Immobilization

Immobilized and stabilized lipases are important biocatalytic tools. In this paper, different tailor-made bifunctional supports were prepared for the immobilization of a new metagenomic lipase (LipC12). The new supports contained hydrophobic groups (different alkyl groups) to promote interfacial adsorption of the lipase and aldehyde groups to react covalently with the amino groups of side chains of the adsorbed lipase. The best catalyst was 3.5-fold more active and 5000-fold more stable than the soluble enzyme. It was successfully used in the regioselective deacetylation of peracetylated d-glucal. The PEGylated immobilized lipase showed high regioselectivity, producing high yields of the C-3 monodeacetylated product at pH 5.0 and 4 °C.

Activated carbons preparation from yellow mombin fruit stones for lipase immobilization

Activated carbons were prepared from yellow mombin fruit stones as carbon precursor and subsequently used as support for lipase immobilization. Carbons were prepared by chemical activation method using phosphoric acid or potassium hydroxide as activating agents. The influence of the activating agent and the carbonization temperature on the physical and chemical properties of carbons was investigated. Although carbon specific surface area increased with increasing activation temperature, there was a reduction in the number of surface functional groups. The activation with phosphoric acid resulted in higher yields and favored a higher surface area and pore volume of carbon. The optimum conditions for lipase immobilization onto activated carbons were carried out varying contact time, pH, initial enzyme concentration, and temperature. The immobilized enzymes showed good activity in both carbons, and can be considered a promising alternative as support for lipase immobilization.

Amine-functionalized magnetic nanoparticles as robust support for immobilization of Lipase

Preparation of magnetic nanoparticles with controlled size and shape along with modulation of their surface properties via introduction of functional groups holds great prospect in the field of nanotechnology. Superparamagnetic, aqueous dispersible iron oxide nanoparticles (Fe3O4) with amine-functionalized surface were prepared through solvothermal method, using poly(ethylene imine) (PEI), ethanolamine (EA), and 2,2 ′-(ethylenedioxy)bis(ethylamine) (EDBE) as amine precursors. These aminated nanoparticles were used as support for the immobilization of lipase, an important industrial enzyme. Lipase was immobilized via glutaraldehyde coupling agent. These functionalized nanoparticles were characterized by XRD, FTIR, TEM, FESEM and VSM analysis. The maximum activity was obtained for the lipase immobilized on EDBE modified Fe3O4 nanoparticles. The lipase immobilized on EDBE-Fe3O4 depicted 83.9% relative activity with respect to the same amount of free lipase. Moreover, lipase immobilized on EDBE-Fe3O4 nanoparticles demonstrated good thermal and storage stability, and easy reusability. The kinetic parameters of lipase immobilized on EDBE-Fe3O4 were compared with those of free lipase and the apparent Michaelis-Menten constant of immobilized lipase was found to be nearly same as that of free lipase.

Immobilization of Candida antarctica Lipase B on Magnetic Poly(Urea-Urethane) Nanoparticles.

Poly(urea-urethane) (PUU) nanoparticles with encapsulated superparamagnetic magnetite (Fe3O4) were obtained by interfacial miniemulsion polymerization and used as support for immobilization of lipase B from Candida antarctica (CALB). CALB enzyme was immobilized on magnetic PUU nanoparticles in two steps. The enzyme was immobilized in the lyophilized nanoparticles (magnetic PUU) after the support synthesis in phosphate buffer (pH 7.6) containing CALB, by the contact between nanoparticles and enzymatic solution. The mixture was incubated at 30°C in an orbital shaker during 0.5 until 6h to determine the time for maximum immobilization efficiency. The enzyme activity was determined by esterification reactions between lauric acid and propanol. Residual activities above 95% in relation to free enzyme were obtained in 1h of immobilization with enzyme concentration of 0.55mg/mL. FTIR spectrum and SEM-FEG images were used to confirm the presence of CALB on magnetic support after immobilization and stability of support even after immobilization process, respectively. Thermal (40, 60, and 80°C) and pH (pH 4, 7, and 10) stabilities, storage stability, and reuse were evaluated. CALB immobilized derivatives showed high stabilities with residual activities of 95, 100, and 100% at 40, 60, and 80°C, respectively, in 6h of incubation. After incubation in different pH values, CALB immobilized derivative presented activities of 81, 76, and 69% in relation to activities in the beginning of the stabilization process in pH 4, 7, and 10, respectively. Furthermore, CALB immobilized derivative reduces only 15% of its activity after 30days of storage at 4°C. Reuse results showed that immobilized CALB on magnetic PUU nanoparticles led to 95% of geranyl oleate conversion after 8cycles of application demonstrating high stability of the CALB immobilized derivative under different conditions.

