Hydrolytic Activity Of Lipase Research Articles

Comparison of enzymatic activities of lipases from Burkholderia plantarii and Burkholderia cepacia.

Lipases (EC 3.1.1.3) are enzymes used in the oils and fats industries to modify the physicochemical properties of triacylglycerol (TAG). Lipase-catalyzed interesterification at high temperatures is an effective method for modifying the physicochemical properties of TAG. The lipase from Burkholderia plantarii (BpL) exhibits excellent catalytic activity for non-regiospecific interesterification at high temperatures, with depressed lipase hydrolytic activity. The detailed catalytic mechanism for reactions involving catalytic residues has not been elucidated because of the lack of a conventional method for estimating interesterification activity. We used our original water-in-oil emulsion system to estimate the interesterification activity of lipases. BpL showed 10% hydrolytic and 140% interesterification activities compared to the lipase from Burkholderia cepacia, which has a high sequence homology with BpL. By comparing the sequence and crystal structure data of the lipases, we clarified that two amino acids near the active center are one of the factors controlling the hydrolytic and interesterification activities of the enzyme.

Nanoemulsion containing Yellow Monascus pigment : Fabrication, characterization, storage stability, and lipase hydrolytic activity in vitro digestion

The natural pigment of monascus is favored by human for its special coloring and physiological activity, and its development and application have attracted much attention. In this study, a novel corn oil-based nanoemulsion encapsulated with Yellow Monascus Pigment crude extract (CO-YMPN) was successfully prepared via the phase inversion composition method. The fabrication and stable conditions of the CO-YMPN including Yellow Monascus pigment crude extract (YMPCE) concentration, emulsifier ratio, pH, temperature, ionic strength, monochromatic light and storage time were investigated systemically. The optimized fabrication conditions were the emulsifier ratio (5:3 ratio of Tween 60 to Tween 80) and the YMPCE concentration (20.00% wt%)). Additionally, the DPPH radical scavenging capability of the CO-YMPN (19.47 ± 0.52%) was more excellent than each YMPCE or corn oil. Moreover, the kinetic analysis results based on Michaelis-Menten equation and constant revealed that CO-YMPN could improve lipase hydrolysis capacity. Therefore, the CO-YMPN complex had excellent storage stability and water solubility in the final water system, and the YMPCE showed brilliant stability.

Synthesis of pyridinium-based ionic liquids and their application to improve Candida rugosa lipase stability in a methanol-water solvent system.

This paper studied the effect of pyridinium-based ionic liquids as cosolvents in a methanol-water solvent system on the hydrolytic activity of Candida rugosa lipase. These ionic liquids were successfully synthesized using imidazolium-based ionic liquid synthesizing methods with a certain adjustment. The hydrolytic activity of Candida rugosa lipase was analyzed using 4-nitrophenol acetate (pNPA) and 4-nitrophenol palmitate (pNPP) as substrates. The addition of ionic liquids had no significant effect on the hydrolytic activity of lipase in a water solvent, and it had a greater effect in methanol. The addition of [C6Py] Br ionic liquid as a methanol cosolvent (methanol: ionic liquid, 10:5) could increase the hydrolytic activity of lipase. The use of ionic liquid as a cosolvent could increase the hydrolytic activity of lipase by about 15.61% while using pNPP as a substrate in the methanol system. A molecular dynamics study for the interaction between lipase and ionic liquids supported the experimental results. The ionic liquid using bromide as an anion provided more stability on lipase conformation. It tends to form the short-range interaction between the lipase and bromide anion.

