Porcine lipase

HR peroxidase horseradish peroxidase PP lipase porcine pancreatic lipase. 

Lipase (porcine) Enantioselective hydrolysis Enzyme covalently immobilized in PVA-cryogel [27]... 

Lipase Pseudomonas fluorescence Lipase porcine pancreas, Candida rugosa (dried powder)... 

PPL = porcine pancreatic lipase PLE = porcine liver esterase. 

Resolution of Racemic Amines and Amino Acids. Acylases (EC3.5.1.14) are the most commonly used enzymes for the resolution of amino acids. Porcine kidney acylase (PKA) and the fungaly3.spet i//us acylase (AA) are commercially available, inexpensive, and stable. They have broad substrate specificity and hydrolyze a wide spectmm of natural and unnatural A/-acyl amino acids, with exceptionally high enantioselectivity in almost all cases. Moreover, theU enantioselectivity is exceptionally good with most substrates. A general paper on this subject has been pubUshed (106) in which the resolution of over 50 A/-acyl amino acids and analogues is described. Also reported are the stabiUties of the enzymes and the effect of different acyl groups on the rate and selectivity of enzymatic hydrolysis. Some of the substrates that are easily resolved on 10—100 g scale are presented in Figure 4 (106). Lipases are also used for the resolution of A/-acylated amino acids but the rates and optical purities are usually low (107). 

ACOCH2CF3, porcine pancreatic lipase, THF, 60 h, 77% yield. This enzymatic method was used to acetylate selectively the primary hydroxyl group of a variety of carbohydrates. 

ACOCH2CCI3, pyridine, porcine pancreatic lipase, 85% yield.These studies examined the selective acylation of carbohydrates. Mannose is acy-lated at the 6-position in 85% yield in one example. 

Candida cylindracea, phosphate buffer pH 7, Bu20. The 6-0-acetyl of Q -methyl peracetylglucose was selectively removed. Porcine pancreatic lipase will also hydrolyze acetyl groups from carbohydrates. These lipases are not specific for acetate since they hydrolyze other esters as well. In general selectivity is dependent on the ester and the substrate. ... 

Porcine pancreatic lipase, pH 7.5, 23° 4.5 h, 55% yield. These conditions were used to suppress facile racemization of 2-chlorocyclohexenone. ... 

The first asymmetric synthesis of (—)-Y-jasmolactone, a fruit fiavor constituent, vas achieved via the enantioselective lactonization (desymmetrization) of a prochiral hydroxy diester promoted by porcine pancreas lipase (PPL) (Figure 6.23) [71]. 

This lactamization process can be promoted by enzymes such as pancreatic porcine lipase. Reduction of co-azido carboxylic acids leads to macrocyclic lactams. Although treatment of carboxylic acids with amines does not directly give amides, the reaction can be made to proceed in good yield at room temperature or... 

Another approach to the synthesis of chiral non-racemic hydroxyalkyl sulfones used enzyme-catalysed kinetic resolution of racemic substrates. In the first attempt. Porcine pancreas lipase was applied to acylate racemic (3, y and 8-hydroxyalkyl sulfones using trichloroethyl butyrate. Although both enantiomers of the products could be obtained, their enantiomeric excesses were only low to moderate. Recently, we have found that a stereoselective acetylation of racemic p-hydroxyalkyl sulfones can be successfully carried out using several lipases, among which CAL-B and lipase PS (AMANO) proved most efficient. Moreover, application of a dynamic kinetic resolution procedure, in which lipase-promoted kinetic resolution was combined with a concomitant ruthenium-catalysed racem-ization of the substrates, gave the corresponding p-acetoxyalkyl sulfones 8 in yields... 

Immobilized PLE was applied to promote stereoselective acetylation of prochiral bis(hydroxymethyl)methyl-phenylgermane 106 (R = Me) with vinyl acetate as a solvent and acyl donor. Later on, the same group reported that each enantiomer of hydridogermane monoacetates 107 (R = H) was obtained either via acetylation of the bis-hydroxy derivative 106 (R = H) or hydrolysis of the corresponding diacetate 108 (R = H). In both methods, porcine pancreatic lipase was used and, obviously, each reaction led to a different enantiomer of 107 (Equation 51). ... 

Various cyclic esters have been subjected to hpase-catalyzed ring-opening polymerization. Lipase catalyzed the ring-opening polymerization of 4- to 17-membered non-substituted lactones.In 1993, it was first demonstrated that medium-size lactones, 8-valerolactone (8-VL, six-membered) and e-caprolactone (e-CL, seven-membered), were polymerized by lipases derived from Candida cylindracea, Burkholderia cepacia (lipase BC), Pseudomonas fluorescens (lipase PF), and porcine pancreas (PPL). °... 

In 1958 Sarda and Desnuelle [79] discovered the lipase activation at the interfaces. They observed that porcine pancreatic lipase in aqueous solution was activated some 10-fold at hydrophobic interfaces which were created by poorly water-soluble substrates. An artificial interface created in the presence of organic solvent can also increase the activity of the lipase. This interfacial activation was hypothesized to be due to a dehydration of the ester substrate at the interface [80], or enzyme conformational change resulting from the adsorption of the lipase onto a hydrophobic interface [42,81,82]. 

Lipase from porcine pancreas Esterification of 1-butanol and oleic acid Oil-deionized water (96.6/3.4) 49.7 103... 

Packed-bed reactor Hydrolysis of olive oil Lipase from porcine pancreas 123... 

Porcine pancreatic lipase (PPL) catalyzed the polymerization of methyl 6-hy-droxyhexanoate [22]. The polymer with DP up to 100 was synthesized by the polymerization in hexane at 69 °C for more than 50 days. The PPL-catalyzed... 

A variety of enzymes (such as acetylcholine esterase, Porcine pancreatic lipase, Pseudomonas cepacia lipase, and Candida antarcita lipase) have been found useful in the preparation of enantiomerically pure cyclopentenol (+)-2 from 1. The enantiomeric (—)-2 has been prepared from diol 4 by enzymatic acetylation catalyzed by VP-345 with isopropenyl acetate in an organic medium. The key intermediate cyclopentanones (+)-6, (—)-6, 7, and 8, which are useful in the preparation of many bioactive molecules, can be obtained from 3 and 5 via routine chemical transformations.7... 

Scheme 4 Reagents and conditions i) Porcine pancreatic lipase, H20 ii) Ps. fluorescens lipase, H20.

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