Kinetic resolution of drug intermediates catalyzed by lipase B fromCandida antarcticaimmobilized on immobead-350

2018 ◽  
Vol 34 (4) ◽  
pp. 878-889 ◽  
Author(s):  
Maísa Pessoa Pinheiro ◽  
Nathalia Saraiva Rios ◽  
Thiago de S. Fonseca ◽  
Francisco de Aquino Bezerra ◽  
Enrique Rodríguez-Castellón ◽  
...  
Keyword(s):  
Kinetic Resolution ◽  
Lipase B ◽  
Drug Intermediates

Kinetic Resolution of 1-Biaryl- and 1-(Pyridylphenyl)alkan-1-ols Catalysed by the Lipase B fromCandida antarctica

2005 ◽  
Vol 347 (5) ◽  
pp. 695-702 ◽  
Author(s):  
Robert Kourist ◽  
Javier González-Sabín ◽  
Ramón Liz ◽  
Francisca Rebolledo
Keyword(s):  
Kinetic Resolution ◽  
Lipase B

scholarly journals Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols

Molecules ◽  
2020 ◽  
Vol 25 (2) ◽  
pp. 350 ◽  
Author(s):  
Cristina Georgiana Spelmezan ◽  
László Csaba Bencze ◽  
Gabriel Katona ◽  
Florin Dan Irimie ◽  
Csaba Paizs ◽  
...  
Keyword(s):  
Magnetic Nanoparticles ◽  
Vinyl Acetate ◽  
Kinetic Resolution ◽  
Covalent Binding ◽  
Enantiomeric Excess ◽  
Candida Antarctica ◽  
Optimal Conditions ◽  
Lipase B ◽  
Magnetic Chitosan ◽  
Enzymatic Kinetic Resolution

Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2–50% conversion in 3–16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols through transesterification with vinyl acetate. Under optimal conditions (vinyl acetate, n-hexane, 45 °C), the biocatalyst remains active after 10 cycles.

Screening, isolation and selection of a potent lipase producing microorganism and its use in the kinetic resolution of drug intermediates

2021 ◽  
pp. 100143
Author(s):  
Linga Banoth ◽  
Kezia Devarapalli ◽  
Indrani Paul ◽  
Karuna Narayan Thete ◽  
Sandip V. Pawar ◽  
...  
Keyword(s):  
Kinetic Resolution ◽  
Selection Of ◽  
Drug Intermediates

scholarly journals Quarter of a Century after: A Glimpse at the Conformation and Mechanism of Candida antarctica Lipase B

Crystals ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 404
Author(s):  
Jarosław Błaszczyk ◽  
Piotr Kiełbasiński
Keyword(s):  
Kinetic Resolution ◽  
Stereoselective Synthesis ◽  
Candida Antarctica ◽  
Enzyme Mechanism ◽  
Three Dimensions ◽  
Candida Antarctica Lipase ◽  
Lipase B ◽  
Long Period ◽  
Lack Of Information ◽  
The Family

Lipase B from Candida antarctica (CAL-B) belongs to the family of α/β-hydrolases, and is one from the most extensively used biocatalysts in the kinetic resolution of amines and alcohols in a racemic state, in the desymmetrization of diacetates or diols, and in the stereoselective synthesis of chiral intermediate compounds for obtaining the various pharmaceuticals and agents which protect plants. There are also many cases of promiscuous reactions catalyzed by CAL-B. The number of very important results appeared recently in the literature in the years 2015–2019, regarding the crystal structure and conformation of CAL-B molecule. Before 2015, there was a long period of a complete lack of information concerning this enzyme’s structure. The earlier reports about CAL-B structure were dated between 1994–1995, and did not provide enough conclusions about the mechanism of the enzyme. The recently solved structures give a hint of the enzyme mechanism in three dimensions.

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