Jet cutter technique as a tool to achieve high lipase hydrolytic activity

Lipase immobilization has been widely studied because it allows for enzyme reuse and provides more assertive control over the catalytic process. This study aimed to evaluate the effect of bead size on the performance of entrapped lipase. Eversa® Transform 2.0 was immobilized on calcium alginate beads by jet cutting and dripping. Beads produced by jet cutting were small (D[3,4] = 803.36 ± 16.9 µm) and had a relatively narrow size distribution (span of 0.79). Beads obtained by extrusion dripping measured 2459.98 ± 15.6 µm and had a span of 0.45. Infrared spectroscopy and microscopic analysis confirmed the presence of lipase in both types of beads. Lipase showed high hydrolytic activity in its free form (15,000 U g−1). Immobilization in calcium alginate was effective but decreased recovered enzyme activity. The porosity of loaded beads varied with size. The high surface area (5.46 vs 3.13 m2 g−1) and porosity (76.33% vs 21.65%) of beads produced by jet cutting, as compared with those produced by dripping, favored enzyme activity (3000 vs 1500 U g−1 protein). The results indicate that facilitated mass transfer is an important factor in the development of immobilized enzymes.

Development and characterization of enzymatic biosensor based on lipase from porcine pancreas for propylparaben detection

Purpose The purpose of this paper is to study the immobilization of porcine pancreatic lipase (PPL), in an organic matrix by a covalent cross-linking method to sense propylparaben (PP) present in aqueous solution. Design/methodology/approach PPL immobilization was performed by the covalent cross-linking method, using bovine serum albumin (BSA) in the presence of saturated glutaraldehyde vapor (GA). The preparation of the enzymatic membrane involves the incorporation of porcine pancreatic lipase (PPL), bovine serum albumin (BSA) and glycerol into a phosphate buffer solution (PBS). Characterization of this sensor was performed by impedance spectroscopy (EIS) and scanning electron microscope (SEM). The effect of experimental conditions such as PPL activity, potential, scan rate, PP concentration, pH and presence of interfering elements were studied by cyclic voltammetry. Findings Under the optimal experimental conditions, a number of significant factors were optimized. The method exhibited good linearity in the range of 10–14 to 10–9 mol/L with a good correlation coefficient of 0.957, detection limit (LOD) of 3.66 × 10–15 mol/L and high sensitivity of 1.086 mA mol−1L. The authors also obtained a very good coverage rate of the surface equal to 91.44%, and hydrolytic activity of lipase is evaluated to 26.64 mmol min−1. The stability and the interference were also evaluated. The equivalent circuit used to explain the electrochemical behavior of modified electrode is a Randle circuit. Practical implications The main application of biosensors is the detection of biomolecules that are either indicators of a disease. For example, electrochemical biosensing techniques can be used as clinical tools to detect breast tumors, because these compounds (PP) were found in breast tumors. Originality/value The result registered in this paper indicates that the developed sensor is an efficient, fast, simple and inexpensive analytical tool that can be used for the analysis of water containing PP.

Increasing Hydrolytic Activity of Lipase on Palm Oil by PCR-Based Random Mutagenesis

ABSTRACT
 Random mutagenesis technique is a powerful technique capable of producing enzymes with desired biocatalytic activity. This study aims to obtain a mutant lipase with improved hydrolytic activity on palm oil substrate using random mutagenesis technique. Random mutagenesis by error-prone PCR was used to generate mutant lipases. A total of 1101 mutants were obtained, out of which two mutants, Lip M14.25, and Lip M14.57, showed an increased relative hydrolytic activity. Lip M14.25 and Lip M14.57 demonstrated a 14% and 16% increased activity respectively. A comparison of the mutants' hydrolytic activities using p-nitrophenyl esters showed a significantly high preference for p-nitrophenyl palmitate. Furthermore, the mutant, Lip M14.25 showed its highest activity at pH 5, and Lip M14.57 exhibited a 10 oC decrease in optimum temperature. The two mutants' protein modelling showed the substitution of N44S/S202N on M14.25 and F154L/S265C on M14.57 lipase, which caused changes in conformation and active site residue distance of the lipase. The study found two mutants of lipase, M14.25 and M14.57, which showed improved hydrolytic activity on palm oil substrate.

