Biocatalytic resolution of (±)-hydroxyalkanoic esters. A strategy for enhancing the enantiomeric specificity of lipase-catalyzed ester hydrolysis.

Scilimati, Antonio; Ngooi, T. K.; Sih, Charles J.

doi:10.1016/s0040-4039(00)80643-7

Cited by 53 publications

(8 citation statements)

References 10 publications

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“…Invariably, @)-configured esters were cleaved preferentially. This is in accordance with results of other groups (Scilimati, Ngooi and Sih, 1988;Laumen and Schneider, 1988;Ziffer et al, 1983) who employed microbial lipases of different origin and/or whole microbial cells for similar substrates, taking into account that ( R / S ) nomenclature rules may alter the priority without a change in bulkiness of substituents.…”

Section: Scheme 4 Enzymatic Hydrolysis Of Racemic 3-acyloxyalkanoatessupporting

confidence: 91%

“…With both of the enzymes some cleavage of the terminal methyl carboxylate was observed as an undesired side reaction. To overcome this obstacle, t-butyl ester 3e was used as substrate since these are usually not cleaved by hydrolases (Scilimati, Ngooi and Sih, 1988). Unfortunately, while GC-4 lipase was unable to hydrolyse 3e, lipase AY-30 showed a disappointing low enantioselectivity, with this substrate.…”

Section: Scheme 4 Enzymatic Hydrolysis Of Racemic 3-acyloxyalkanoatesmentioning

confidence: 99%

“…Since the potential therapeutic significance of lipid A has created increasing synthetic efforts in this area (Briner and Vasella, 1987 and references cited therein), we initiated a search for methods for the preparation of optically active long-chain 3hydroxyalkanoates. Although several methods for the lower homologs possessing a chain length of up to six carbon atoms are available (Hirama, Shimizu and Iwashita, 1983;Mohr, Rosslein and Tamm, 1987;Noyori et al, 1987;Seebach, Roggo and Zimmermann, 1987;Scilimati, Ngooi and Sih, 1988), me corresponding long-chain derivatives have been investigated only to a limited extent. Yeast mediated reduction of 3-oxooctadecanoic acid gave the enantiomerically pure (R)-3-hydroxy acid in moderate yield (Utaka, Higashi and Takeda, 1987) and, on Methyl 3-oxotetradecanoate l b Yield 82%; mp 28-30°C.…”

Section: Introductionmentioning

confidence: 99%

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Chemoenzymatic Preparation of Optically Active Long-Chain 3-Hydroxyalkanoates

