Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate

2020 ◽  
Vol 43 (12) ◽  
pp. 2253-2268 ◽  
Author(s):  
Ticiane C. de Souza ◽  
Thiago de Sousa Fonseca ◽  
Jouciane de Sousa Silva ◽  
Paula J. M. Lima ◽  
Carlos A. C. G. Neto ◽  
...  
Molecules ◽  
2020 ◽  
Vol 25 (2) ◽  
pp. 350 ◽  
Author(s):  
Cristina Georgiana Spelmezan ◽  
László Csaba Bencze ◽  
Gabriel Katona ◽  
Florin Dan Irimie ◽  
Csaba Paizs ◽  
...  

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.


2015 ◽  
Vol 5 (6) ◽  
pp. 3130-3136 ◽  
Author(s):  
Stefânia P. de Souza ◽  
Jonathan Bassut ◽  
Heiddy V. Marquez ◽  
Ivaldo I. Junior ◽  
Leandro S. M. Miranda ◽  
...  

Aminoalkyl functionalised sporopollenin exine capsules have been used to immobilizeCandida antarcticalipase B using a covalent diimine-based linker.


Crystals ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 404
Author(s):  
Jarosław Błaszczyk ◽  
Piotr Kiełbasiński

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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