Inhibition of CpLIP2 Lipase Hydrolytic Activity by Four Flavonols (Galangin, Kaempferol, Quercetin, Myricetin) Compared to Orlistat and Their Binding Mechanisms Studied by Quenching of Fluorescence.

The inhibition of recombinant CpLIP2 lipase/acyltransferase from Candida parapsiolosis was considered a key model for novel antifungal drug discovery and a potential therapeutic target for candidiasis. Lipases have identified recently as potent virulence factors in C. parapsilosis and some other yeasts. The inhibition effects of orlistat and four flavonols (galangin, kaempferol, quercetin and myricetin) characterized by an increasing degree of hydroxylation in B-ring, were investigated using ethyl oleate hydrolysis as the model reaction. Orlistat and kaempferol (14 µM) strongly inhibited CpLIP2 catalytic activity within 1 min of pre-incubation, by 90% and 80%, respectively. The relative potency of flavonols as inhibitors was: kaempferol > quercetin > myricetin > galangin. The results suggested that orlistat bound to the catalytic site while kaempferol interacted with W294 on the protein lid. A static mechanism of interactions between flavonols and CpLIP2 lipase was confirmed by fluorescence quenching analyses, indicating that the interactions were mainly driven by hydrophobic bonds and electrostatic forces. From the Lehrer equation, fractions of tryptophan accessibility to the quencher were evaluated, and a relationship with the calculated number of binding sites was suggested.

An improved method to measure lipase activity in aqueous media

An improved method based on the p-nitrophenyl long chain esters method is proposed for measuring lipase hydrolytic activity in aqueous media. Using ethylene glycol as co-solvent for hydrophobic p-nitrophenyl substrates in aqueous buffer, lipase activity is measured by following the release of p-nitrophenol.This fast and easy to handle method improves the solubility of both substrate and product, and also the stability of the substrate. It avoids the use of solvents such as ethanol or propanol, permits the comparison of all the p-nitrophenol acyl ester substrates and allows the influence of ions like Ca+2 to be studied, while avoiding turbidity in the reaction medium.

Production of Whole-Cell Lipase from Streptomyces clavuligerus in a Bench-Scale Bioreactor and Its First Evaluation as Biocatalyst for Synthesis in Organic Medium.

This work evaluated a wild-type Streptomyces clavuligerus strain as a whole-cell lipase (Sc-WCL) producer by submerged fermentation. In an orbital shaker, lipase hydrolytic activity of 3000UL-1, measured at pH9.0 and 37°C by using p-nitrophenyl palmitate as substrate, was achieved after 36h fermentation using glycerol-free production medium in a baffled Erlenmeyer flask at 28°C and pH6.8. Maximum productivity of 52.5UL-1h-1 was achieved after 24h in bioreactor using glycerol-free production medium at pH6.8 and 28°C, with agitation at 400rpm and aeration at 1vvm. Sc-WCL was shown to be more active at 60°C and pH10.7, while higher activity retention was observed at 30-40°C after 1h incubation at pH10. Sc-WCL showed to have potential to be used as biocatalyst in hydrolysis and esterification reactions. In the hydrolysis of p-nitrophenyl palmitate, lyophilized Sc-WCL expressed a hydrolytic activity (330unitsg-1 solid, measured at 37°C and pH9.0) around 100-fold higher than the ones declared by a supplier of lyophilized powders of mixtures of intracellular lipases from Thermus thermophiles and Thermus flavus (≥3.0unitsg-1 solid, measured at 65°C and pH8.0). In the synthesis of butyl butyrate in anhydrous medium, 85% ester conversion was achieved at 37°C after 8h reaction. Thus, Sc-WCL showed to be a promising biocatalyst because it is cheaper than the isolated and purified lipases.

