Immobilized Porcine Pancreatic Lipase Research Articles

Adsorption of PPL on a high thermal stable DUT-5 and their catalytic activity in a transesterification reaction of cinnamyl alcohol and vinyl acetate

Lipase-assisted catalytic esterification reactions have been concentrated on due to their green synthetic route for cinnamate acetate. In this paper, a high thermal stable Al-MOF (DUT-5) was chosen as a carrier to immobilize Porcine pancreatic lipase (PPL), and the resulting composites of PPL@DUT-5 were then employed in the catalytic transesterification reaction of cinnamyl alcohol and vinyl acetate. The adsorption conditions of PPL on the surface of DUT-5 were varied to optimize PPL loading uptakes, the adsorption kinetics were analyzed to explore the adsorption behavior of PPL on the DUT-5. In the catalytic transesterification reaction, the resulting PPL@DUT-5 represents the prominent enhanced catalytic stability under a varied reaction condition but with a higher catalytic activity, such as under the relative wide optimum pH value and at the increased operation temperature. And, the good reusability of the PPL@DUT-5 in cyclic catalytic processes highlights their prospect applications in the practical organic conversion reactions.

Surface Modification of Magnetic ZIF-90 Nanoparticles Improves the Microenvironment of Immobilized Lipase and Its Application in Esterification.

Interactions of enzymes with supports significantly affect the activity and stability of immobilized enzymes. Herein, amino-functionalized ionic liquid (IL)-grafted magnetic zeolitic imidazolate framework-90 (MZIF-90) was prepared and used to immobilize porcine pancreatic lipase (PPL). The nanocomposites were fully characterized; meanwhile, the interactions between ILs and ZIF-90 were calculated based on density functional theory. The prepared biocatalyst (PPL-ILs/MZIF-90) had a lipase loading of 178.3 mg/g and hydrolysis activity up to 287.5 U/g. When the biocatalyst was used to synthesize isoamyl acetate, the reaction media, molar ratio of alcohol/acid, temperature, and reaction time were optimized. Under the optimized reaction conditions (in hexane, alcohol/acid = 3:1, under 45 °C, reacted for 9 h), the ester yield reached 85.5%. The results of the stability test showed that PPL-ILs/MZIF-90 retained 88.7% of the initial activity after storing for 35 days and 92.5% of the initial activity after reusing for seven cycles for synthesizing isoamyl acetate. Moreover, the secondary structure analysis showed that the synthesized supports protected the active conformation of immobilized lipase, which lead to the enhanced catalytic performance. Additionally, the biocatalyst can be easily separated with a magnet, which facilitated the reusability. This study provides insights regarding the application of metal organic framework composites in the field of enzyme catalysis.

Immobilization for Lipase: Enhanced Activity and Stability by Flexible Combination and Solid Support

In this study, an enhanced activity and stability method for immobilizing porcine pancreatic lipase (PPL) was developed based on ZIF-8 encapsulated supramolecular-modified gold nanoparticle complexes (pSC4-AuNPs@ZIF-8). Supramolecular calix[4]arene (pSC4) can recognize the amino group of PPL through non-covalent force, and this flexible binding method protected the structure of PPL during the immobilization process. Due to the hydrophilic of pSC4-AuNPs and hydrophobic of ZIF-8, PPL can maintain a "lid open" conformation, which can enhance the stability of PPL structure and reduce PPL activity loss. ZIF-8 was used to immobilize PPL to avoid the difficult recovery of free PPL. Compared with the native form of PPL, it exhibited 70.6% maintained activity with terrific pH and temperature stability, and had good performance in thermal stability, time stability, and reusability. In addition, three immobilized PPL methods were designed to further clarify the influence of synthetic methods and additives on the activity and stability of PPL. Importantly, the loading rate of pSC4-AuNPs@ZIF-8@PPL was up to 51.2% among these immobilized PPL systems. Therefore, pSC4-AuNPs@ZIF-8 may serve as a versatile and promising immobilization system for enzymes.

