Lipase‐catalyzed Kinetic Resolution of 3‐Hydroxy Esters: Optimization, Batch, and Continuous Reactions<sup>a</sup>

Bornscheuer, Uwe T.; Herar, A.; Capewell, A.; Wendel, V.; Kreye, Lars; Scheper, Thomas; Voss, E.; Wünsche, Kerstin; Meyer, H.

doi:10.1111/j.1749-6632.1995.tb19954.x

Cited by 5 publications

(4 citation statements)

References 5 publications

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“…The lipases that successfully catalyzed reactions with ct-and fl-HFA did so with quite high enantioselectivities, but in the case of a-HAE, enantiomeric excesses, or ee's (defined in Ref. 53) were sensitive to the alcohol moiety esterified to the hydroxy acyl group's carbonyl (40)(41)(42). Both Pseudomonas sp.…”

Section: Activity Of Lipases Toward Hydroxy Acids and Their Derivativesmentioning

confidence: 99%

“…In addition, if these reactions were allowed to proceed to equilibrium, nearly equimolar amounts of free HFA and estolide were produced. In other experimental work, ct-and fl-hydroxy acid esters were successfully esterified with short-chain free fatty acids when the latter were present as activated esters (e.g., vinyl acetate) (40)(41)(42). Hayes and Kleiman (34) performed a series of reactions between lesquerolic and octadecanoic acids.…”

Section: Activity Of Lipases Toward Hydroxy Acids and Their Derivativesmentioning

confidence: 99%

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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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Section: Activity Of Lipases Toward Hydroxy Acids and Their Derivativesmentioning

confidence: 99%

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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“…Even supercritical fluids have been used as solvent, thus facilitating downstream processing (Marty et al 1992; Beckman et al 1995; Ikushima 1997). Intense research has been performed on the impact of various parameters on the stereoselectivity of lipases, such as immobilization, coating of lipases with surfactants, use of acid anhydrides as substrates, or controlling stereoselectivity via the surface pressure of substrate monolayers (Rogalska et al 1990, 1991, 1993a, 1993b; Ransac et al 1991; Bianchi et al 1993; Bornscheuer et al 1993, 1995; Cygler et al 1995; Kamiya et al 1995; Stadler et al 1995; Yang et al 1996; Koteshwar and Fadnavis 1997).…”

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confidence: 99%

Directed Evolution of N‐Carbamyl‐d‐amino Acid Amidohydrolase for Simultaneous Improvement of Oxidative and Thermal Stability

Nam

Kim

2002

Biotechnology Progress

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Directed evolution of N-carbamyl-D-amino acid amidohydrolase from Agrobacterium tumefaciens NRRL B11291 was attempted in order to simultaneously improve oxidative and thermal stability. A mutant library was generated by DNA shuffling, and positive clones with improved oxidative and thermal stability were screened on the basis of the activity staining method on a solid agar plate containing pH indicator (phenol red) and substrate (N-carbamyl-D-p-hydroxyphenylglycine). Two rounds of directed evolution resulted in the best mutant 2S3 with a significantly improved stability. Oxidative stability of the evolved enzyme 2S3 was about 18-fold higher than that of the wild type, and it also showed an 8-fold increased thermostability. The K(m) value of 2S3 was comparable to that of wild-type enzyme, but k(cat) was slightly decreased. DNA sequence analysis revealed that six amino acid residues (Q23L, V40A, H58Y, G75S, M184L, and T262A) were substituted in 2S3. From the mutational analysis, four mutations (Q23L, H58Y, M184L, and T262A) were found to lead to an improvement of both oxidative and thermal stability. Of them, T262A had the most significant effect, and V40A and G75S only increased the oxidative stability.

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“…on the impact of various parameters on the stereoselectivity of lipases, such as immobilization, coating of lipases with surfactants, use of acid anhydrides as substrates, or controlling stereoselectivity via the surface pressure of substrate monolayers (Rogalska et al 1990(Rogalska et al , 1991(Rogalska et al , 1993a(Rogalska et al , 1993bRansac et al 1991;Bianchi et al 1993;Bornscheuer et al 1993Bornscheuer et al , 1995Cygler et al 1995;Kamiya et al 1995;Stadler et al 1995;Yang et al 1996;Koteshwar and Fadnavis 1997).…”

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confidence: 99%

A model of the pressure dependence of the enantioselectivity of Candida rugosalipase towards (±)‐menthol

2001

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Transesterification of (±)-menthol using propionic acid anhydride and Candida rugosa lipase was performed in chloroform and water at different pressures (1, 10, 50, and 100 bar) to study the pressure dependence of enantioselectivity E. As a result, E significantly decreased with increasing pressure from E ‫ס‬ 55 (1 bar) to E ‫ס‬ 47 (10 bar), E ‫ס‬ 37 (50 bar), and E ‫ס‬ 9 (100 bar). To rationalize the experimental findings, molecular dynamics simulations of Candida rugosa lipase were carried out. Analyzing the lipase geometry at 1, 10, 50, and 100 bar revealed a cavity in the Candida rugosa lipase. The cavity leads from a position on the surface distinct from the substrate binding site to the core towards the active site, and is limited by F415 and the catalytic H449. In the crystal structure of the Candida rugosa lipase, this cavity is filled with six water molecules. The number of water molecules in this cavity gradually increased with increasing pressure: six molecules in the simulation at 1 bar, 10 molecules at 10 bar, 12 molecules at 50 bar, and 13 molecules at 100 bar. Likewise, the volume of the cavity progressively increased from about 1864 Å 3 in the simulation at 1 bar to 2529 Å 3 at 10 bar, 2526 Å 3 at 50 bar, and 2617 Å 3 at 100 bar. At 100 bar, one water molecule slipped between F415 and H449, displacing the catalytic histidine side chain and thus opening the cavity to form a continuous water channel. The rotation of the side chain leads to a decreased distance between the H449-N and the (+)-menthyl-oxygen (nonpreferred enantiomer) in the acyl enzyme intermediate, a factor determining the enantioselectivity of the lipase. Although the geometry of the preferred enantiomer is similar in all simulations, the geometry of the nonpreferred enantiomer gets gradually more reactive. This observation correlates with the gradually decreasing enantioselectivity E.

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Lipase‐catalyzed Kinetic Resolution of 3‐Hydroxy Esters: Optimization, Batch, and Continuous Reactions^a

Cited by 5 publications

References 5 publications

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

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

Directed Evolution of N‐Carbamyl‐d‐amino Acid Amidohydrolase for Simultaneous Improvement of Oxidative and Thermal Stability

A model of the pressure dependence of the enantioselectivity of Candida rugosalipase towards (±)‐menthol

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Lipase‐catalyzed Kinetic Resolution of 3‐Hydroxy Esters: Optimization, Batch, and Continuous Reactionsa

Cited by 5 publications

References 5 publications

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

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

Directed Evolution of N‐Carbamyl‐d‐amino Acid Amidohydrolase for Simultaneous Improvement of Oxidative and Thermal Stability

A model of the pressure dependence of the enantioselectivity of Candida rugosalipase towards (±)‐menthol

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Product

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About

Lipase‐catalyzed Kinetic Resolution of 3‐Hydroxy Esters: Optimization, Batch, and Continuous Reactions^a