Epoxy-silanization - tool for improvement of silica nanoparticles as support for lipase immobilization with respect to esterification activity

BACKGROUND In this study, in order to obtain the best support for the immobilization of lipase from Candida rugosa (CRL), the procedure for chemical modification of fumed silica nanoparticles (FNS) with (3-Glycidyloxypropyl)trimethoxysilane (GOPTMS) was optimized by varying the amount of GOPTMS used and the duration of support modification. To evaluate the prospects of chemical modification of FNS surface on the immobilization process, the activity and thermal stability of lipase immobilized on GFNS was compared with lipase immobilized on FNS and cyanuric chloride functionalized amino silica (CCAFNS). RESULTS The epoxy functionalized silica nanoparticles (GFNS) with 400–500 µmol of introduced epoxy groups per g of support were the most efficient, since immobilized preparations in 1 mol L−1 buffer had the highest activity of approximately 1495 IU g−1 and a loading capacity of 294 mg g−1. Lipase immobilized on GFNS exhibited 1.5-fold higher hydrolytic activity and 2-fold higher esterification activity in the synthesis of aroma esters than lipase immobilized on CCAFNS, while its thermal stability was similar to CCAFNS preparations. CONCLUSION These results indicated that the type of modification of the FNS surface has an influence on the specificity of the immobilized lipase, since lipase immobilized on GFNS showed improved properties for ester synthesis which is a promising area for immobilized lipase application. © 2015 Society of Chemical Industry

Fabrication and characterization of core-shell magnetic chitosan nanoparticles as a novel carrier for immobilization of Burkholderia cepacia lipase.

In this study, the chitosan magnetic core-shell nanoparticles (CMNPs) was synthesized and then used as a support for immobilization of lipase. The characteristics of CMNPs, including morphology, topography and spectra type before and after immobilization were determined. The scanning electron micrographs of the CMNPs showed that they were approximately uniform spheres and the distribution chart indicated that the particles have the mean diameter of 100 nm. Kinetic parameters of Km and Vm were calculated as 1.07 mM and 29.43 U/mg for free B. cepacia lipase and 1.29 mM and 25.82 U/mg for immobilized lipase on CMNPs, respectively. The activity of immobilized lipase was 32 U/mg under optimum temperature and pH. CMNP's were used in trasesterification reaction in order to evaluate the activity of the immobilized enzyme compared to the free enzyme. Immobilization of lipase on CMNPs improved stability and total relative activity of the enzyme. It could be concluded that CMNPs be considered as a suitable carrier for enzyme immobilization.

Poly (lactic acid)/chitosan fiber mats: Investigation of effects of the support on lipase immobilization

The greatest challenge for biotechnological processes is to have immobilized enzymes acting as good green catalysts with high reusability rates. In this work, we have produced electrospun fibers from poly (lactic acid)/chitosan blends. Further, we evaluated the influence of these materials as support for lipase immobilization. The PLA/chitosan fiber mats were composed by non-woven nanofibers, with diameters ranging from 200nm to 1.3μm. The solvent (TFA) as well as the chitosan addition influenced morphology, hydrophobicity and mechanical properties of PLA nanofibers. It was observed that even for lower concentration of lipase (5U) higher enzyme activity retention was detected in the PLA/chitosan blends. In addition, a remarkable improvement of lipase activity on pure PLA fiber mat was verified, indicating that most of the enzymes were probably in their active form.

Influence of the morphology of core-shell supports on the immobilization of lipase B from Candida antarctica.

Core-shell polymer particles with different properties were produced through combined suspension-emulsion polymerizations and employed as supports for immobilization of lipase B from Candida antarctica. In order to evaluate how the morphology of the particles affects the immobilization parameters, empirical models were developed to describe the performance of the biocatalysts as a function of the specific area, volume of pores and average pore diameter of the supports. It was observed that the average pore sizes did not affect the enzymatic activities in the analyzed range of pore sizes. It was also observed that the increase of the specific area (and of the volume of pores) led to higher enzyme loadings, also leading to an increase in the esterification activity, as expected. However, when the specific area (and volume of pores) increased, the hydrolytic activity and the retention of hydrolytic activity of the biocatalysts decreased, indicating the existence of diffusional limitations for some hydrolytic reactions, probably because of the high reaction rates.

Amino silicones finished fabrics for lipase immobilization: Fabrics finishing and catalytic performance of immobilized lipase

Finishing of silk fabric was achieved by using amino-functional polydimethylsiloxane (PDMS) and lipase from Candida sp. 99-125 was immobilized on the treated silk fabrics. Hydrophobic fabrics were obtained by dipping the native fabric in 0.125–0.25% (w/v) PDMS solution and dried at 70°C. The direct adsorption on PDMS-treated fabric was verified to be a better strategy for lipase immobilization than that by covalent binding. Compared to unfinished fabrics, the hydrolytic activity of immobilized enzyme on the finished fabric was improved by 1.6 times. Moreover, the activity of immobilized enzymes on hydrophobic fabrics was significantly improved in different concentrations of strong polar solvents such as methanol and ethanol, and in common organic solvents with different octanol–water partition coefficients (LogP). Enzymatic activity and stability in 15% water content system (added water accounted for the total reaction mixtures, v/v) showed more than 30% improvement in each batch. The amino–silicone finished fabric surface was investigated by scanning electron microscopy and X-ray photoelectron spectroscopy. The hydrophobic fabric immobilized enzyme could be recycled for more than 80 times with no significant decrease in esterification activity. PDMS-treated woven silk fabrics could be a potential support for lipase immobilization in catalytic esterification processes.