Chitosan derivative functionalized carbon nanotubes as carriers for enzyme immobilization to improve synthetic efficiency of ethyl caproate

To acquire stable non-covalent functionalized carbon nanotubes with good dispersion and biocompatibility, cinnamaldehyde-chitosan conjugates (CA-CS conjugates) were synthesized to modify carbon nanotubes. The functionalized carbon nanotubes (CA–CS–CNTs) were characterized by FTIR, TGA and TEM. CA–CS–CNTs could be dispersed well in water, and the loading of CA-CS conjugates on carbon nanotubes was about 23%. CA–CS–CNTs were further extended to immobilize porcine pancreatic lipase (PPL), and the successful attachment of PPL onto CA–CS–CNTs was revealed by the result of FTIR. The lipase loading and relative lipase hydrolysis activity of immobilized PPL (CA–CS–CNTs-PPL) reached 248 mg/g and 8064 U/g, respectively. CA–CS–CNTs-PPL possessed good thermostability, and maintained 69% of enzyme activity after reusing 7 times. Additionally, characteristic flavor of strong aromatic liquors, ethyl caproate, was prepared using CA–CS–CNTs-PPL as biocatalysts, and the highest yield of 88% was observed. CA–CS–CNTs-PPL possessed positive properties, which could be expected to become low-cost and useful biocatalysts.

Magnetic Graphene Oxide as a Carrier for Lipases Immobilization: An Approach for Hydrolysis of Olive Oil Emulsion

The use of lipases in industrials processes has increased due to its ability to catalyze total or partial hydrolysis reactions of fatty acids. However, due to the difficulty of isolation and purification of lipases, as well as its separation from the reaction medium, it becomes an expensive input. In this study, graphene oxide was used as carrier for enzymes. The magnetic properties of the carrier were obtained through decoration with magnetic iron oxide nanoparticles on graphene oxide surface.XRD was used to elucidate the structure and morphology of the compounds obtained. By measuring hydrolytic activity, it was possible to determine the optimum pH and temperature for three different types of immobilized lipases, being 37 °C and pH 8 (porcine pancreatic lipase), 50 °C and pH 6 (Candida rugosa lipase), and 40 °C and pH 9 (Aspergillus niger lipase). The enzymatic recovery test, during five minutes each, showed the immobilized porcine pancreatic lipase can be recycled six times without significant loss of catalytic activity. It was confirmed the efficiency of the magnetic graphene oxide as a carrier for different lipases allowing its use for transesterification process in mild temperature and pH conditions.

A Comparison of the Resolution of Selective (+/-)-Glycidyl Butyrate by Using Free and Nano-SiO₂ Immobilized Porcine Pancreatic Lipase.

To explore the hydrolyzed properties of nano-SiO₂ immobilized porcine pancreatic lipase, the selective hydrolysis of immobilized lipase for glycidyl butyrate was compared with the free enzyme. The hydrolysis selectivity of the immobilized biocatalyst was evaluated and compared with the free enzyme using the enantiomeric excess (ee) of resolving racemic glycidyl butyrate as the indicator. The enantiomeric excess of the immobilized biocatalyst could be increased by 4.5%-10.0% which compared with the free enzyme under every single technological condition. The ee was improved from 84.7% for free enzyme to 91.6% for the immobilized enzyme with 61.2% conversion. Compared with free enzyme, the conversion rate of the immobilized enzyme was increased slightly, but the % enantiomeric excess of the immobilized enzyme was increased greatly.

Synthesis of functional ionic liquid modified magnetic chitosan nanoparticles for porcine pancreatic lipase immobilization

