Natural prostaglandins (PG) F2alpha and E1 as well as (+)-cloprostenol were regioselectively 11-acylated using Novozym 435 as a catalyst and vinyl acetate as an acyl donor. Unlike the above compounds the 15-OH group of PGE2 was also acylated with a significant velocity under the same conditions. The enantiospecificity of the lipase-catalysed 11-acetylation of cloprostenol was established by separate treatment of(+)- and (-)-cloprostenols.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/s0960-894x(99)00295-4 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Lipase-Catalysed Enzymatic Kinetic Resolution of Aromatic Morita-Baylis-Hillman Derivatives by Hydrolysis and Transesterification.
Chembiochem
November 2022
Molecular Sciences Institute School of Chemistry, University of the Witwatersrand Private Bag X3, PO WITS, Johannesburg, 2050, South Africa.
Acylated Morita-Baylis-Hillman (MBH) adducts were synthesised and subjected to enzymatic kinetic resolution (EKR) by hydrolysis employing various lipase enzymes: from P. fluorescens, P. cepacia (PCL), C.
View Article and Find Full Text PDFLipase-catalysed synthesis of mono- and di-acyl esters of glyceryl caffeate in propylene carbonate and their antioxidant properties in tuna oil.
J Biotechnol
January 2021
The New Zealand Institute for Plant and Food Research Limited, 293 Akersten St, Port Nelson, Nelson 7010, New Zealand. Electronic address:
Development of new non-toxic antioxidants with diverse hydrophobic properties is important due to growing concerns about the toxicity of artificial oil-soluble antioxidants, the comparatively low effectiveness of natural options, and the complex role hydrophobicity plays in antioxidant effectiveness. Using caffeic acid, a naturally occurring phenolic acid with potent antioxidant activity, a range of glyceryl caffeate esters (decanoate and palmitate) were prepared using lipase-catalysed esterification reactions. Glyceryl-1-caffeate (GC) was prepared from ethyl caffeate and glycerol (acting as both the solvent and the substrate), catalysed by immobilised Candida Antarctica lipase B (Novozym-435) at 80 °C under vacuum.
View Article and Find Full Text PDFChiral β-lactam-based integrin ligands through Lipase-catalysed kinetic resolution and their enantioselective receptor response.
Bioorg Chem
July 2019
Department of Chemistry "G. Ciamician", University of Bologna, Via Selmi 2, 40126 Bologna, Italy. Electronic address:
Obtainment and testing of pure enantiomers are of great importance for bioactive compounds, because of the assessed implications of enantioselectivity in receptor-mediated responses. Herein we evaluated the use of biocatalysis to obtain enantiomerically pure β-lactam intermediates further exploited in the synthesis of novel integrin ligands as single enantiomers. From a preliminary screening on a set of commercially available hydrolases, Burkholderia Cepacia Lipase (BCL) emerged as a suitable and highly performing enzyme for the kinetic resolution of a racemic azetidinone, key intermediate for the synthesis of novel agonists of integrins.
View Article and Find Full Text PDFLipase Catalysed Kinetic Resolution of Racemic 1,2-Diols Containing a Chiral Quaternary Center.
Molecules
June 2018
Departamento de Química Orgánica, Universidad de Sevilla, c/Profesor García González 1, 41012 Sevilla, Spain.
Optically active 1,2-diols are valuable buildings blocks in organic synthesis. In the present paper, a set of racemic 1,2-diols with an ester functional group are prepared, starting from α-ketoesters in a three-step procedure with moderate yields. The racemic 1,2-diols, containing a chiral quaternary center in their structure, are subjected to selective acylation in order to perform their kinetic resolution catalysed by a set of commercially available lipases.
View Article and Find Full Text PDFWe here describe a study of the enzyme-mediated acylation reaction of 6,7-dihydroxy-linalool stereoisomers, which are natural triols occurring in different vegetal species. We found that only few lipases are able to catalyze the acylation of the secondary hydroxy group present in these isomers and only lipase from Candida rugosa and novozyme 435 provide either (3R,6R)-6-acetoxy-7-hydroxylinalool or (3R,6S)-6-acetoxy-7-hydroxylinalool in moderate and very good isomeric purity, respectively. Even for these favorable cases the reaction proceeds very sluggishly.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!