Lipase Immobilized porcine pancreas

S) -isopropylmorpholine-2,5 -dione immobilized porcine pancreas lipase iterative tandem catalysis indium tin oxide kinetic resolution polymerization large... 

In addition to homopolymers a number of copolymers of cyclic carbonates were synthesized by enzymatic ROP. Among them are amphiphilic block copolymers of PBTMC and PEG which were synthesized through enzymatic polymerization using immobilized porcine pancreas lipase (IPPL). The copolymerization of co-pentadecalactone (PDL) and TMC was also studied by using lipase catalysts. Of the six lipases evaluated for PDL/TMC copolymerizations in toluene at 70 ° C, an immobilized form of lipase-B from C. antarctica (Novozym-435) was preferred. Changing the PDL/TMC comonomers feed ratio from 1 10 to 10 1 (moLmol) provided copolymers that ranged... 

Porcine Pancreas Lipase (PPL), a common lipase with low cost, could be immobilized on silica particles with good stability and recyclablity. Then the immoblized lipase (IPPL) was employed as the catalyst for polymer synthesis, such as polyesters, polycarbonates, polyphosphates, and their copolymers. Here we present a mini-review of some works in our lab within this area. 

In our study (6), porcine pancreas lipase (PPL) immobilized on silica particles (narrow distributed micron particles) was employed for ring-opening polymerization of TMC. No evidence of decarboxylation occurring during the polymerization. The results showed that silica microparticles improved immobilization efficiency much more. The most preferable polymerization temperature of TMC was 100 °C during 24h polymerization. The M of the resulting polymers was significantly increased compared with that catalyzed by... 

Bagi, K., L. M. Simon, and B. Szajani. 1997. Immobilization and Characterization of Porcine Pancreas Lipase. Enzyme and Microbial Technology 20 (7) 531—535. 

Various lipases can be used, the most employed being Candida antartica lipase A (CAL-A). Nevertheless, the best results have been obtained with CAL-B immobilized on a Celite R-633 support, yielding 97% of conversion in the synthesis of mandelonitrile acetate 12 with an ee of 98%. Many applications can be envisaged considering that numerous hydrophobic compounds, from aliphatic chains to various aromatics, can be used as substrates, and both (R)- and (5)-enantiomers can be obtained by an appropriate choice of the enzyme (examples of (R)-enantiomers with CAL-A,Burkholderia cepiaca lipase [BCL], Candida rugosa lipase [CRL], " S) with CAL-B, BCL, and porcine pancreas lipase [PPL] " ). 

Martins et al. [78,80] described the enzymatic resolution of racemic glycidol in SCCO2. The chosen reaction route was the esterification with butyric acid catalyzed by either free or immobilized PPL (porcine pancreas lipase). The solubility of glycidol was measured in CO2 at 35 C and pressures in the range of 70-180 bar for butyric acid concentrations up to 500 mM. The partitioning of water between CO2 and the enzyme... 

We collaborated with Professor Palligamai Vasudevan of the Chemical Engineering Department of the University of New Hampshire on a study of immobilization of lipases on CoFoam. Immobilization was performed at the Hydrophilix facility in Portland, ME. Approximately 2 g lipase (from porcine pancreas and Mucor miehei) were stirred into 500 ml deionized water. The enzyme solution was emulsified with an equal volume of a methylene diisocyanate (MDI)-based hydrophilic polyurethane... 

Hydrolysis has traditionally been used for the production of fatty acids and glycerols, which find widespread apphcation in soaps and detergents, cosmetics, pharmaceuticals, and food products (174). Hydrolysis of soybean (181), canola (147, 208, 209), sunflower (149, 181, 210), tuna (150), and blackcurrant oils (145), tri-palmitin (146), triolein (211), and ethyl stearate (202) in SCCO2 has been reported. These investigations employed a variety of lipases, including immobilized lipase from porcine pancreas (211), Novozyme 435 (146, 181), Lipozyme (147, 150, 208, 209), non-immobilized Candida rugosa (150, 181), Lipase OL (150), and Lipolase lOOT (149, 181, 210). The effects of water content, enzyme load, operating conditions (temperature and pressure), pH, enzyme/substrate ratio, oil/buffer ratio, and CO2 flow rate (for continuous reactions) on the hydrolysis reaction were reported. 

Martins et al. [52] investigated the enantioselective esterification of glycidol with butyric acid at 35°C and 140 bar. They received a enantiomeric excess of (5)-glycidyl butyrate with lipase from porcine pancreas of 72-82%. The conversions were between 11% and 23%. With immobilized lipase they optimize the enantiomeric excess to 88-90% e.e. and a conversion of 20%. The e.e. of the substrate was 20%. In his dissertation, Bomscheuer [83] described the lipase-catalyzed transesterification of 3-hydroxymethyloc-tanoate with cyclohexyl acetate in organic solvents and supercritical GO2 (40°C/100 bar). After 400 h reaction time the author yielded 20% substrate and 96% product e.e. The... 

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