Accessing regio-and typo-selectivity of Yarrowia lipolytica lipase in its free form and immobilized onto magnetic nanoparticles

The growing interest in lipases is related to its high biotechnological potential. In this work we investigated the regio- and typo-selectivity of extracellular lipase from Yarrowia lipolytica 583 (IMUFRJ 50682) in its free form and immobilized on magnetic nano-sized particles. Results of p-nitrophenyl laurate hydrolysis showed optimal stability of these biocatalysts at pH 6–8 and between 20 and 45°C. The immobilization of lipase on nano-sized magnetic particles increased thermo and pH stabilities of the enzyme. Both catalysts displayed high hydrolytic activity on triolein and on triacylglycerols in vegetable oils in 5min. The free lipase showed a strict 1,3-regioselectivity, whereas the immobilized lipase was only slightly 1,3-regioselective, in hydrolysis reactions of triolein and vegetable oils. Both lipases were able to hydrolyze saturated esters, but showed no typo-selectivity for this group. However, the lipases are selective for the hydrolysis of unsaturated esters, especially for 18:2 fatty acids. These results give a better knowledge of this lipase hydrolytic activity, both in the free form and immobilized and widen their potential biotechnological use, especially in the synthesis of structured lipids.

Biocatalytic characterization of a naturally immobilized lipase found in Araujia sericifera Brot. (Apocynaceae) latex

Lipase activity found in the insoluble fraction of Araujia sericifera Brot. (Apocynaceae) (ASL) latex, a native South American milkweed, was characterized by use of different test reactions and under different reaction conditions. In this context, hydrolytic lipase activity towards both natural and synthetic substrates and towards fatty acid esterifications was assayed at different temperatures, pH values, and biocatalyst loads. In the case of natural substrates (cottonseed oil), highest lipase activity was found at pH 8.5 and 60 °C. In the hydrolysis of synthetic substrates (p-nitrophenyl esters) the lipase showed preference for the lowest molecular-weight p-nitrophenyl ester assayed (butyrate). Results of the direct esterification of fatty acids of different chain length in organic media showed that esterification levels of up to 45% could be obtained in one hour of reaction. Activity results were compared with the activity shown by the commercial immobilized lipase Novozym 435 under defined reaction conditions. The high activity exhibited by ASL in the hydrolysis of natural substrates and particularly in the direct esterification of different fatty acids in organic medium, together with its high storage stability, suggests that this plant lipase is a promising biocatalyst for various biotechnological applications.

Effect of imidazolium ionic liquids on the hydrolytic activity of lipase

The effect of 1-alkyl-3-methylimidazolium ionic liquids (ILs) on the hydrolysis activityof Candida rugosa lipase (CRL) toward triacylglycerol was investigated. The critical micelle concentrations (CMC) of ILs with Br − , Cl − , and [BF 4 ] − anions and the solubility of ILs with [PF 6 ] − anions were determined in phosphate buffer. Results suggested that the content of the ILs, not kosmotropicity, highly influenced the effects of anions and cations of ILs on CRL activity. As the length of alkyl chain of the cation [C n MIM] + increased, lower IL content was required to achieve high enzyme activity. Once the concentrations of the ILs with Br − , Cl − , and [BF 4 ] − anions exceeded the CMC value, enzyme activity was suppressed. The positive promotion effect of anions on enzyme activity was in the order of Br − Cl − [BF 4 ] − [PF 6 ] − . The effect of ionic liquid on enzyme activity was highly dependent on the pH and temperature of the system, with the optimum pH being 7.000. Under optimal conditions of pH 7.000, 30 °C, and 47.6 mmol/L of [C 8 MIM]Br, the highest relative activity of CRL (1734%) was achieved, with a specific activity of 54.4 U/mg protein. 考察了1-烷基-3-甲基咪唑类离子液体对柱状假丝酵母脂肪酶(CRL)催化橄榄油水解反应活性的影响, 14;利用电导法确定了磷酸盐缓冲液中Br − , 14;Cl − , 14;[BF 4 ] − 系列咪唑离子液体的临界胶束浓度(CMC)和[PF 6 ] − 系列咪唑离子液体的溶解度. 结果显示, 14;离子液体的阴、阳离子对酶活性的影响规律与离子液体的Kosmotropicity性质无明显关联, 14;但与离子液体在体系中的含量密切相关, 14;在最适离子液体含量时, 14;酶活性达到最高; 阳离子[C n MIM] + 中的 n 越大, 14;可促进酶活性的离子液体适宜含量越低; Br − , 14;[BF 4 ] − 系列离子液体的浓度超过CMC时则抑制酶活; 阴离子对酶活性的最大促进作用顺序为Br − >Cl − >[BF 4 ] − >[PF 6 ] − . 离子液体对酶活性的影响随体系pH和温度的不同而改变, 14;在最适离子液体浓度时的最适pH均为7.000. 在pH 7.000, 14;30°C以及[C 8 MIM]Br离子液体浓度为47.6 mmol/L的最佳条件下, 14;最高相对酶活力和比活力分别达到1734%和54.4 U/mg protein. Lipase hydrolytic activity was strongly affected by the concentrations, cation structure and anion type of the ILs. The beneficial effect of the IL on lipase activity was eliminated as the IL approached its CMC.