We developed magnetic chitosan nanoparticles (CS‑Fe3O4) with mean diameter of 15–20 nm. Subsequently, these inorganic-organic composite nanoparticles were modified using an imidazole-based functional ionic liquid (IL). The prepared support (IL‑CS‑Fe3O4), which was used to immobilize porcine pancreatic lipase (PPL), was characterized using Fourier transform infrared (FTIR) spectroscopy, vibrating sample magnetometry (VSM), thermogravimetry (TG), transmission electron microscopy (TEM) and X-ray diffraction (XRD). Circular dichroism (CD) was used to analyze the secondary structure of immobilized PPL. The immobilized PPL (PPL‑IL‑CS‑Fe3O4) exhibited 1.93-fold higher specific activity than PPL‑CS-Fe3O4 when triacetin was used as the substrate, and showed 95 mg/g of lipase immobilization capacity and 382% of activity recovery. The residual activity of PPL‑IL‑CS‑Fe3O4 was above 60% of the initial activity after incubation at 50 °C for 6 h, as was higher than that of PPL‑CS‑Fe3O4 which showed 40% of the initial activity. In addition, PPL‑IL‑CS‑Fe3O4 retained 84.6% of the initial activity after 10 cycles, whereas PPL‑CS‑Fe3O4 retained only 75.5% activity. Furthermore, the kinetic parameters, apparent Km and Vmax of PPL‑IL‑CS‑Fe3O4 were 2.51 mg/mL and 1.395 U/mg respectively, these results indicated that the immobilized PPL had better affinity towards the substrate, especially when the nanoparticles were modified by functional IL. Besides, the magnetic chitosan nanoparticles loaded with PPL were easily recovered. A novel, efficient, and practical method for enzyme immobilization was developed.

Quick separation and enzymatic performance improvement of lipase by ionic liquid-modified Fe3O4 carrier immobilization.

To promote the activity and stability of immobilized porcine pancreatic lipase (PPL), novel carrier was combined with special immobilization method. Enzymatic activity was enhanced after immobilized onto ionic liquid modified magnetic Fe3O4 by electrostatic adsorption. Activity of immobilized enzyme (PPL-IM/BF4-Fe3O4@CA) reached 596U/g PPL. Through the combination of electrostatic adsorption and embedding immobilization methods, we improve binding force between the carrier and enzyme, and further enhance the efficiency and stability of immobilized enzyme. The activity of PPL-IM/BF4-Fe3O4@CA after repeated third use was 78%. After storage at room temperature for 5days, the residual activity was 89%. Enzymatic properties and catalytic kinetics of immobilized enzymes were studied, and the effect mechanism of ionic liquid modified Fe3O4 on PPL was revealed. The effect of ionic liquid on the carrier structure was investigated by characterization of XRD, FT-IR, SEM and TG. The mechanism and enzymatic properties of immobilized PPL via electrostatic adsorption and embedding were analyzed. A novel and efficient immobilized PPL was developed.

Biodegradation of mycotoxin patulin in apple juice by calcium carbonate immobilized porcine pancreatic lipase

The degradation of mycotoxin patulin in apple juice by calcium carbonate immobilized porcine pancreatic lipase (PPL) was investigated. Batch experiments was used to study the optimal degradation conditions, including immobilized PPL addition, temperature, degradation time and initial concentration of immobilized PPL for apple juice. The concentration of patulin in apple juice was determined by HPLC. The results showed that the optimal degradation conditions were 40 °C for 18 h, adding 0.03 g/mL immobilized PPL. After the degradation of patulin, the amount of amino acids, aroma components, polyphenols had changed insignificantly in apple juice, and the patulin degradation rate was over 70% at the initial concentration of 1 mg/L. Consequently, the addition of immobilized PPL would not have a significant effect on the nutritional content. It suggested that immobilized PPL could be used for patulin degradation in apple juice.

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.

Effective detoxification of patulin from aqueous solutions by immobilized porcine pancreatic lipase

Porcine pancreatic lipase (PPL) was immobilized by physical adsorption onto CaCO3. The detoxification of the immobilized PPL for patulin from aqueous solutions was investigated. Batch experiments were carried out to obtain its optimal conditions for the immobilization process and to evaluate the influence of the immobilized PPL amount, pH, temperature, initial patulin concentration and time on the detoxification. Enzyme properties were assayed by the immobilization yield and enzyme activity, and partial structures of the immobilized PPL were characterized by Fourier Transform Infrared spectroscopy (FTIR). The immobilization yield was more than 99% during 3 h at pH 5.0, 30 °C when 0.6 mg/mL of PPL was adsorbed onto 0.5 g of CaCO3. The immobilized PPL was effective in detoxification of patulin from aqueous solutions at pH 6.0, 40 °C during 42 h. Furthermore, the immobilized PPL after detoxification still kept high yield and enzyme activity, and was reusable for usage of detoxification. Detoxification properties of the immobilized PPL could represent a novel strategy for a possible application in decontaminating patulin aqueous solutions.

