Highly efficient one pot dynamic kinetic resolution of benzoins with entrapped Pseudomonas stutzeri lipase

Hoyos, Pilar; Buthe, Andreas; Ansorge‐Schumacher, Marion B.; Sinisterra, J. V.; Alcántara, Andrés R.

doi:10.1016/j.molcatb.2007.10.009

Cited by 40 publications

(28 citation statements)

References 43 publications

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“…It yielded an enantiomeric excess of > 99% of (R)-a-methylbenzyl butyrate (2) at full conversion (50%) and thus exhibited no difference to the native NZ435. Combined with the findings of Hoyos et al [27] who entrapped Lipase TL (Meito Sangyo, Japan) in pure silicone without affecting the stereoselectivity, this provides a strong hint that composite particles obtained from silicone have no influence on the given stereoselectivity of an enzyme catalyst and can therefore also be effectively applied to the synthesis of chiral compounds.…”

Section: Stereoselective Synthesis and Transferabilitymentioning

confidence: 59%

Enabling Industrial Biocatalytic Processes by Application of Silicone‐Coated Enzyme Preparations

et al. 2011

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Composite particles of the commercial lipase preparation NZ435 and silicone (silcoat-NZ435) have recently been described as promising biocatalysts for synthetic use. In this study, their actual potential for enhanced performance in industrial applications was evaluated, focusing on scenarios where carrier disintegration and catalyst leaching constitute key limitations. All three investigated model reactions, the syntheses of myristyl myristate, poly(ethylene glycol) 400-coconut fatty acid monoester and ethylene oxide and propylene oxide co-A C H T U N G T R E N N U N G polymer (EO/PO)-oleic acid diester, were considerably improved in terms of the maximal number of reaction cycles performed with the same batch of catalyst, and consequently in terms of the obtainable product amount. The total turnover numbers (TTN) increased by a factor up to 50, making the realization of this type of reactions in an industrial process more feasible. The utility of silcoat-NZ435 for stereoselective transformations was demonstrated with the enantioselective acylation of 1-phenylethanol with vinyl butyrate, in which full retention of the excellent stereoselectivity of native NZ435 was observed. Moreover, it was demonstrated for the first time that the methodology by which silcoat-catalysts are obtained can be successfully transferred to alternative carriers and enzymes (e.g., protease, esterase and laccase), opening a broad field for the implementation and advancement of biocatalysis in industrial processes.

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Section: Stereoselective Synthesis and Transferabilitymentioning

confidence: 59%

Enabling Industrial Biocatalytic Processes by Application of Silicone‐Coated Enzyme Preparations

et al. 2011

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“…co.jp/meito/kaseihin/index e.html) has proven to be an attractive alternative for the recognition of alcohols possessing large groups at the asymmetric carbon atom, such as wood sterols [10], benzoins [11][12][13] and other bulky secondary alcohols [14][15][16]. On the other hand, this enzyme has been shown to be very active in hydrophobic solvents, such as toluene [15], or polar ones, such as acetone, 1,4-dioxane [16] or THF [11][12][13][14], also displaying an increase in activity and stability upon immobilization [17]. Furthermore, Lipase TL has proven to be also useful for N-acetylalanine deprotection [18], stereoselective acylation of 2-chloro-1-(2,4-difluorophenyl)ethanol [19] or aminolysis reactions [20] in 2-methyltetrahydrofuran (2-MeTHF), a greener substitute for THF displaying very interesting properties.…”

Section: Introductionmentioning

confidence: 99%

Lipase from Pseudomonas stutzeri: Purification, homology modelling and rational explanation of the substrate binding mode

Maraite

Hoyos²,

Carballeira³

et al. 2013

Journal of Molecular Catalysis B: Enzymatic

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“…Nevertheless, a systematic study on lipase-promoted transacylation (five different wild-type lipases were screened) concluded that Pseudomonas aeruginosa lipase is active and R selective toward bulky phenylalkanols. [6] Pseudomonas stutzeri lipase-catalyzed dynamic kinetic resolution (DKR) of 1,2-diarylethanols [7] and benzoins [8][9] (1,2-diaryl-2-hydroxyethanone structures) have been recently reported. In addition, substrates that have very bulky side groups flanking the carbonyl, such as phenyl isopropyl ketone, tend to be poor substrates for most known alcohol dehydrogenases.…”

Section: Introductionmentioning

confidence: 99%

Mutant Lipase‐Catalyzed Kinetic Resolution of Bulky Phenyl Alkyl sec‐Alcohols: A Thermodynamic Analysis of Enantioselectivity

2010

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The size of the stereoselectivity pocket of Candida antarctica lipase B limits the range of alcohols that can be resolved with this enzyme. These steric constrains have been changed by increasing the size of the pocket by the mutation W104A. The mutated enzyme has good activity and enantioselectivity toward bulky secondary alcohols, such as 1-phenylalkanols, with alkyl chains up to eight carbon atoms. The S enantiomer was preferred in contrast to the wild-type enzyme, which has R selectivity. The magnitude of the enantioselectivity changes in an interesting way with the chain length of the alkyl moiety. It is governed by interplay between entropic and enthalpic contributions and substrates with long alkyl chains are resolved best with E values higher than 100. The enantioselectivity increases with temperature for the small substrates, but decreases for the long ones.

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Highly efficient one pot dynamic kinetic resolution of benzoins with entrapped Pseudomonas stutzeri lipase

Cited by 40 publications

References 43 publications

Enabling Industrial Biocatalytic Processes by Application of Silicone‐Coated Enzyme Preparations

Enabling Industrial Biocatalytic Processes by Application of Silicone‐Coated Enzyme Preparations

Lipase from Pseudomonas stutzeri: Purification, homology modelling and rational explanation of the substrate binding mode

Mutant Lipase‐Catalyzed Kinetic Resolution of Bulky Phenyl Alkyl sec‐Alcohols: A Thermodynamic Analysis of Enantioselectivity

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