Substrate sorption into the polymer matrix of Novozym 435® and its effect on the enantiomeric ratio determination

Heinsman, N.W.J.T.; Schroën, Carin G.P.H.; Padt, A. van der; Franssen, M.C.R.; Boom, R.M.; Riet, Klaas van’t

doi:10.1016/s0957-4166(03)00577-9

Cited by 31 publications

(14 citation statements)

References 27 publications

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“…[d] CAL-B replaced with lipase PS preparation (30 mg/mL ). [26] allowing the attached water to be released into organic solvents. S-Selective hydrolysis was seen clearly when rac-1 was subjected to the enzymatic reaction conditions in the absence of an added competitive nucleophile (entries 1 and 2).…”

Section: Enantioselective Cleavage Of the B-lactam Ring By Lipase Catmentioning

confidence: 99%

Lipase‐Involved Strategy to the Enantiomers of 4‐Benzyl‐β‐Lactam as a Key Intermediate in the Preparation of β‐Phenylalanine Derivatives

Li¹,

Kanerva²

2006

Adv Synth Catal

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A simple chemoenzymatic method for the preparation of the enantiomers of 4-benzyl-b-lactam (4-benzylazetidin-2-one) from allylbenzene has been described. The enantiomers of this key intermediate have been used to produce the corresponding enantiomers of b-phenylalanine and N-Boc-protected bphenylalanine amide through the simple cleavage of the lactam ring by acid-catalyzed hydrolysis and by ammonolysis, respectively. Burkholderia cepacia lipase-catalyzed kinetic double resolution techniques were responsible for achieving enantiopurity in the products. This was performed through the acylation of N-hydroxymethylated b-lactam followed by the butanolysis of the obtained (S)-ester. Direct lipase-catalyzed cleavage of the b-lactam ring has also been studied.

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Section: Enantioselective Cleavage Of the B-lactam Ring By Lipase Catmentioning

confidence: 99%

Lipase‐Involved Strategy to the Enantiomers of 4‐Benzyl‐β‐Lactam as a Key Intermediate in the Preparation of β‐Phenylalanine Derivatives

Li¹,

Kanerva²

2006

Adv Synth Catal

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“…[27] In comparison, Novozyme 435 is adsorbed on a divinylbenzene-cross-linked, hydrophobic macroporous polymer based on methyl and butyl methacrylic esters. [29] This lipophilic material will readily release any water that is attached to it into the dry reaction mixture, thereby enabling the hydrolysis of both the product and the acyl donor. Not all types of Celite are suitable for enzyme immobilisations and care has been taken to choose a suitable one.…”

Section: Full Papersmentioning

confidence: 99%

Optimisation of the Enantioselective Synthesis of Cyanohydrin Esters

et al. 2005

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Abstract:The base-and lipase-catalysed enantioselective synthesis of cyanohydrin esters was investigated, and the problem of previously reported low yields due to residual water in the reaction mixture was addressed. When the lipase was immobilised on Celite R-633 as a carrier, both the enantioselectivity and the reaction times for this dynamic kinetic resolution were improved, thus enabling a highly enantioselective synthesis of aromatic and heteroaromatic cyanohydrin acetates.

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“…This lipophilic support material will readily release any water present into the anhydrous reaction mixture. [12] Moreover, a water tunnel allowing direct access of water from the medium to the active site was previously shown to exist in CAL-B. [13] Together, these factors expose the active site to residual water that can lead to acyl-enzyme intermediate hydrolysis in addition to the desired lysis with another nucleophile.…”

Section: Enzymatic Kinetic Resolution Of Amino Estersmentioning

confidence: 99%

Candida antarctica Lipase B in a Chemoenzymatic Route to Cyclic α‐Quaternary α‐Amino Acid Enantiomers

Li¹,

Rantapaju²,

Kanerva³

2011

Eur J Org Chem

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Kinetic resolution of three cyclic quaternary ethyl 1‐amino‐2,3‐dihydro‐1H‐indene‐1‐carboxylates and both 1‐ and 2‐amino‐1,2,3,4‐tetrahydronaphthalene analogues have been studied. Interesterification with butyl butanoate and Candida antarctica lipase B accomplished the task. The enantiomers of all 1‐amino analogues reacted with excellent enantioselectivity (enantiomeric ratio er greater than 200), whereas the 2‐amino analogue was not enantioselective (er = 4). Amino acid enantiomers were finally obtained as their respective hydrochlorides with almost maximum theoretical yields. For the first time, a lipase enzyme was effectively used in the kinetic resolution of cyclic α‐quaternary α‐amino esters.

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Substrate sorption into the polymer matrix of Novozym 435® and its effect on the enantiomeric ratio determination

Cited by 31 publications

References 27 publications

Lipase‐Involved Strategy to the Enantiomers of 4‐Benzyl‐β‐Lactam as a Key Intermediate in the Preparation of β‐Phenylalanine Derivatives

Lipase‐Involved Strategy to the Enantiomers of 4‐Benzyl‐β‐Lactam as a Key Intermediate in the Preparation of β‐Phenylalanine Derivatives

Optimisation of the Enantioselective Synthesis of Cyanohydrin Esters

Candida antarctica Lipase B in a Chemoenzymatic Route to Cyclic α‐Quaternary α‐Amino Acid Enantiomers

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