Effect of Metal Ions on the Hydrolytic and Transesterification Activities of Candida rugosa Lipase

In order to study the effect of metal ions on lipase activity, hydrolytic and transesterification activities of Candida rugosa lipase were investigated in presence of alkali (Na⁺ and K⁺), alkaline earth (Ca⁺² and Ba⁺²) and transition (Cr⁺³, Fe⁺³, Co⁺², Cu⁺² and Ni⁺²) metal ions. Maximum enhancement in hydrolytic activity of lipase was observed by Ca⁺², and in transesterification activity by Cr⁺³ and Co⁺². The kinetics of the lipase catalyzed transesterification (methanolysis and ethanolysis) reactions were also studied, and the activation energies of methanolysis and ethanolysis were reduced from 10.16 and 10.24 kcal mol⁻¹, respectively, to 5.41 and 7.55 kcal mol⁻¹, respectively, when reactions were performed in presence of Co⁺². Thus, in lipase catalyzed transesterification Cr⁺³ or Co⁺² could be added to the assay in order to produce the biodiesel in relatively shorter reaction duration.

Selection of lipase producing yeasts for methanol-tolerant biocatalyst as whole cell application for palm-oil transesterification

Methanol-tolerant lipase producing yeast was successfully isolated and selected thorough ecological screening using palm oil-rhodamine B agar as one step-approach. All 49 lipase-producing yeasts exhibited the ability to catalyze esterification reaction of oleic acid and methanol at 3 molar equivalents. However, only 16 isolates catalyzed transesterification reaction of refined palm oil and methanol. Rhodotorula mucilagenosa P11I89 isolated from oil contaminated soil showed the strongest hydrolytic lipase activity of 1.2U/ml against palm oil. The production of oleic methyl ester and fatty acid methyl ester (FAME) of 64.123 and 51.260% was obtained from esterification and transesterification reaction catalyzed by whole cell of R. mucilagenosa P11I89 in the presence of methanol at 3 molar equivalents against the substrates, respectively. FAME content increased dramatically to 83.29% when 6 molar equivalents of methanol were added. Application of the methanol-tolerant-lipase producing yeast as a whole cell biocatalyst was effectively resolved major technical obstacles in term of enzyme stability and high cost of lipase, leading to the feasibility of green biodiesel industrialization.

Study of the Interaction of Pancreatic Lipase with Procyanidins by Optical and Enzymatic Methods

The interactions between porcine pancreatic lipase (PL) and grape seed procyanidins were studied by an enzymatic assay, fluorescence quenching, nephelometry, and dynamic light scattering (DLS). An inhibitory effect of grape seed procyanidins on lipase hydrolytic activity was found. Both the inhibition of lipase activity by procyanidins and the respective quenching of intrinsic protein fluorescence increased with the average degree of polymerization of the tested procyanidins. The association between procyanidins and enzyme involves a specific interaction as inferred from the fluorescence assays despite not changing significantly the tertiary structure of the protein. For all tested procyanidins it was shown, both by DLS and by nephelometry, that an increase in aggregation occurs up to a stoichiometric maximum after which further procyanidin addition causes a decrease in aggregation of aggregates. The maximum size of aggregates was shown to be closely related to the maximum overall aggregation. It was also shown that the inhibition of enzyme activity is to a large extent independent of the formation of aggregates.