Enhancing stabilities of lipase by enzyme aggregate coating immobilized onto ionic liquid modified mesoporous materials

Abstract Mesoporous material SBA-15 as the matrix and hydrophilic methyl imidazolium ionic liquids [MSiIM] + BF 4 − as modifier were involved in preparing ionic liquid modified materials as enzyme carriers through after-grafting silane coupling reaction. The method of enzyme aggregates coating was firstly used to immobilize porcine pancreatic lipase (PPL) onto ionic liquid modified SBA-15. Characterization before and after modification and immobilization were conducted using infrared spectroscopy (FT-IR), differential thermal-thermal analysis (DTA-TG) and N 2 adsorption–desorption method (BET). The results indicated that the ordering degree of SBA-15 declined after ionic liquid modification, but mesoporous structure remained. After enzyme immobilization, pore size and specific surface area of carrier became smaller. The cross-linking agent amount, reaction temperature and pH were optimized in this paper. The result demonstrated that the initial activity of enzyme was raised from 35% to 53% after five times recycle by enzyme aggregate coating. 74% of the original activity remained after 25 days storage.

Effect of polyvinylpyrrolidone on mesoporous silica morphology and esterification of lauric acid with 1-butanol catalyzed by immobilized enzyme

Mesoporous silica materials with a range of morphology evolution, i.e., from curved rod-shaped mesoporous silica to straight rod-shaped mesoporous silica, were successfully prepared using polyvinylpyrrolidone (PVP) and triblock copolymer as dual template. The effects of PVP molecular weight and concentration on mesoporous silica structure parameters were studied. Results showed that surface area and pore volume continuously decreased with increased PVP molecular weight. Mesoporous silica prepared with PVP K30 also possessed larger pore diameter, interplanar spacing (d100), and cell parameter (a0) than that prepared with PVP K15 and PVP K90. In addition, with increased PVP concentration, d100 and a0 continuously decreased. The mechanism of morphology evolution caused by the change in PVP concentration was investigated. The conversion rate of lauric acid with 1-butanol catalyzed by immobilized Porcine pancreatic lipase (PPL) was also evaluated. Results showed that PPL immobilized on amino-functionalized straight rod-shaped mesoporous silica maintained 50% of its esterification conversion rate even after five cycles of use with a maximum conversion rate was about 90.15%.

Covalent immobilization of porcine pancreatic lipase on carboxyl-activated magnetic nanoparticles: Characterization and application for enzymatic inhibition assays

Using carboxyl functionalized silica-coated magnetic nanoparticles (MNPs) as carrier, a novel immobilized porcine pancreatic lipase (PPL) was prepared through the 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride/N-hydroxysuccinimide (EDC/NHS) coupling reaction. Transmission electron microscopic images showed that the synthesized nanoparticles (Fe3O4–SiO2) possessed three dimensional core–shell structures with an average diameter of ~20nm. The effective enzyme immobilization onto the nanocomposite was confirmed by atomic force microscopic (AFM) analysis. Results from Fourier-transform infrared spectroscopy (FT-IR), Bradford protein assay, and thermo-gravimetric analysis (TGA) indicated that PPL was covalently attached to the surface of magnetic nanoparticles with a PPL immobilization yield of 50mg enzyme/g MNPs. Vibrating sample magnetometer (VSM) analysis revealed that the MNPs-PPL nanocomposite had a high saturation magnetization of 42.25emu·g−1. The properties of the immobilized PPL were investigated in comparison with the free enzyme counterpart. Enzymatic activity, reusability, thermo-stability, and storage stability of the immobilized PPL were found significantly superior to those of the free one. The Km and the Vmax values (0.02mM, 6.40U·mg−1 enzyme) indicated the enhanced activity of the immobilized PPL compared to those of the free enzyme (0.29mM, 3.16U·mg−1 enzyme). Furthermore, at an elevated temperature of 70°C, immobilized PPL retained 60% of its initial activity. The PPL-MNPs nanocomposite was applied in the enzyme inhibition assays using orlistat, and two natural products isolated from oolong tea (i.e., EGCG and EGC) as the test compounds.