1990

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The synthesis of optically active 3-hydroxyalkanoates of varying chain length (C,,, C,, and C18) was investigated using chemoenzymatic methods. While bakers' yeast mediated reduction of 3oxoalkanoates gave (R)-3-hydroxyalkanoates (e.e. >80%, yield -lo%), both enantiomers were obtained by enzymatic resolution of racemic methyl 3-butanoyloxyalkanoates using Geotrichum candidum lipase with moderate to good optical purity (e.e. 32-92%, yield 4040% for both enantiomers). Lipase-catalysed interesterification, however, was found to proceed with similar enantioselectivity but with slow rate of conversion. the other hand, asymmetric reduction of 3-oxoalkanoates using a chirally modified hydrogenation catalyst led to 3-hydroxy derivatives with better than 80% e.e. (Nakahata et al., 1982). Furthermore, optically pure 3-hydroxyalkanoates were obtained in a six step sequence starting from (R)or (S)-malic acid (Larchevsque and Henrot, 1987).In this study we compare the applicability of different chemoenzymatic methods-i.e. yeast reduction, enzymatic hydrolysis and enzymatic transesterification-for the synthesis of enantiomerically enriched long-chain 3-hydroxyalkanoates with a total chain length of Cl0, C14 and C18 (for a preliminary communication see Feichter, Faber and Griengl, 1989). In addition, a branched derivative was investigated since fatty acids of such type have been found to be constitutents of microbial lipopolysaccharides (Wollenweber et al., 1985). MATERIALS AND METHODS GeneralMelting points were determined on a Tottoli apparatus and are uncorrected. Preparative column chromatography was performed on silica gel 60 (230-400 mesh, Merck) and for TLC Merck silica gel 60 FZ4 plates were used. Compounds were visualized either with UV-light or by spraying with vanilline/conc. H2S04 and heat treatment, GLC-analyses were performed on a Hewlett-Packard 7620A chromatograph (2.2 m X l/8" glass column, 3% OV 225 on Supelcoport 100/120) equipped with an FID. Elemental analyses (C, H) of all novel compounds were within 0.5% of calculated values. Optical rotations ([a13 were measured on a Jasco DIP 370 polarimeter in CHC13 solution. 'H and 19FNMR spectra were recorded on a Bruker MSL 300 (300 and 282MHz, respectively) or a Hitachi-Perkin-Elmer R-24-B (60 MHz) spectrometer in CDC13 solution unless otherwise stated. Chemical shifts are reported from TMS or CFC13 as internal standard in ppm (6-scale) and coupling constants (J) in Hz (s = singlet, d = doublet, t = triplet, m = multiplet). All commercially obtained compounds were used as received except acid chlorides which were distilled prior to use. Crude enzyme preparations were employed without further purification. Lipases A, A-6, AY-30,

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Section: Scheme 4 Enzymatic Hydrolysis Of Racemic 3-acyloxyalkanoatessupporting

confidence: 91%

Section: Scheme 4 Enzymatic Hydrolysis Of Racemic 3-acyloxyalkanoatesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Chemoenzymatic Preparation of Optically Active Long-Chain 3-Hydroxyalkanoates

1990

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“…Hence, estolide formation is a reaction that is strongly driven in the forward direction. However, in aqueous medium, lipolysis of watersoluble estolides has been conducted successfully at high yields (47)(48)(49). In addition, poly-e-caprolactone (poly-C6o)- HFA lactone) was successfully hydrolyzed in aqueous medium when emulsified with surfactant (51,52).…”

Section: Activity Of Lipases Toward Hydroxy Acids and Their Derivativesmentioning

confidence: 99%

The catalytic activity of lipases toward hydroxy fatty acids—A review

Hayes

1996

J Americ Oil Chem Soc

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Hydroxy fatty acids, derived from several natural and synthetic sources, have many applications. Lipases have been employed to catalyze reactions involving hydroxy acids to narrowly shape the product distribution via their regio-and stereoselectivities. This manuscript reviews the action of lipase on hydroxy acids and their derivatives. The formation of estolides or lactones by lipase-catalyzed reactions depends strongly on the position of the hydroxyl moiety on the hydroxy acyl group and slightly on the hydroxy acid chainlength and concentration. Pseudomonas sp. and porcine pancreatic lipases are the most useful for catalyzing formation of optically pure lactones, while lipases lacking positional selectivity catalyze estolide formation best. The product distribution of lipase-catalyzed esterification between hydroxy-and nonhydroxy-acyl groups is strongly dependent on the lipase type. Lipase-catalyzed reactions between hydroxy acids and alcohols yield hydroxy esters, not estolides, as the major product. JAOCS 73, 543-549 (I 996).

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“…This rule suggests a strategy for improving the stereoselectivity of these enzymes: lipases poorly resolve secondary alcohols with two similarly-sized substituents, but they efficiently resolve secondary alcohols when the size of one substituent is increased. Consistent with this rule, researchers successfully increased the stereoselectivity of lipase-catalyzed reactions of secondary alcohols by increasing the difference in size of the two substituents [26,28,[36][37][38][39][40][41]. The advantage of this rule is that it is applicable to a wide range of substrates, the disadvantages are the several exceptions.…”

Section: Empirical Rule For Secondary Alcoholsmentioning

confidence: 94%