Suppressed Native Hydrolytic Activity of a Lipase to Reveal Promiscuous Michael Addition Activity in Water

AbstractSuppression of the native hydrolytic activity of Pseudozyma antarctica lipase B (PalB) (formerly Candida antarctica lipase B) in water is demonstrated. By replacing the catalytic Ser 105 residue with an alanine unit, promiscuous Michael addition activity is favored. A Michael addition reaction between methyl acrylate and acetylacetone was explored as a model system. For the PalB Ser 105 Ala mutant, the hydrolytic activity was suppressed more than 1000 times and, at the same time, the Michael addition activity was increased by a factor of 100. Docking studies and molecular dynamics simulations revealed an increased ability of the PalB Ser 105 Ala mutant to harbor the substrates close to a catalytically competent conformation.

Improvement of a Candida antarctica lipase B-displaying yeast whole-cell biocatalyst and its application to the polyester synthesis reaction

A Candida antarctica lipase B (CALB)-displaying yeast whole-cell biocatalyst was constructed with the integration of the CALB cell-surface display expression cassette in the yeast genome and cell fusion by mating. Lipase hydrolytic activity of the yeast whole-cell biocatalyst subsequently increased, in both a- and alpha-type yeast cells, with the number of copies of the CALB cell-surface display expression cassette introduced, and reached 43.6 and 32.2 U/g-dry cell at 168 h cultivation, respectively. The lipase hydrolytic activity of whole cells in diploid yeast cells containing eight copies of the CALB cell-surface expression cassette reached 117 U/g-dry cell, and this value is approximately ninefold higher than that of the previously reported haploid CALB cell-surface displaying yeast using a multi-copy plasmid (Tanino et al. Appl. Microbial Biotechnol 75:1319-1325, 2007). This improved novel CALB-displaying yeast whole-cell biocatalyst could repeatedly catalyze the polyester, polybutylene adipate, synthesis reaction, using adipic acid and 1, 4-butandiol as the monomer molecules, four times in succession. This is the first report of the polymer synthesis using enzyme displaying yeast as the catalyst. The ratios of cyclic compounds in the polybutylene adipates synthesized with the CALB-displaying yeast whole-cells were lower than that in the polybutylene adipate synthesized with conventional metal catalysis. From these results, it appears that the use of CALB-displaying yeast cells could be useful for the polyester synthesis reaction, with reduced by-product production.

The SGNH-hydrolase of Streptomyces coelicolor has (aryl)esterase and a true lipase activity

The Streptomyces coelicolor A3(2) gene SCI11.14c was overexpressed and purified as a His-tagged protein from heterologous host, Streptomyces lividans. The purification procedure resulted in 34.1-fold increase in specific activity with an overall yield of 21.4%. Biochemical and physical properties of the purified enzyme were investigated and it was shown that it possesses (aryl)esterase and a true lipase activity. The enzyme was able to hydrolyze p-nitrophenyl-, α- and β-naphthyl esters and poly(oxyethylene) sorbitan monoesters (Tween 20–80). It showed pronounced activity towards p-nitrophenyl and α- and β-naphthyl esters of C 12–C 16. Higher activity was observed with α-naphthyl esters. The enzyme hydrolyzed triolein (specific activity: 91.9 U/mg) and a wide range of oils with a preference for those having higher content of linoleic or oleic acid (C18:2; C18:1, cis). The active-site serine specific inhibitor 3,4-dichloroisocoumarin (DCI) strongly inhibited the enzyme, while tetrahydrofurane and 1,4-dioxane significantly increased (2- and 4- fold, respectively) hydrolytic activity of lipase towards p-nitrophenyl caprylate. The enzyme exhibited relatively high temperature optimum (55 °C) and thermal stability. CD analysis revealed predominance of α-helical structure (54% α-helix, 21% β-sheet) and a T m value at 66 °C. Systematic bioinformatic analysis of deduced amino acid sequence of S. coelicolor enzyme placed it to the SGNH-hydrolase family. Phylogenetic analysis of the predicted protein homologous to the S. coelicolor SGNH-hydrolase generated three distinct groups consisting of proteins from Actinomycetales, Ascomycota and Nematoda. At present it seems that these enzymes are most conserved among soil inhabiting organisms.