Immobilization of porcine pancreatic lipase on poly-hydroxybutyrate particles for the production of ethyl esters from macaw palm oils and pineapple flavor

Poly-hydroxybutyrate particles (PHB) were used as support to immobilize porcine pancreatic lipase (PPL). The biocatalysts prepared were tested in the synthesis of pineapple flavor by esterification of butanol and butyric acid in heptane medium, and in the synthesis of ethyl esters by transesterification of macaw palm pulp (MPPO) and macaw palm kernel (MPKO) oils with ethanol in solvent-free systems. The effect of protein loading on the biocatalyst activity was assessed in olive oil hydrolysis. Maximum hydrolytic activity of 292.8±8.60IU/g was observed. Langmuir isotherm model was applicable to the adsorption of PPL on PHB particles. Maximum immobilized protein amount was 24.3±1.70mg/g. The optimal pH and temperature in hydrolysis reaction for the immobilized PPL were at pH 8.5 and 50°C, while for the crude PPL extract were at pH 8.0 and 45°C. Immobilized PPL exhibited full hydrolytic activity after 2h of incubation in non-polar solvents. In esterification reaction, optimal conversion was around 93% after 2h of reaction. After six esterification cycles, the biocatalyst retained 63% of its initial activity. The biocatalyst prepared attained transesterification yield of 50% after 48h of reaction for MPKO and 35% after 96h of reaction for MPPO.

Enhancing the catalytic properties of porcine pancreatic lipase by immobilization on SBA-15 modified by functionalized ionic liquid

The mesoporous silica SBA-15 was modified by carboxyl-functionalized ionic liquid (COOH-IL-SBA). The prepared support was used to immobilize porcine pancreatic lipase (PPL) by physical adsorption (PPL-COOH-IL-SBA) and covalent attachment (PPL-CON-IL-SBA). Enzymatic properties of the immobilized PPL were investigated in the triacetin hydrolysis reaction. It was found that carboxyl functionalized ionic liquid modification of the support surface was an effective method to improve the properties of immobilized PPL. Incorporating into the functionalized SBA-15 made PPL more resistant to temperature and pH changes, compared with PPL immobilized on parent SBA-15 (PPL-SBA). Especially, after the covalent attachment to a functionalized support, the stability of PPL was improved obviously, which retained 81.25% and 52.50% of the original activity after incubation for 20days and four times recycling, respectively, whereas PPL-SBA exhibited only 58.80% and 27.78% of the original activity under the same conditions. In addition, physical and chemical properties of the supports and immobilized PPL were characterized by small-angle X-ray powder diffraction (SAXRD), Fourier transform infrared spectroscopy (FT-IR), scanning electron microscope (SEM), nitrogen adsorption, nuclear magnetic resonance (NMR) and thermogravimetry (TG). The images and data confirmed chemical modification in SBA-15 and PPL immobilization on the tested support.

Biocatalytic esterification of caprylic acid with caprylic alcohol by immobilized lipase on amino-functionalized mesoporous silica

Ordered mesoporous silica (MS) materials were prepared using Pluronic P123 (triblock copolymer poly(ethylene glycol)–block–poly(propylene glycol)–block–poly(ethylene glycol)) and poly(ethylene glycol) as dual templates, and functionalized with (3-aminopropyl)triethoxysilane using the postsynthesis-grafting method. Fourier-transform infrared spectroscopy, 29Si and 13C cross-polarization and magic angle spinning nuclear magnetic resonance, elemental analysis, small-angle X-ray powder diffraction, scanning electron microscopy, transmission electron microscopy, and N2 adsorption–desorption were used to monitor the effect of surface functionalization on the structural and textural features of MS. MS was found to possess a short rod-shaped macrostructure and a two-dimensional hexagonal P6mm mesoscopic structure. After functionalization, the mesoscopic structure was retained and the interplanar spacing d (100) increased, whereas the pore diameters, pore volumes, and surface areas decreased. MS and functionalized MS were used as carriers to immobilize porcine pancreatic lipase (PPL). The immobilized PPL on both kinds of carriers were then employed to catalyze the hydrolysis of triacetin and esterification of caprylic acid with caprylic alcohol. All observed biocatalytic characteristics of PPL immobilized on functionalized MS were compared with those of PPL immobilized on MS. The hydrolysis activity of lipase immobilized on functionalized MS was almost twice that on MS. Functionalized MS immobilized PPL showed greater reusability, and its hydrolysis conversion was still retained at 24%, which was 15% higher than that of lipase immobilized on MS after the fifth reuse. The synthetic activity and effect of several parameters on caprylic caprylate production for immobilized PPL were investigated. Immobilized PPL exhibited significantly higher activity, with a caprylic acid conversion ratio of 67.47% when the reaction was catalyzed by PPL immobilized on functionalized MS. The corresponding value was 58.75% using PPL immobilized on MS at 50°C.