Optimization of enzymatic treatment of polyester fabrics by lipase from Porcine Pancreas

The aim of this study was to provide the optimum condition for improving the hydrophilicity of PET fabrics by lipase treatment. The lipase hydrolytic activity, moisture regain, and wettability of PET fabrics were measured at different pH, temperature, reaction time, and concentration. The hydrolytic activity of lipase was evaluated by the number of carboxylic groups, using the titration method. Each treatment condition was controlled by measuring the hydrolytic activity, moisture regain, and wettability. The lipase treatment condition was controlled at pH 7.5, temperature 40 °C, treatment time 90 min, and concentration 6.25 g/l. Lipase treatment was an effective method to improve the moisture regain and wettability of PET fabrics because lipase hydrolysis formed hydrophilic groups on the surface of PET fabrics. The surface of the lipase-treated PET fabrics showed cracks and voids, largely responsible for the increase in the PET’s water-related properties. The nitrogen contents of the lipase-treated PET fabrics were measured at only 0.072 %. Thus, the improvement of the surface wettability of the lipase-treated PET surface was associated with the hydrolytic action of lipase rather than with protein absorption.

폴리에스터 직물의 리파제 처리시 Triton X-100 및 염화칼슘의 영향

본 연구는 폴리에스터 직물에 리파제 처리시 첨가제에 따른 수분특성 변화를 검토하였다. 활성제(염화칼슘) 및 비이온 계면활성제(Triton X-100) 첨가가 수분율, 접촉각, 흡수속도, 표면형태변화에 미치는 영향을 비교, 분석하였다. 연구결과, 리파제 처리된 폴리에스터 직물의 수분율은 비이온 계면활성제인 Triton X-100 첨가시 현저히 감소하는 것으로 나타났다. 그러나 리파제의 활성제로 알려진 염화칼슘 첨가 시 폴리에스터 직물의 수분특성은 다소 증가하는 것으로 나타났다. 특히 리파제 처리 시 염화칼슘이 10mM이상 첨가된 경우 폴리에스터 직물의 수분특성이 증가되었다. 리파제 처리된 폴리에스터 직물의 표면관찰 결과, 섬유표면에 생성된 보이드와 크랙이 폴리에스터 직물의 수분특성 증가에 영향을 미치는 것으로 확인되었다. 이상의 결과를 통해, 폴리에스터 직물에 리파제 처리시 Triton X-100은 리파제의 활성을 저해하고, 염화칼슘은 리파제의 활성을 다소 증가시키는 것을 확인하였다. In this study, we reported the effect of porcine pancreas lipase treatment in the presence of a calcium chloride and Triton X-100 on moisture regain and wettability of PET fabrics. The moisture regain of PET fabrics in the presence of 0.5% surfactant showed a 1.5-fold decrease, compared to the absence of it. Triton X-100 acted as an inhibitor to porcine pancreas lipase hydrolytic activity. The moisture regain and wettability of porcine pancreas lipase treated PET fabrics improved when more than 10mM of calcium chloride was added to the treatment solution. Porcine pancreas lipase treatment caused voids and cracks on PET fabrics.