Conversion of Sunflower Oil to Biodiesel by Alcoholysis using Immobilized Lipase

Transesterification reaction was performed using sunflower oil and short-chain alcohol by immobilized lipases in organic solvents. The fatty acid ester, which is the product of this reaction, can be used as a diesel fuel that does not produce sulfur oxide and minimize the soot particulate. Immobilized porcine pancreatic lipase (PPL) and Candida rugosa lipase (CRL) showed the satisfactory activity in these reactions. Immobilization of lipases was carried out using inorganic absorbance Celit 545 particle as a carrier. Organic solvent like hexane in reactions was required when methanol and ethanol were used as alcoholic substrate. The reaction could be performed in absence of solvent when 1-propanol and 1-butanol were used as short-chain alcohol. The activities of immobilized lipases were highly increased in comparison with free lipases because its activity sites became more effective. Immobilized enzyme could be repeatedly used without difficult method of separation and the decrease in its activity was not largely observed.

Temperature-dependence of enantioselectivity and desymmetrization in the acetylation of 2-mono- and 2,2-di-substituted 1,3-propanediols by a novel lipase isolated from the yeast Cryptococcus spp. S-2

The effect of temperature on enantioselectivity and desymmetrization in the acetylation of 2-phenyl-1,3-propanediol (1a), 2-benzyl-1,3-propanediol (1b), 2-methyl-2-phenyl-1,3-propanediol (1c) and 2-benzyl-2-methyl-1,3-propanediol (1d) by a novel lipase (CSL) isolated from the yeast Cryptococcus spp. S-2 was studied. Desymmetrization of 1a, 1c and 1d by CSL-catalyzed acetylation was observed in the temperature range of −20°C to 40°C, while diacetylation of 1b occurred considerably even at 0°C. The kinetic parameters of the selectivity indicated that the acetylation of 1a is an entropy controlled process whereas the reaction of 1c and 1d is mainly controlled by the enthalpy term. In the monoacetylation of the diol 1d, the preferred configuration in the enantiomeric induction by CSL was opposite to that of immobilized porcine pancreatic lipase (PPL).

Comparison of the chiral recognition of prochiral substrates in the acetylation reaction by a novel lipase (CSL) from the yeast, Cryptococcus spp. S-2 with immobilized PPL : Enzyme-catalyzed desymmetrization and asymmetrization of prochiral 2-substituted 1,3-propanediols by CSL and immobilized PPL

In order to elucidate the nature of a novel lipase (CSL), isolated from the yeast Cryptococcus spp. S-2, in chiral recognition by comparison with that of immobilized PPL, the desymmetrization and asymmetrization of prochiral 2-phenyl-1,3-propanediol ( 1a), 2-benzyl-1,3-propanediol ( 1b), 2-methyl-2-phenyl-1,3-propanediol ( 1c), 2-benzyl-2-methyl-1,3-propanediol ( 1d), 2-ethyl-2-phenyl-1,3-propanediol ( 1e), and 2-benzyl-2-ethyl-1,3-propanediol ( 1f) by acetylation was investigated. Acetylation of 1a with excess vinyl acetate by the CSL-enzyme catalyst gave the corresponding monoacetate 2a with high enantioselectivity (80% ee) in 46% yield. Very high levels of desymmetrization were observed in the tertiary systems of 1c– f, giving the corresponding monoacetates 2c– f, respectively, in >97%. In the desymmetrization of diols 1a, 1c, 1d, and 1f, the sense of chiral differentiation of CSL was opposite to that of immobilized porcine pancreatic lipase (PPL).